|
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: 1037.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGETLQANHIRDTER 80
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKHLTVLENIFLGAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 161 VRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDIITMMVG 240
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 241 RELTALYPSEPHAHGEEILRVEHLTAWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRWQGEIF 320
Cdd:PRK13549 242 RELTALYPREPHTIGEVILEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 321 IDGQPVSISNCQQAIAHGIAMVPEDRKKDGIVPVMAVGKNITLAALNQFTGaMSSLDDAAEQHCIQQSIQRLKIKTSSPE 400
Cdd:PRK13549 322 IDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTG-GSRIDDAAELKTILESIQRLKVKTASPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 401 LAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHE 480
Cdd:PRK13549 401 LAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHE 480
|
490 500
....*....|....*....|....*.
gi 489011807 481 GRLKANLVNQHLTQEQVMEAALRSER 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: 868.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGETLQANHIRDTERKGI 83
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLGAEISRHG-LLDYETMTLRCQKLLAQVNLPISPDTR-VGDLGLGQQQLVEIAKALNKQV 161
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGgRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 162 RLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDIITMMVGR 241
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 242 ELTALYPSEPHAHGEEILRVEHLTAWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRWQGEIFI 321
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 322 DGQPVSISNCQQAIAHGIAMVPEDRKKDGIVPVMAVGKNITLAALNQFTGaMSSLDDAAEQHCIQQSIQRLKIKTSSPEL 401
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCF-KMRIDAAAELQIIGSAIQRLKVKTASPFL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 402 AIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
490 500
....*....|....*....|.
gi 489011807 482 RLKANLVNQHLTQEQVMEAAL 502
Cdd:TIGR02633 480 KLKGDFVNHALTQEQVLAAAL 500
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-508 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 761.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTERKGI 83
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDS--GEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLGAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 164 LILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDIITMMVGREL 243
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGREL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 244 TALYPSEPHAHGEEILRVEHLTAWhpvnrhiKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDG 323
Cdd:COG1129 242 EDLFPKRAAAPGEVVLEVEGLSVG-------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP-ADSGEIRLDG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 324 QPVSISNCQQAIAHGIAMVPEDRKKDGIVPVMAVGKNITLAALNQFTGAMsSLDDAAEQHCIQQSIQRLKIKTSSPELAI 403
Cdd:COG1129 314 KPVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGG-LLDRRRERALAEEYIKRLRIKTPSPEQPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 404 GRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
490 500
....*....|....*....|....*
gi 489011807 484 KANLVNQHLTQEQVMEAALRSERHV 508
Cdd:COG1129 473 VGELDREEATEEAIMAAATGGAAAA 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: 659.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGETLQANHIRDTERKGI 83
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLGAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 164 LILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASG--MSEDDIITMMVGR 241
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRAdeVTEDRIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 242 ELTALYPSEPHAHGEEILRVEHLTAWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRWQGEIF 320
Cdd:NF040905 241 DLEDRYPERTPKIGEVVFEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYGRNISGTVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 321 IDGQPVSISNCQQAIAHGIAMVPEDRKKDGIVPVMAVGKNITLAALnqftGAMSS---LDDAAEQHCIQQSIQRLKIKTS 397
Cdd:NF040905 321 KDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANL----GKVSRrgvIDENEEIKVAEEYRKKMNIKTP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 398 SPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLV 477
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYV 476
|
490 500
....*....|....*....|...
gi 489011807 478 MHEGRLKANLVNQHLTQEQVMEA 500
Cdd:NF040905 477 MNEGRITGELPREEASQERIMRL 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: 559.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTER 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDA--GSILYLGKEVTFNGPKSSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKHLTVLENIFLGAEI-SRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:PRK10762 79 AGIGIIHQELNLIPQLTIAENIFLGREFvNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 160 QVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDIITMMV 239
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 240 GRELTALYPSEPHAHGEEILRVEHLTAwhpvnrhiKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEI 319
Cdd:PRK10762 239 GRKLEDQYPRLDKAPGEVRLKVDNLSG--------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP-RTSGYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 320 FIDGQPVSISNCQQAIAHGIAMVPEDRKKDGIVPVMAVGKNITLAALNQFTGAMSSLDDAAEQHCIQQSIQRLKIKTSSP 399
Cdd:PRK10762 310 TLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 400 ELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMH 479
Cdd:PRK10762 390 EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMH 469
|
490 500
....*....|....*....|...
gi 489011807 480 EGRLKANLVNQHLTQEQVMEAAL 502
Cdd:PRK10762 470 EGRISGEFTREQATQEKLMAAAV 492
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-502 |
1.33e-179 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 513.69 E-value: 1.33e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTER 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA--GSILIDGQEMRFASTTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKHLTVLENIFLGAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK11288 79 AGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 161 VRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGT-RDASGMSEDDIITMMV 239
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRDQLVQAMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 240 GRELTALYPSEPHAHGEEILRVEHLTAwhpvnrhIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEI 319
Cdd:PRK11288 239 GREIGDIYGYRPRPLGEVRLRLDGLKG-------PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATR-RTAGQV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 320 FIDGQPVSISNCQQAIAHGIAMVPEDRKKDGIVPVMAVGKNITLAALNQFTGAMSSLDDAAEQHCIQQSIQRLKIKTSSP 399
Cdd:PRK11288 311 YLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 400 ELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMH 479
Cdd:PRK11288 391 EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMR 470
|
490 500
....*....|....*....|...
gi 489011807 480 EGRLKANLVNQHLTQEQVMEAAL 502
Cdd:PRK11288 471 EGRIAGELAREQATERQALSLAL 493
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-497 |
7.48e-179 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 511.88 E-value: 7.48e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAGETLQANHIRDTE 79
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqPD---SGEILIDGKPVRIRSPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALVKHLTVLENIFLGAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:COG3845 79 ALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 160 QVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDIITMMV 239
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 240 GRELTALYPSEPHAHGEEILRVEHLTAwhPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEI 319
Cdd:COG3845 239 GREVLLRVEKAPAEPGEVVLEVENLSV--RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP-PASGSI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 320 FIDGQPVSISNCQQAIAHGIAMVPEDRKKDGIVPVMAVGKNITLaaLNQFTGAMSS---LD-DAAEQHCiQQSIQRLKIK 395
Cdd:COG3845 316 RLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLIL--GRYRRPPFSRggfLDrKAIRAFA-EELIEEFDVR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 396 TSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRV 475
Cdd:COG3845 393 TPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRI 472
|
490 500
....*....|....*....|..
gi 489011807 476 LVMHEGRLKANLVNQHLTQEQV 497
Cdd:COG3845 473 AVMYEGRIVGEVPAAEATREEI 494
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-505 |
8.52e-156 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 453.47 E-value: 8.52e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTER 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTK--GTITINNINYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKHLTVLENIFLGAEISRH----GLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 157 LNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDIIT 236
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 237 MMVGRELTALYPSEPHAHG----EEILRVEHLTAwhpvnRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWP 312
Cdd:PRK09700 240 LMVGRELQNRFNAMKENVSnlahETVFEVRNVTS-----RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 313 gRWQGEIFIDGQPVSISNCQQAIAHGIAMVPEDRKKDGIVPVMAVGKNITLA---ALNQFTGAMSSLDDAAEQHCIQQSI 389
Cdd:PRK09700 315 -RAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrslKDGGYKGAMGLFHEVDEQRTAENQR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 390 QRLKIKTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVL 469
Cdd:PRK09700 394 ELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEII 473
|
490 500 510
....*....|....*....|....*....|....*..
gi 489011807 470 GLSDRVLVMHEGRLKANLVN-QHLTQEQVMEAALRSE 505
Cdd:PRK09700 474 TVCDRIAVFCEGRLTQILTNrDDMSEEEIMAWALPQE 510
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-501 |
8.10e-151 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 440.32 E-value: 8.10e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 7 MKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGsyEGEIIFAGETLQANHIRDTERKGIAII 86
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD--SGSILFQGKEIDFKSSKEALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 87 HQELALVKHLTVLENIFLGAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLIL 166
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 167 DEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDIITMMVGRELTAL 246
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 247 YPSEPHAHGEEILRVEHLTAWHPVNrhikrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPV 326
Cdd:PRK10982 239 FPDKENKPGEVILEVRNLTSLRQPS-----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-KSAGTITLHGKKI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 327 SISNCQQAIAHGIAMVPEDRKKDGIVPVMAVGKNITLAALNQFTGAMSSLDDAAEQHCIQQSIQRLKIKTSSPELAIGRL 406
Cdd:PRK10982 313 NNHNANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 407 SGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLkAN 486
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV-AG 471
|
490
....*....|....*.
gi 489011807 487 LVN-QHLTQEQVMEAA 501
Cdd:PRK10982 472 IVDtKTTTQNEILRLA 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-511 |
2.30e-117 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 355.13 E-value: 2.30e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTER 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS--GTLEIGGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKHLTVLENIFLGaeISRHGLlDYETMTlrcqKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK15439 86 LGIYLVPQEPLLFPNLSVKENILFG--LPKRQA-SMQKMK----QLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 161 VRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDIITMM-- 238
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAItp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 239 VGRELTA-----LYPSEP-----HAHGEEILRVEHLTAwhpvnrhiKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLF 308
Cdd:PRK15439 239 AAREKSLsasqkLWLELPgnrrqQAAGAPVLTVEDLTG--------EGFRNISLEVRAGEILGLAGVVGAGRTELAETLY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 309 GVWPGRwQGEIFIDGQPVSISNCQQAIAHGIAMVPEDRKKDGIVPVMAVGKNITLAALNQFTgamSSLDDAAEQHCIQQS 388
Cdd:PRK15439 311 GLRPAR-GGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVCALTHNRRG---FWIKPARENAVLERY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 389 IQRLKIKTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEV 468
Cdd:PRK15439 387 RRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEI 466
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489011807 469 LGLSDRVLVMHEGRLKANLVNQHLTQEQVMEAALRSERHVEEH 511
Cdd:PRK15439 467 EQMADRVLVMHQGEISGALTGAAINVDTIMRLAFGEHQAQEAS 509
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
255-483 |
4.98e-88 |
|
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: 268.15 E-value: 4.98e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 255 GEEILRVEHLTAWhpvnrhiKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPVSISNCQQA 334
Cdd:cd03215 1 GEPVLEVRGLSVK-------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-PASGEITLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 335 IAHGIAMVPEDRKKDGIVPVMAVGKNITLAALnqftgamsslddaaeqhciqqsiqrlkiktsspelaigrLSGGNQQKA 414
Cdd:cd03215 73 IRAGIAYVPEDRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKV 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 415 ILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-483 |
2.54e-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: 243.66 E-value: 2.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTF--GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPH-GSYEGEIIFAGETLQANHIRD 77
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHgGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 TERKgIAIIHQE--LALVKhLTVLENIflgAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAK 155
Cdd:COG1123 81 RGRR-IGMVFQDpmTQLNP-VTVGDQI---AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 156 ALNKQVRLLILDEPTASLTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDI 234
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 235 ITMMVGRELTALYPSEPHAH-GEEILRVEHLTAWHPVNR--HIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW 311
Cdd:COG1123 236 ALAAVPRLGAARGRAAPAAAaAEPLLEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 312 PgRWQGEIFIDGQPVSISNCQQ--AIAHGIAMV---PEdrkkDGIVPVMAVGKNITLAALNQFTgamssLDDAAEQHCIQ 386
Cdd:COG1123 316 R-PTSGSILFDGKDLTKLSRRSlrELRRRVQMVfqdPY----SSLNPRMTVGDIIAEPLRLHGL-----LSRAERRERVA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 387 QSIQRLKIktsSPELA---IGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVIS 462
Cdd:COG1123 386 ELLERVGL---PPDLAdryPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFIS 462
|
490 500
....*....|....*....|.
gi 489011807 463 SELPEVLGLSDRVLVMHEGRL 483
Cdd:COG1123 463 HDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-223 |
4.81e-66 |
|
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: 210.75 E-value: 4.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTERKGIA 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS--GEILVDGKEVSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQelalvkhltvleniflgaeisrhglldyetmtlrcqkllaqvnlpispdtrvgdLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGT 223
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-482 |
4.28e-52 |
|
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: 184.89 E-value: 4.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGA----VKAVDNVSLRLNAGEVVSLCGENGSGKS----TLMKVLCgiYPHGSYEGEIIFAGETL-- 70
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLP--DPAAHPSGSILFDGQDLlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 71 ----QANHIRDTErkgIAIIHQE--LALVKHLTVLENIflgAE-ISRHGLLDYETMTLRCQKLLAQVNLPiSPDTRVGD- 142
Cdd:COG4172 81 lserELRRIRGNR---IAMIFQEpmTSLNPLHTIGKQI---AEvLRLHRGLSGAAARARALELLERVGIP-DPERRLDAy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 143 ---LGLGQQQLVEIAKALNKQVRLLILDEPTASL--TEQetATLLAIVRDLQN-HDIACIYISHKLNEVKAISDTICVIR 216
Cdd:COG4172 154 phqLSGGQRQRVMIAMALANEPDLLIADEPTTALdvTVQ--AQILDLLKDLQReLGMALLLITHDLGVVRRFADRVAVMR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 217 DG---------------QHIGTRdasgmseddiitmmvgreltALYPSEPH-------AHGEEILRVEHLTAWHPVNR-- 272
Cdd:COG4172 232 QGeiveqgptaelfaapQHPYTR--------------------KLLAAEPRgdprpvpPDAPPLLEARDLKVWFPIKRgl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 273 ------HIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGrwQGEIFIDGQPVSISNcqqaiahGIAMVPEdR 346
Cdd:COG4172 292 frrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS--EGEIRFDGQDLDGLS-------RRALRPL-R 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 347 KKDGIV---------PVMAVGKNIT--LAALNqftgamSSLDDAAEQHCIQQSIQRLKIktsSPElAIGR----LSGGNQ 411
Cdd:COG4172 362 RRMQVVfqdpfgslsPRMTVGQIIAegLRVHG------PGLSAAERRARVAEALEEVGL---DPA-ARHRypheFSGGQR 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 412 QK-AIlARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:COG4172 432 QRiAI-ARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-232 |
1.56e-48 |
|
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: 167.23 E-value: 1.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGE---TLQANHIRdteRK 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTS--GSVLFDGEditGLPPHEIA---RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 82 GIAIIHQELALVKHLTVLENIFLGAEISRHGLL-------DYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIA 154
Cdd:cd03219 76 GIGRTFQIPRLFPELTVLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 155 KALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIgtrdASGMSED 232
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI----AEGTPDE 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-221 |
2.12e-48 |
|
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: 167.52 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTER 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYR--PTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKHLTVLENIFLGAEI-SRHGLLDYETMTLRCQK-----------LLAQVNLPISPDTRVGDLGLGQQ 148
Cdd:COG0411 79 LGIARTFQNPRLFPELTVLENVLVAAHArLGRGLLAALLRLPRARReereareraeeLLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 149 QLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-243 |
2.43e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.38 E-value: 2.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTERkgIA 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR--PTSGEVRVLGEDVARDPAEVRRR--IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAEIsrHGlLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARL--YG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSE---DDIITMMVGR 241
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKArllEDVFLELTGE 233
|
..
gi 489011807 242 EL 243
Cdd:COG1131 234 EA 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-219 |
1.79e-42 |
|
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: 151.55 E-value: 1.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQanHIRDTERKGI 83
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS--GSILIDGEDVR--KEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLGAEIsrHGLLDYETmTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAEL--YGLFDEEL-KKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 164 LILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 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 |
2.04e-40 |
|
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: 144.94 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGA----VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLqaNHIRDTE- 79
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVRVDGTDI--SKLSEKEl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 ----RKGIAIIHQELALVKHLTVLENIFLGAEISRHGLLDYEtmtLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAK 155
Cdd:cd03255 77 aafrRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERR---ERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 156 ALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKlNEVKAISDTICVIRDGQ 219
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-481 |
5.40e-40 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 151.78 E-value: 5.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF---GAVK-AVDNVSLRLNAGEVVSLCGENGSGKS----TLMKVLCG---IYPHGsyegEIIFAGETL-- 70
Cdd:PRK15134 5 LLAIENLSVAFrqqQTVRtVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYPSG----DIRFHGESLlh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 71 -QANHIRDTERKGIAIIHQElALVKhLTVLENI--FLGAEISRHGLLDYE---TMTLRCqklLAQVNLPiSPDTRVGD-- 142
Cdd:PRK15134 81 aSEQTLRGVRGNKIAMIFQE-PMVS-LNPLHTLekQLYEVLSLHRGMRREaarGEILNC---LDRVGIR-QAAKRLTDyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 143 --LGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK15134 155 hqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 220 HIGTRDAsgmseDDIITMMVGRELTALYPSEPH-------AHGEEILRVEHLTAWHPVNRHIKR--------VNDVSFSL 284
Cdd:PRK15134 235 CVEQNRA-----ATLFSAPTHPYTQKLLNSEPSgdpvplpEPASPLLDVEQLQVAFPIRKGILKrtvdhnvvVKNISFTL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 285 RRGEILGIAGLVGAGRTEAVQCLFGVWPGrwQGEIFIDGQPVSISNCQQ--AIAHGIAMVPED-----RKKDGIVPVMAV 357
Cdd:PRK15134 310 RPGETLGLVGESGSGKSTTGLALLRLINS--QGEIWFDGQPLHNLNRRQllPVRHRIQVVFQDpnsslNPRLNVLQIIEE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 358 GKNITLAALNqftgamsslddAAEQHciQQSIQRLKIKTSSPELAI---GRLSGGNQQKAILARCLLLNPRILILDEPTR 434
Cdd:PRK15134 388 GLRVHQPTLS-----------AAQRE--QQVIAVMEEVGLDPETRHrypAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489011807 435 GIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-219 |
6.08e-40 |
|
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: 143.81 E-value: 6.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQAnhiRDTERKGIA 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDS--GEILIDGRDVTG---VPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAeisRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGL---KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQrELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-219 |
4.97e-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: 137.14 E-value: 4.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDteRKGIA 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK--PDSGEIKVLGKDIKKEPEEV--KRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIflgaeisrhglldyetmtlrcqkllaqvnlpispdtrvgDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03230 77 YLPEEPSLYENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-219 |
1.58e-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: 137.21 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 6 EMKNITKTF--GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGETLQANHIRDTeRKGI 83
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSLKEL-RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQ--ELALVKHlTVLENIFLGAEisrHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:cd03225 78 GLVFQnpDDQFFGP-TVEEEVAFGLE---NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 162 RLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-171 |
1.75e-37 |
|
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: 135.08 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 20 VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTeRKGIAIIHQELALVKHLTVL 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS--PTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 100 ENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPTA 171
Cdd:pfam00005 78 ENLRLGLLLKG---LSKREKDARAEEALEKLGLGDLADRPVGERPGtlsgGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-219 |
2.49e-36 |
|
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: 135.00 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGA-VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGE---TLQANHIRDTeR 80
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL--VEPTSGSVLIDGTdinKLKGKALRQL-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKHLTVLENIFLGAeISRHGLLD------YETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIA 154
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVLSGR-LGRRSTWRslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 155 KALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-219 |
4.24e-36 |
|
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: 133.79 E-value: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF----GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQAN--HIRD 77
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTS--GSIIFDGKDLLKLsrRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 TERKGIAIIHQE--LALVKHLTVLENIflgAEISRH--GLLDYETMTLRCQKLLAQVNLPIS-PDTRVGDLGLGQQQLVE 152
Cdd:cd03257 79 IRRKEIQMVFQDpmSSLNPRMTIGEQI---AEPLRIhgKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 153 IAKALNKQVRLLILDEPTASL--TEQetATLLAIVRDLQN-HDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03257 156 IARALALNPKLLIADEPTSALdvSVQ--AQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-219 |
8.49e-36 |
|
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: 131.16 E-value: 8.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQA-NHIRDTERKGI 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE--PDSGSILIDGEDLTDlEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLGaeisrhglldyetmtlrcqkllaqvnlpispdtrvgdLGLGQQQLVEIAKALNKQVRL 163
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 164 LILDEPTASLTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-219 |
9.49e-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: 132.84 E-value: 9.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTF-GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGETLQANHIRDTeRKGI 83
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP--TSGEVLVDGKDITKKNLREL-RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQ--ELALVKhLTVLENIFLGAEisRHGlLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:COG1122 78 GLVFQnpDDQLFA-PTVEEDVAFGPE--NLG-LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 162 RLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-253 |
1.50e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.87 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 3 WLLEMKNITKTF-GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTE-- 79
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE--PTSGEILVDGQDVTALRGRALRrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALVKHLTVLENIFLGAeISRHGLLD------YETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEI 153
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVLAGR-LGRTSTWRsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 154 AKALNKQVRLLILDEPTASL----TEQETATLLAIVRDlqnHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGM 229
Cdd:COG3638 158 ARALVQEPKLILADEPVASLdpktARQVMDLLRRIARE---DGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
250 260
....*....|....*....|....
gi 489011807 230 SEDdiitmmvgrELTALYPSEPHA 253
Cdd:COG3638 235 TDA---------VLREIYGGEAEE 249
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-219 |
2.10e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 131.70 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFG----AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGI-YPhgsYEGEIIFAGETLqaNHI 75
Cdd:COG1136 1 MSPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRP---TSGEVLIDGQDI--SSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 76 RDTE-----RKGIAIIHQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQL 150
Cdd:COG1136 76 SERElarlrRRHIGFVFQFFNLLPELTALENVALPLLLAG---VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 151 VEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLnEVKAISDTICVIRDGQ 219
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-223 |
5.45e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.07 E-value: 5.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLqaNHIRdTERKGI 83
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET--PDSGRILLDGRDV--TGLP-PEKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLG--------AEISRhglldyetmtlRCQKLLAQVNLPISPDTRVGDL-GlGQQQLVEIA 154
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGlrmrgvpkAEIRA-----------RVAELLELVGLEGLADRYPHQLsG-GQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 155 KALNKQVRLLILDEPTASL-------TEQEtatLLAIVRDLqnhDIACIYISHKLNEVKAISDTICVIRDG--QHIGT 223
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALdaklreeMREE---LRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGriEQVGT 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-214 |
8.77e-35 |
|
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: 132.87 E-value: 8.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF----GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSY-EGEIIFAGE---TLQANHI 75
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGItSGEILFDGEdllKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 76 RDTERKGIAIIHQE--LALVKHLTVLENIflgAE-ISRHGLLDYETMTLRCQKLLAQVNLPiSPDTRVGDL-----GlGQ 147
Cdd:COG0444 81 RKIRGREIQMIFQDpmTSLNPVMTVGDQI---AEpLRIHGGLSKAEARERAIELLERVGLP-DPERRLDRYphelsG-GM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 148 QQLVEIAKALNKQVRLLILDEPTASL--TEQetATLLAIVRDLQN-HDIACIYISHKLNEVKAISDTICV 214
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALdvTIQ--AQILNLLKDLQReLGLAILFITHDLGVVAEIADRVAV 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-219 |
1.25e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.17 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTeRKGIA 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP--PTSGEIYLDGKPLSAMPPPEW-RRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHlTVLENIFLGAEIsRHGLLDYETMtlrcQKLLAQVNLPISP-DTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:COG4619 78 YVPQEPALWGG-TVRDNLPFPFQL-RERKFDRERA----LELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 164 LILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-483 |
1.64e-34 |
|
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: 136.09 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIF------------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 66 ----AGETLQ---------ANHIRDTERKGIAIIHQE-LALVKHLTVLENIFLG-AEISRHGlldyETMTLRCQKLLAQV 130
Cdd:TIGR03269 81 pcpvCGGTLEpeevdfwnlSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEAlEEIGYEG----KEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 131 NLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLtEQETATLL--AIVRDLQNHDIACIYISHKLNEVKAI 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTL-DPQTAKLVhnALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 209 SDTICVIRDGQHIgtrdASGMSEDDIITMMVGreLTALYPSEPHAHGEEILRVEHLTA-WHPVNRH-IKRVNDVSFSLRR 286
Cdd:TIGR03269 236 SDKAIWLENGEIK----EEGTPDEVVAVFMEG--VSEVEKECEVEVGEPIIKVRNVSKrYISVDRGvVKAVDNVSLEVKE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 287 GEILGIAGLVGAGRTEAVQCLFGVWP---GRWQ---GEIFIDGQPVSISNCQQAIAHgIAMVPEDRkkdGIVPVMAVGKN 360
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEptsGEVNvrvGDEWVDMTKPGPDGRGRAKRY-IGILHQEY---DLYPHRTVLDN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 361 ITLAAlnqftgamsSLDDAAEqHCIQQSIQRLKIKTSSPELAIG-------RLSGGNQQKAILARCLLLNPRILILDEPT 433
Cdd:TIGR03269 386 LTEAI---------GLELPDE-LARMKAVITLKMVGFDEEKAEEildkypdELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489011807 434 RGIDIGAKYEIYKLI-NQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:TIGR03269 456 GTMDPITKVDVTHSIlKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
277-499 |
1.68e-34 |
|
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: 129.98 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV-WPGRwqGEIFIDGQPVSISNcQQAIAHgIAMVPEDRkkdGIVPVM 355
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlKPDS--GSILIDGEDVRKEP-REARRQ-IGVLPDER---GLYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVGKNItlaalnQFTGAMSSLDDAAEQHCIQQSIQRLKIkTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:COG4555 90 TVRENI------RYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 436 IDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKANLVNQHLTQEQVME 499
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-253 |
4.81e-34 |
|
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: 128.77 E-value: 4.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGA----VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGETLQANHIRDTe 79
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP--WSGEVTFDGRPVTRRRRKAF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQ--ELALVKHLTVLENIFLGAEIsrHGLLDYETmtlRCQKLLAQVNLPIS-PDTRVGDLGLGQQQLVEIAKA 156
Cdd:COG1124 78 RRRVQMVFQdpYASLHPRHTVDRILAEPLRI--HGLPDREE---RIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 157 LNKQVRLLILDEPTASLTEQETATLLAIVRDLQN-HDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDdiI 235
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG--P 230
|
250
....*....|....*...
gi 489011807 236 TMMVGRELTALYPSEPHA 253
Cdd:COG1124 231 KHPYTRELLAASLAFERA 248
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-236 |
4.17e-33 |
|
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: 126.26 E-value: 4.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFG-AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGETLQANHIRD--TER 80
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL--VEPSSGSILLEGTDITKLRGKKlrKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKHLTVLENI---FLGAEISRHGLL------DYEtmtlRCQKLLAQVNLPISPDTRVGDLGLGQQQLV 151
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVlhgRLGYKPTWRSLLgrfseeDKE----RALSALERVGLADKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 152 EIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGqHIGTRDASGMS 230
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAG-EIVFDGAPSEL 233
|
....*.
gi 489011807 231 EDDIIT 236
Cdd:TIGR02315 234 DDEVLR 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-223 |
9.97e-33 |
|
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: 123.87 E-value: 9.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHiRDTERKGiA 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS--GEITFDGKSYQKNI-EALRRIG-A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIhQELALVKHLTVLENIFLGAEIsrHGLLDYetmtlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03268 77 LI-EAPGFYPNLTARENLRLLARL--LGIRKK-----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGT 223
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
259-482 |
1.22e-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: 124.08 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNrHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPVSISNCQQAIAHG 338
Cdd:cd03224 1 LEVENLNAGYGKS-QI--LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-PRSGSIRFDGRDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 339 IAMVPEDRkkdGIVPVMAVGKNITLAAlnqFTGAMSSLDDAAEQhcIQQSIQRLKIKTSSPElaiGRLSGGNQQKAILAR 418
Cdd:cd03224 77 IGYVPEGR---RIFPELTVEENLLLGA---YARRRAKRKARLER--VYELFPRLKERRKQLA---GTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 419 CLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
259-507 |
1.93e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 124.02 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTawhpvnrhiKR------VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSiSNCQ 332
Cdd:COG1131 1 IEVRGLT---------KRygdktaLDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT-SGEVRVLGEDVA-RDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 333 QAIAHgIAMVPEDrkkDGIVPVMAVGKNItlaalnQFTGAMSSLDDAAEQHCIQQSIQRLKIkTSSPELAIGRLSGGNQQ 412
Cdd:COG1131 70 EVRRR-IGYVPQE---PALYPDLTVRENL------RFFARLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 413 KAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKA-----NL 487
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAdgtpdEL 218
|
250 260
....*....|....*....|
gi 489011807 488 VNQHLtqEQVMEAALRSERH 507
Cdd:COG1131 219 KARLL--EDVFLELTGEEAR 236
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-200 |
3.86e-32 |
|
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: 122.20 E-value: 3.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANhiRDTERKGI 83
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP--PSAGEVLWNGEPIRDA--REDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENI-----FLGAEISRHGLLDyetmtlrcqkLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:COG4133 78 AYLGHADGLKPELTVRENLrfwaaLYGLRADREAIDE----------ALEAVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489011807 159 KQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISH 200
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-226 |
7.21e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 123.18 E-value: 7.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHGsyeGEIIFAGETLQANHIRDTERKG 82
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTG---GTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHLTVLENIFLGAEisRH-------GLL--------DYETMTlRCQKLLAQVNLPISPDTRVGDLGLGQ 147
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENLLVAQH--QQlktglfsGLLktpafrraESEALD-RAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 148 QQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQN-HDIACIYISHKLNEVKAISDTICVIRDGQHI--GTR 224
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNeHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLanGTP 238
|
..
gi 489011807 225 DA 226
Cdd:PRK11300 239 EE 240
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-219 |
1.81e-31 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 118.89 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 6 EMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRdTERKGIAI 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDGKDIAKLPLE-ELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 86 IHQelalvkhltvleniflgaeisrhglldyetmtlrcqkllaqvnlpispdtrvgdLGLGQQQLVEIAKALNKQVRLLI 165
Cdd:cd00267 78 VPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489011807 166 LDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-219 |
1.94e-31 |
|
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: 120.71 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIR-DTERKGI 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS--GTIIIDGLKLTDDKKNiNELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLgAEISRHGlLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITL-APIKVKG-MSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 164 LILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
258-483 |
2.44e-31 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 120.69 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTAWHPV-NRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPVSISN--CQQA 334
Cdd:cd03257 1 LLEVKNLSVSFPTgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-PTSGSIIFDGKDLLKLSrrLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 335 IAHGIAMVPED--RKKDgivPVMAVGKNITLAALNQFTgamsslDDAAEQhcIQQSIQRLKIKTSSPELAIGR----LSG 408
Cdd:cd03257 80 RRKEIQMVFQDpmSSLN---PRMTIGEQIAEPLRIHGK------LSKKEA--RKEAVLLLLVGVGLPEEVLNRypheLSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 409 GNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
271-478 |
4.19e-31 |
|
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: 119.56 E-value: 4.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 271 NRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNcqqaiaHGIAMVPEDRKKDG 350
Cdd:cd03235 11 GHPV--LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT-SGSIRVFGKPLEKER------KRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 351 IVPVMAvgKNITLAALNQFTGAMSSLDdAAEQHCIQQSIQRLKIKtsspELA---IGRLSGGNQQKAILARCLLLNPRIL 427
Cdd:cd03235 82 DFPISV--RDVVLMGLYGHKGLFRRLS-KADKAKVDEALERVGLS----ELAdrqIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489011807 428 ILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVM 478
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-219 |
4.23e-31 |
|
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: 119.69 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDterkgIA 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL--PDSGEVLFDGKPLDIAARNR-----IG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLEN-IFLGaeiSRHGLLDYETMTlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:cd03269 74 YLPEERGLYPKMKVIDQlVYLA---QLKGLKKEEARR-RIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 164 LILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-215 |
5.04e-31 |
|
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: 119.50 E-value: 5.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFG----AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQAnhirdtER 80
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTS--GEVLVDGEPVTG------PG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKHLTVLENIFLGAEIsrHGLLDYETMTlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLEL--QGVPKAEARE-RAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 161 VRLLILDEPTASLTEQeTATLL--AIVRDLQNHDIACIYISHKLNEVKAISDTICVI 215
Cdd:cd03293 150 PDVLLLDEPFSALDAL-TREQLqeELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
259-482 |
5.26e-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: 118.06 E-value: 5.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPvnrHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPgrWQGEIFIDGQPVsisncqqaiAH 337
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEP--DSGSILIDGEDL---------TD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 338 GIAMVPEDRKKDGIV-------PVMAVGKNITLAalnqftgamsslddaaeqhciqqsiqrlkiktsspelaigrLSGGN 410
Cdd:cd03229 67 LEDELPPLRRRIGMVfqdfalfPHLTVLENIALG-----------------------------------------LSGGQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 411 QQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:cd03229 106 QQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-223 |
9.37e-31 |
|
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: 119.26 E-value: 9.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGETLqaNHIrDTERKGIA 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF--ETPTSGEILLDGKDI--TNL-PPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKK---LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISDTICVIRDG--QHIGT 223
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQkELGITFVFVTHDQEEALTMSDRIAVMNKGkiQQIGT 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
9.62e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 9.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGETLQAnhirdtER 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP--TSGTVRLFGKPPRR------AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKH--LTVLENIFLGAeISRHGLL------DYEtmtlRCQKLLAQVNLpiSP--DTRVGDLGLGQQQL 150
Cdd:COG1121 75 RRIGYVPQRAEVDWDfpITVRDVVLMGR-YGRRGLFrrpsraDRE----AVDEALERVGL--EDlaDRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 151 VEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQH 220
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
256-511 |
1.84e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.65 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLTAW---HPVnrhikrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPVSISNcq 332
Cdd:COG1121 4 MPAIELENLTVSyggRPV------LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-PTSGTVRLFGKPPRRAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 333 qaiaHGIAMVPEDRKKDGIVP-----VMAVGKNITLAALNQFTgamsslddAAEQHCIQQSIQRLKIKtsspELA---IG 404
Cdd:COG1121 75 ----RRIGYVPQRAEVDWDFPitvrdVVLMGRYGRRGLFRRPS--------RADREAVDEALERVGLE----DLAdrpIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLK 484
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA 218
|
250 260
....*....|....*....|....*..
gi 489011807 485 ANLVNQHLTQEqVMEAALRSERHVEEH 511
Cdd:COG1121 219 HGPPEEVLTPE-NLSRAYGGPVALLAH 244
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-219 |
5.46e-30 |
|
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: 116.76 E-value: 5.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGE--TLQANHIRdtERKG 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP--PRSGSIRFDGRdiTGLPPHER--ARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHLTVLENIFLGAEISRHGLLDYEtmtlrcqklLAQVnLPISP------DTRVGDLGLGQQQLVEIAKA 156
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRRAKRKAR---------LERV-YELFPrlkerrKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 157 LNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-225 |
1.34e-29 |
|
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: 116.28 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGETLQANHIRDterKGIA 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL--ERPDSGTILFGGEDATDVPVQE---RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAEIS-RHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 164 LILDEPTASLTEQETATLLAIVRDLqnHD---IACIYISHKLNEVKAISDTICVIRDGQ--HIGTRD 225
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRL--HDelhVTTVFVTHDQEEALEVADRVVVMNKGRieQVGTPD 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
277-483 |
1.83e-29 |
|
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: 113.65 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPvsISNCQQAIAHGIAMVPEDrkkDGIVPVMA 356
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-PDSGEIKVLGKD--IKKEPEEVKRRIGYLPEE---PSLYENLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNItlaalnqftgamsslddaaeqhciqqsiqrlkiktsspelaigRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:cd03230 90 VRENL-------------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489011807 437 DIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-219 |
2.17e-29 |
|
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: 115.36 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSY---EGEIIFAGETLQANHIRDTE-R 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdEGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVkHLTVLENIFLGAEIsrHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGL--GQQQLVEIAKALN 158
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYGLRL--HGIKLKEELDERVEEALRKAALWDEVKDRLHALGLsgGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 159 KQVRLLILDEPTASLTEQETATLLAIVRDLqNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-236 |
2.88e-29 |
|
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: 115.91 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGETLQANHIRDTERKgI 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP--SSGEVLLDGRDLASLSRRELARR-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLGAeISRHGLL------DYEtmtlRCQKLLAQVNlpISP--DTRVGDLGLGQQQLVEIAK 155
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGR-YPHLGLFgrpsaeDRE----AVEEALERTG--LEHlaDRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 156 ALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQHIgtrdASGMSEdDI 234
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIV----AQGPPE-EV 225
|
..
gi 489011807 235 IT 236
Cdd:COG1120 226 LT 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-240 |
3.82e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.13 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNIT-KTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTERKG 82
Cdd:COG3845 257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS--GSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQE---LALVKHLTVLENIFLG----AEISRHGLLDYETMTLRCQKLLAQ--VNLPiSPDTRVGDLGLGQQQLVEI 153
Cdd:COG3845 335 VAYIPEDrlgRGLVPDMSVAENLILGryrrPPFSRGGFLDRKAIRAFAEELIEEfdVRTP-GPDTPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 154 AKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDD 233
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATREE 493
|
....*..
gi 489011807 234 IITMMVG 240
Cdd:COG3845 494 IGLLMAG 500
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-223 |
4.19e-29 |
|
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: 114.14 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFG--AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANhiRDTERKG 82
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS--GTAYINGYSIRTD--RKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHLTVLENIFLGAEIsrHGLLDyETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVR 162
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARL--KGLPK-SEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 163 LLILDEPTASLTEQETATLLAIVRDLQnHDIACIYISHKLNEVKAISDTICVIRDGQ--HIGT 223
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKlrCIGS 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-483 |
5.88e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 120.73 E-value: 5.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF----GAVKAVDNVSLRLNAGEVVSLCGENGSGKS----TLMKVL--------CGIYPHGSYEGEIIFAG 67
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqagglvqCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 68 ETLQAnHIRDTERKGIAIIHQE--LALVKHLTVLENIflGAEISRHGLLDYETMTLRCQKLLAQVNLPISPD--TRV-GD 142
Cdd:PRK10261 92 EQSAA-QMRHVRGADMAMIFQEpmTSLNPVFTVGEQI--AESIRLHQGASREEAMVEAKRMLDQVRIPEAQTilSRYpHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 143 LGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 222 GTRDA-------------SGMSEDDIITMMVGRELTALYP---------SEPHAH------GEEILRVEHLTAWHP---- 269
Cdd:PRK10261 249 ETGSVeqifhapqhpytrALLAAVPQLGAMKGLDYPRRFPlislehpakQEPPIEqdtvvdGEPILQVRNLVTRFPlrsg 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 270 ----VNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPV-SISNCQ-QAIAHGIAMVP 343
Cdd:PRK10261 329 llnrVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-GGEIIFNGQRIdTLSPGKlQALRRDIQFIF 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 344 EDrKKDGIVPVMAVGKNITLAALnqftgAMSSLDDAAEQHCIQQSIQRLKIKtssPELAI---GRLSGGNQQKAILARCL 420
Cdd:PRK10261 408 QD-PYASLDPRQTVGDSIMEPLR-----VHGLLPGKAAAARVAWLLERVGLL---PEHAWrypHEFSGGQRQRICIARAL 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 421 LLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
256-482 |
1.21e-28 |
|
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: 113.54 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLTAWHPvNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPVSISNCQQAI 335
Cdd:COG0410 1 MPMLEVENLHAGYG-GIHV--LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-PRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 336 AHGIAMVPEDRkkdGIVPVMAVGKNITLAALnqftgamsSLDDAAEQHCIQQSI--------QRLKIKTsspelaiGRLS 407
Cdd:COG0410 77 RLGIGYVPEGR---RIFPSLTVEENLLLGAY--------ARRDRAEVRADLERVyelfprlkERRRQRA-------GTLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 408 GGNQQKAILARCLLLNPRILILDEPTRG-----IDigakyEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:COG0410 139 GGEQQMLAIGRALMSRPKLLLLDEPSLGlapliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-223 |
1.75e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 116.01 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGI-YPhgsYEGEIIFAGETLQAN-HIRDterKG 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLeTP---DSGRIVLNGRDLFTNlPPRE---RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHLTVLENIFLGAEISRHGLLDYETmtlRCQKLLAQVNLPispdtrvgdlGL----------GQQQLVE 152
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRA---RVEELLELVQLE----------GLadrypsqlsgGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 153 IAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLqnHD---IACIYISHKLNEVKAISDTICVIRDGQ--HIGT 223
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRL--HDelgGTTVFVTHDQEEALELADRVVVMNQGRieQVGT 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-233 |
1.93e-28 |
|
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: 112.77 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGETLQANHIRDTERKGI 83
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPP--RSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLGAEISRHGLLDYETM----TL--RCQKLLAQvnlpispdtRVGDLGLGQQQLVEIAKAL 157
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLervyELfpRLKERRRQ---------RAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 158 NKQVRLLILDEPTA----SLTEQetatLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDD 233
Cdd:COG0410 152 MSRPKLLLLDEPSLglapLIVEE----IFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-225 |
9.14e-28 |
|
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: 111.05 E-value: 9.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQA--NHIRDTERKG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS--GEVLIDGEDISGlsEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHLTVLENIFLGaeISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVR 162
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 163 LLILDEPTASLTEQETATLLAIVRDLQN-HDIACIYISHKLNEVKAISDTICVIRDGQHI--GTRD 225
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVaeGTPE 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-219 |
9.85e-28 |
|
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: 109.06 E-value: 9.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 6 EMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTERKgIAI 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK--PSSGEILLDGKDLASLSPKELARK-IAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 86 IHQELALVkhltvleniflgaeisrhGLLDyetmtlrcqklLAqvnlpispDTRVGDLGLGQQQLVEIAKALNKQVRLLI 165
Cdd:cd03214 78 VPQALELL------------------GLAH-----------LA--------DRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 166 LDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
259-483 |
2.28e-27 |
|
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: 107.51 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPvnrHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPVSISNCQQAIAHG 338
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-PDSGEILVDGKEVSFASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 339 IAMVPEdrkkdgivpvmavgknitlaalnqftgamsslddaaeqhciqqsiqrlkiktsspelaigrLSGGNQQKAILAR 418
Cdd:cd03216 77 IAMVYQ-------------------------------------------------------------LSVGERQMVEIAR 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 419 CLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-225 |
2.45e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 111.35 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGETLQANHIRDT-----E 79
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP--DSGEVLWDGEPLDPEDRRRIgylpeE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RkgiaiihqelALVKHLTVLENI-FLGAeisRHGLLDYETMTlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:COG4152 80 R----------GLYPKMKVGEQLvYLAR---LKGLSKAEAKR-RADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 159 KQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHI--GTRD 225
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVlsGSVD 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-218 |
3.16e-27 |
|
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: 109.03 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGA-VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLqaNHIRDTE---- 79
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTS--GTIRVNGQDV--SDLRGRAipyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALVKHLTVLENIFLGAEISRHGLLDYETmtlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRK---RVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 160 QVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
259-485 |
3.99e-27 |
|
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: 108.96 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQAiahg 338
Cdd:COG1122 1 IELENLSFSYPGGTPA--LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT-SGEVLVDGKDITKKNLREL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 339 iamvpedRKKDGIV---P----VMA-VGKNITLAALNQftgamsSLDDAAEQHCIQQSIQRLKIKtsspELA---IGRLS 407
Cdd:COG1122 74 -------RRKVGLVfqnPddqlFAPtVEEDVAFGPENL------GLPREEIRERVEEALELVGLE----HLAdrpPHELS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 408 GGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:COG1122 137 GGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
260-482 |
5.03e-27 |
|
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: 106.56 E-value: 5.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 260 RVEHLTAWHPvnrHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPVSiSNCQQAIAHGI 339
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-PTSGEILIDGKDIA-KLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 340 AMVPEdrkkdgivpvmavgknitlaalnqftgamsslddaaeqhciqqsiqrlkiktsspelaigrLSGGNQQKAILARC 419
Cdd:cd00267 76 GYVPQ-------------------------------------------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 420 LLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-226 |
5.06e-27 |
|
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: 114.47 E-value: 5.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 15 GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHiRDTERKGIAIIHQELALVk 94
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP--PYSGSILINGVDLSDLD-PASWRRQIAWVPQNPYLF- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 95 HLTVLENIFLGA-EISRHglldyetmtlRCQKLLAQVN-------LPISPDTRVGDLGL----GQQQLVEIAKALNKQVR 162
Cdd:COG4988 424 AGTIRENLRLGRpDASDE----------ELEAALEAAGldefvaaLPDGLDTPLGEGGRglsgGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 163 LLILDEPTASL---TEQEtatLLAIVRDLQNHDIaCIYISHKLNEVKAiSDTICVIRDGQHI--GTRDA 226
Cdd:COG4988 494 LLLLDEPTAHLdaeTEAE---ILQALRRLAKGRT-VILITHRLALLAQ-ADRILVLDDGRIVeqGTHEE 557
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
275-485 |
6.09e-27 |
|
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: 107.14 E-value: 6.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 275 KRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGrWQGEIFIDGQPVSisncqqaiahgiAMVPEDR-KKDGIVP 353
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP-SSGEILLDGKDLA------------SLSPKELaRKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 354 vmavgknitlaalnqftgamsslddaaeqhciqQSIQRLKIKtsspELA---IGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:cd03214 80 ---------------------------------QALELLGLA----HLAdrpFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 431 EPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-219 |
6.34e-27 |
|
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: 108.11 E-value: 6.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLqaNHIRDTERkGIA 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTS--GRIYIGGRDV--TDLPPKDR-DIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAEISRHGLLDYETMTLRCQKLLAQVNLpisPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHL---LDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 165 ILDEPTASLTEQETATLLA-IVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAeLKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
258-485 |
7.05e-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: 108.98 E-value: 7.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTAWHPvNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPV-SISncQQAIA 336
Cdd:COG1120 1 MLEAENLSVGYG-GRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDGRDLaSLS--RRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 337 HGIAMVPEDRkkdgivpvmAVGKNIT---LAAL--NQFTGAMSSLDDAAEQHcIQQSIQRLKIKtsspELA---IGRLSG 408
Cdd:COG1120 75 RRIAYVPQEP---------PAPFGLTvreLVALgrYPHLGLFGRPSAEDREA-VEEALERTGLE----HLAdrpVDELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 409 GNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-219 |
9.96e-27 |
|
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: 107.38 E-value: 9.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 22 NVSLRLNaGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGETL---QANHIRDTERKGIAIIHQELALVKHLTV 98
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGL--EKPDGGTIVLNGTVLfdsRKKINLPPQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 99 LENIFLGAEISRHGlldyeTMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQET 178
Cdd:cd03297 93 RENLAFGLKRKRNR-----EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489011807 179 ATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03297 168 LQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-219 |
9.97e-27 |
|
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: 108.05 E-value: 9.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFG----AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGI-YPHgsyEGEIIFAGE--TLQANHIR 76
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPT---SGSVLVDGTdlTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 77 DTERKGIAIIHQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSSRTVFENVALPLEIAG---VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 157 LNKQVRLLILDEPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-223 |
1.52e-26 |
|
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: 108.50 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 10 ITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGE---TLQANHIRDTERKGIAII 86
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTS--GKVLIDGQdiaAMSRKELRELRRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 87 HQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLIL 166
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQG---VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 167 DEPTASL-----TEQETaTLLAIVRDLQnhdIACIYISHKLNEVKAISDTICVIRDGQ--HIGT 223
Cdd:cd03294 185 DEAFSALdplirREMQD-ELLRLQAELQ---KTIVFITHDLDEALRLGDRIAIMKDGRlvQVGT 244
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-226 |
1.63e-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: 113.78 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFG--AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGETLQANHIRDTeRKG 82
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP--TSGRILIDGIDLRQIDPASL-RRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVkHLTVLENIFLGAEisrhgLLDYETMTLRCQklLAQV-----NLPISPDTRVGDLGL----GQQQLVEI 153
Cdd:COG2274 551 IGVVLQDVFLF-SGTIRENITLGDP-----DATDEEIIEAAR--LAGLhdfieALPMGYDTVVGEGGSnlsgGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 154 AKALNKQVRLLILDEPTASLTEQETATLLAIVRDLqNHDIACIYISHKLnEVKAISDTICVIRDGQ--HIGTRDA 226
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRL-STIRLADRIIVLDKGRivEDGTHEE 695
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
259-483 |
1.77e-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: 107.52 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTawhpvnrhiKR------VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQ 332
Cdd:cd03219 1 LEVRGLT---------KRfgglvaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT-SGSVLFDGEDITGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 333 QAIAHGIAmvpedRK--KDGIVPVMAVGKNITLAALNQ------FTGAMSSLDDAAEQhcIQQSIQRLKIKTSSPELAiG 404
Cdd:cd03219 71 EIARLGIG-----RTfqIPRLFPELTVLENVMVAAQARtgsgllLARARREEREARER--AEELLERVGLADLADRPA-G 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
260-482 |
1.87e-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: 106.78 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 260 RVEHLTAWHPvNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVwPGRWQGEIFIDGQPVSiSNCQQAIAHGI 339
Cdd:cd03225 1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-LGPTSGEVLVDGKDLT-KLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 340 AMV---PEDrkkdgivpvmavgknitlaalnQFTGAmSSLDDAA---EQHCIQQSIQRLKIKTSSPELAIG--------R 405
Cdd:cd03225 78 GLVfqnPDD----------------------QFFGP-TVEEEVAfglENLGLPEEEIEERVEEALELVGLEglrdrspfT 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:cd03225 135 LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-221 |
2.27e-26 |
|
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: 106.69 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLqanhIRDTE--RKG 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS--GRATVAGHDV----VREPRevRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHLTVLENIFLGAEIsrHGlLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVR 162
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARL--YG-VPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 163 LLILDEPTASLTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-219 |
3.09e-26 |
|
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: 104.77 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFG--AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGETLQaNHIRDTERKG 82
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP--TSGEILIDGVDLR-DLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVkHLTVLENIFLGaeisrhglldyetmtlrcqkllaqvnlpispdtrvgdlglGQQQLVEIAKALNKQVR 162
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENILSG----------------------------------------GQRQRIAIARALLRDPP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 163 LLILDEPTASL---TEQEtatLLAIVRDLQnHDIACIYISHKLNEVKaISDTICVIRDGQ 219
Cdd:cd03228 117 ILILDEATSALdpeTEAL---ILEALRALA-KGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-173 |
3.18e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 106.29 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTF-GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLqaNHIRDTE---- 79
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER--PTSGQVLVNGQDL--SRLKRREipyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALVKHLTVLENIFLGAEISRHGLLDYETmtlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRR---RVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170
....*....|....
gi 489011807 160 QVRLLILDEPTASL 173
Cdd:COG2884 155 RPELLLADEPTGNL 168
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-219 |
3.34e-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: 107.09 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 2 TWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG-IYPhgSYEGEIIFAGETLQANHIRDTeR 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPP--TYGNDVRLFGERRGGEDVWEL-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELA--LVKHLTVLE--------NIFLGAEISrhglldyETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQL 150
Cdd:COG1119 78 KRIGLVSPALQlrFPRDETVLDvvlsgffdSIGLYREPT-------DEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 151 VEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEV-KAISDTIcVIRDGQ 219
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIpPGITHVL-LLKDGR 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-223 |
7.32e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 108.62 E-value: 7.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLqaNHIRDTERkGIA 84
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTS--GEILIGGRDV--TDLPPKDR-NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLG--------AEISRhglldyetmtlRCQKLLAQVNlpISP--DTRVGDLGLGQQQLVEIA 154
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPlklrkvpkAEIDR-----------RVREAAELLG--LEDllDRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 155 KALNKQVRLLILDEPT----ASLTEQETATLLAIVRDLqnhDIACIYISHKLNEVKAISDTICVIRDG--QHIGT 223
Cdd:COG3839 146 RALVREPKVFLLDEPLsnldAKLRVEMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGriQQVGT 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-219 |
7.81e-26 |
|
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: 105.59 E-value: 7.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTF-----GAVK--AVDNVSLRLNAGEVVSLCGENGSGKSTLMKvlcGIYphGSY---EGEIIFAGETL 70
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLK---CIY--GNYlpdSGSILVRHDGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 71 QANHIRDTERKGIAIIHQELALV-KHLTV------LEnifLGAEISRHGLLDYETMTLRCQKLLAQVNLP-----ISPDT 138
Cdd:COG4778 76 WVDLAQASPREILALRRRTIGYVsQFLRViprvsaLD---VVAEPLLERGVDREEARARARELLARLNLPerlwdLPPAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 139 RVGdlglGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:COG4778 153 FSG----GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
.
gi 489011807 219 Q 219
Cdd:COG4778 229 S 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
9.35e-26 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 105.45 E-value: 9.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTE- 79
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS--GEILVDGQDITGLSEKELYe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 -RKGIAIIHQELALVKHLTVLENIFLGaeISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:COG1127 80 lRRRIGMLFQGGALFDSLTVFENVAFP--LREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 159 KQVRLLILDEPTASLTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISDTICVIRDGQ--HIGTRD 225
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLADGKiiAEGTPE 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
258-485 |
1.09e-25 |
|
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: 104.76 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLT-AWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGqpVSISNCQQAIA 336
Cdd:cd03266 1 MITADALTkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDG--FDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 337 HGIAMVPEdrkKDGIVPVMAVGKNItlaalnQFTGAMSSLDDAAEQHCIQQSIQRLKIKTSSpELAIGRLSGGNQQKAIL 416
Cdd:cd03266 78 RRLGFVSD---STGLYDRLTARENL------EYFAGLYGLKGDELTARLEELADRLGMEELL-DRRVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 417 ARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
259-483 |
1.11e-25 |
|
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: 105.66 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRHIKRV-NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGrWQGEIFIDGQPVSISNcQQAIAH 337
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVlKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP-WSGEVTFDGRPVTRRR-RKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 338 GIAMVPEDrkKDGIV-PVMAVGKNITLAALNQ-FTGAMSSLDDAAEQHCIqqsiqrlkiktsSPELA---IGRLSGGNQQ 412
Cdd:COG1124 80 RVQMVFQD--PYASLhPRHTVDRILAEPLRIHgLPDREERIAELLEQVGL------------PPSFLdryPHQLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 413 KAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-225 |
1.16e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.86 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDteRKgIA 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS--GHIRFHGTDVSRLHARD--RK-VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAEI-SRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGLTVlPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 164 LILDEPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDG--QHIGTRD 225
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGniEQAGTPD 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-232 |
3.89e-25 |
|
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: 103.39 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTERKGIA 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS--GKILLDGQDITKLPMHKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRG---LSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIgtrdASGMSED 232
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVL----AEGTPEE 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-203 |
3.93e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.63 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTE-RKG 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITS--GDLIVDGLKVNDPKVDERLiRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHLTVLENIFLGAEISRhGLLDYETMTLrCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVR 162
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFGPLRVR-GASKEEAEKQ-ARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489011807 163 LLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLN 203
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
277-482 |
4.07e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 102.74 E-value: 4.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSIsncqqAIAHGIAMVPEDRkkdGIVPVMA 356
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-SGEVLFDGKPLDI-----AARNRIGYLPEER---GLYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNitLAALNQFTGAmsSLDDAAEQhcIQQSIQRLKIkTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:cd03269 87 VIDQ--LVYLAQLKGL--KKEEARRR--IDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489011807 437 DIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-221 |
4.12e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.84 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLqaNHIRDTER 80
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ--PTAGQIMLDGVDL--SHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KgIAIIHQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK11607 92 P-INMMFQSYALFPHMTVEQNIAFGLKQDK---LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 161 VRLLILDEPTASLTEQETATL-LAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-214 |
4.28e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 105.58 E-value: 4.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF-----------GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLqa 72
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTS--GEILFDGQDI-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 73 NHIRDTE----RKGIAIIHQE--LALVKHLTVLENIFLGAEIsrHGLLDYETMTLRCQKLLAQVNLPisPD--TRV---- 140
Cdd:COG4608 83 TGLSGRElrplRRRMQMVFQDpyASLNPRMTVGDIIAEPLRI--HGLASKAERRERVAELLELVGLR--PEhaDRYphef 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 141 -GdlglGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQN-HDIACIYISHKLNEVKAISDTICV 214
Cdd:COG4608 159 sG----GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDeLGLTYLFISHDLSVVRHISDRVAV 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-219 |
5.12e-25 |
|
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: 101.74 E-value: 5.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITktfgAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTERKGI 83
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP--PASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AII----HQElALVKHLTVLENIFLGAEISrhGlldyetmtlrcqkllaqvnlpispdtrvgdlglGQQQLVEIAKALNK 159
Cdd:cd03215 78 AYVpedrKRE-GLVLDLSVAENIALSSLLS--G---------------------------------GNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 160 QVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-219 |
5.31e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.96 E-value: 5.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGETLQANHI--RDterkg 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL--EKPTEGQIFIDGEDVTHRSIqqRD----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVR 162
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGLKMLG---VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 163 LLILDEPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-234 |
7.69e-25 |
|
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: 102.60 E-value: 7.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTERKGIA 84
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKS--GSIRLDGEDITKLPPHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAEI--SRHGLLDYETMTL--RCQKLLAQvnlpispdtRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:TIGR03410 79 YVPQGREIFPRLTVEENLLTGLAAlpRRSRKIPDEIYELfpVLKEMLGR---------RGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 161 VRLLILDEPT----ASLTEQETATLLAIVRDlqnHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDI 234
Cdd:TIGR03410 150 PKLLLLDEPTegiqPSIIKDIGRVIRRLRAE---GGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKV 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
259-486 |
1.39e-24 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 101.85 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLtawhpVNRHIKR--VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGrwQGEIFIDGQPVSISNCQQAI 335
Cdd:cd03218 1 LRAENL-----SKRYGKRkvVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlVKPD--SGKILLDGQDITKLPMHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 336 AHGIAMVPED----RKkdgivpvMAVGKNItLAALNQFTgamssLDDAAEQHCIQQSIQRLKIKTSSPELAIgRLSGGNQ 411
Cdd:cd03218 74 RLGIGYLPQEasifRK-------LTVEENI-LAVLEIRG-----LSKKEREEKLEELLEEFHITHLRKSKAS-SLSGGER 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 412 QKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKAN 486
Cdd:cd03218 140 RRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-212 |
2.11e-24 |
|
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: 101.07 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 6 EMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQAnhirdtERKGIAI 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK--PTSGSIRVFGKPLEK------ERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 86 IHQELALVKH--LTVLENIFLGAeISRHGLLDYETMTLRC--QKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:cd03235 73 VPQRRSIDRDfpISVRDVVLMGL-YGHKGLFRRLSKADKAkvDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489011807 162 RLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTI 212
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV 202
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-227 |
2.22e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGE------TLQANHIRDT 78
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDS--GQLNIAGHqfdfsqKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 79 ERKgIAIIHQELALVKHLTVLENIfLGAEISRHGLLDYETMTlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:COG4161 81 RQK-VGMVFQQYNLWPHLTVMENL-IEAPCKVLGLSKEQARE-KAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 159 KQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAS 227
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-219 |
2.31e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.40 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG-IYPHGSYEGEIIFAGETLQ-----ANH 74
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlITGDKSAGSHIELLGRTVQregrlARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 75 IRDTeRKGIAIIHQELALVKHLTVLENIFLGAEISR---HGLLDYETMTLRCQKL--LAQVNLPISPDTRVGDLGLGQQQ 149
Cdd:PRK09984 81 IRKS-RANTGYIFQQFNLVNRLSVLENVLIGALGSTpfwRTCFSWFTREQKQRALqaLTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 150 LVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
277-483 |
3.73e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 100.29 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSisnCQQAIAHGIAMVPEDrkkDGIVPVMA 356
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-SGEILIDGRDVT---GVPPERRNIGMVFQD---YALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNItlaalnQFTGAMSSLDDAAEQHCIQQSIQRLKIktsSPELA--IGRLSGGNQQKAILARCLLLNPRILILDEPTR 434
Cdd:cd03259 89 VAENI------AFGLKLRGVPKAEIRARVRELLELVGL---EGLLNryPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489011807 435 GIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03259 160 ALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-218 |
5.27e-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: 5.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVK----AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG-IYPHGsyeGEIIFAGetLQANHIRDT 78
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGlLEPDA---GFATVDG--FDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 79 ERKGIAIIHQELALVKHLTVLENIFLGAEIsrHGLLDYEtMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRLTARENLEYFAGL--YGLKGDE-LTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 159 KQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-219 |
7.89e-24 |
|
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: 104.85 E-value: 7.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTF--GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHiRDTERKG 82
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD--PQSGSITLGGVDLRDLD-EDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQElalvKHL---TVLENIFLGAE----------ISRHGLLDyetmtlrcqkLLAQvnLPISPDTRVGDLGL---- 145
Cdd:COG4987 411 IAVVPQR----PHLfdtTLRENLRLARPdatdeelwaaLERVGLGD----------WLAA--LPDGLDTWLGEGGRrlsg 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 146 GQQQLVEIAKALNKQVRLLILDEPTASL---TEQetatllAIVRDLQNH--DIACIYISHKLNEVKAIsDTICVIRDGQ 219
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLdaaTEQ------ALLADLLEAlaGRTVLLITHRLAGLERM-DRILVLEDGR 546
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-215 |
1.46e-23 |
|
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: 103.91 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 3 WLLEMKNITKTF-GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHiRDTERK 81
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD--PTEGSIAVNGVPLADAD-ADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 82 GIAIIHQELALVKHlTVLENIFLG------AEISRH----GLLDYETmtlrcqkllaqvNLPISPDTRVGD----LGLGQ 147
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIRLArpdasdAEIREAleraGLDEFVA------------ALPQGLDTPIGEggagLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 148 QQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIacIYISHKLnEVKAISDTICVI 215
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaQGRTV--LLVTHRL-ALAALADRIVVL 529
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
5-223 |
2.15e-23 |
|
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: 101.27 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIyphgsyegEIIFAGETLQANhiRDT-----E 79
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL--------ERQTAGTIYQGG--RDItrlppQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:TIGR03265 75 KRDYGIVFQSYALFPNLTVADNIAYGLKNRG---MGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALAT 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 160 QVRLLILDEPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQ--HIGT 223
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVieQVGT 218
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-218 |
2.19e-23 |
|
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: 98.91 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVL---CGIYPHGSYEGEIIFAGETLQANHIRDTE- 79
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmNDLVPGVRIEGKVLFDGQDIYDKKIDVVEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALVKhLTVLENIFLGAEIsrHGLLDYETMTLRCQKLLAQVNLPISPDTRVGD--LGL--GQQQLVEIAK 155
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRL--HGIKDKKELDEIVEESLKKAALWDEVKDRLHDsaLGLsgGQQQRLCIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 156 ALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNhDIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:TIGR00972 158 ALAVEPEVLLLDEPTSALDPIATGKIEELIQELKK-KYTIVIVTHNMQQAARISDRTAFFYDG 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
258-483 |
4.65e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 99.74 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTAWHPV-NRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV--WPGRWQGEIFIDGQPV-SISNCQ- 332
Cdd:COG0444 1 LLEVRNLKVYFPTrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlpPPGITSGEILFDGEDLlKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 333 QAI-AHGIAMVPEDrkkdgivPVMAVGKNI--TLAALNQFTGAmsslddAAEQHCIQQsIQRLKIktSSPELAIGR---- 405
Cdd:COG0444 81 RKIrGREIQMIFQDpmt-slnPVMTVGDQIaePLRIHGGLSKA------EARERAIEL-LERVGL--PDPERRLDRyphe 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-223 |
5.82e-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: 97.41 E-value: 5.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKaVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQAnhiRDTERKGIA 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS--GKILLNGKDITN---LPPEKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAeisRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGL---KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISDTICVIRDGQ--HIGT 223
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNGKliQVGK 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-227 |
6.63e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.39 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAG------ETLQANHIRDT 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL--EMPRSGTLNIAGnhfdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 79 ERKgIAIIHQELALVKHLTVLENIfLGAEISRHGLLDYETMTlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:PRK11124 81 RRN-VGMVFQQYNLWPHLTVQQNL-IEAPCRVLGLSKDQALA-RAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 159 KQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAS 227
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-223 |
7.09e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.02 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGETLqaNHIrDTERKGI 83
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF--ETPDSGRIMLDGQDI--THV-PAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLGaeisrhglldyetmtLRCQKL------------LAQVNLPISPDTRVGDLGLGQQQLV 151
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFG---------------LRMQKTpaaeitprvmeaLRMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 152 EIAKALNKQVRLLILDEPTASLT----EQETATLLAIVRDLqnhDIACIYISHKLNEVKAISDTICVIRDG--QHIGT 223
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGriEQDGT 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-219 |
7.57e-23 |
|
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: 96.49 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGeVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANhiRDTERKGIA 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSS--GTIRIDGQDVLKQ--PQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLEniFLGAEISRHGLLDYETMTlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03264 76 YLPQEFGVYPNFTVRE--FLDYIAWLKGIPSKEVKA-RVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDL-QNHdiaCIYIS-HKLNEVKAISDTICVIRDGQ 219
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELgEDR---IVILStHIVEDVESLCNQVAVLNKGK 206
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-226 |
9.69e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.30 E-value: 9.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTERKgIA 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA--GTVLVAGDDVEALSARAASRR-VA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLG--AEISRHGLLDyETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVR 162
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGrtPHRSRFDTWT-ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 163 LLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGqhiGTRDA 226
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG---RVRAA 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-219 |
1.14e-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: 96.84 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 17 VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGETLQANHIRDTeRKGIAIIHQELALVKhL 96
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFY--DPTSGEILLDGVDIRDLNLRWL-RSQIGLVSQEPVLFD-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 97 TVLENIFLGaeisRHGLLDYETMTLrCQKLLAQ---VNLPISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEP 169
Cdd:cd03249 92 TIAENIRYG----KPDATDEEVEEA-AKKANIHdfiMSLPDGYDTLVGERGSqlsgGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489011807 170 TASL-TEQETATLLAIVRDLQNhdIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03249 167 TSALdAESEKLVQEALDRAMKG--RTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-219 |
1.49e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.34 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTF----GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVL-CGIYPHGsyeGEIIFAGE---TLQA 72
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgCLDKPTS---GTYRVAGQdvaTLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 73 NHIRDTERKGIAIIHQELALVKHLTVLEN-----IFLGAEISRHglldyetmTLRCQKLLAQVNLPISPDTRVGDLGLGQ 147
Cdd:PRK10535 78 DALAQLRREHFGFIFQRYHLLSHLTAAQNvevpaVYAGLERKQR--------LLRAQELLQRLGLEDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 148 QQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKlNEVKAISDTICVIRDGQ 219
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGE 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-219 |
1.65e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.01 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 15 GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGETLqaNHI-RDTERKGIAIIHQELALV 93
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP--TSGRILIDGVDI--RDLtLESLRRQIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 94 kHLTVLENIFLGA-EISRHGLLDyetmTLRcqklLAQV-----NLPISPDTRVGDLGL----GQQQLVEIAKALNKQVRL 163
Cdd:COG1132 427 -SGTIRENIRYGRpDATDEEVEE----AAK----AAQAhefieALPDGYDTVVGERGVnlsgGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 164 LILDEPTASL-TEQETATLLAIVRDLQNHdiACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:COG1132 498 LILDEATSALdTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDDGR 551
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
277-433 |
2.50e-22 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 93.10 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQAiAHGIAMVPEDrkkDGIVPVMA 356
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-EGTILLDGQDLTDDERKSL-RKEIGYVFQD---PQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 357 VGKNITLAALNQFTGAMSSLDDAAEqhcIQQSIQRLKIKTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPT 433
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEE---ALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-219 |
4.04e-22 |
|
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: 94.58 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGA--VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGETLQANHIRDTeRKG 82
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY--KPTSGSVLLDGTDIRQLDPADL-RRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHlTVLENIFLGA-EISRHGLLdyETMTLRCQKLLAQvNLPISPDTRVGDLGL----GQQQLVEIAKAL 157
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITLGApLADDERIL--RAAELAGVTDFVN-KHPNGLDLQIGERGRglsgGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 158 NKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIAcIYISHKLNeVKAISDTICVIRDGQ 219
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTL-IIITHRPS-LLDLVDRIIVMDSGR 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-484 |
5.66e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 7 MKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFagetlqANHIRdterkgIAII 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEP--DSGEVSI------PKGLR------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 87 HQELALVKHLTVLENIFLG--------------------------------AEISRHGLLDYETmtlRCQKLLAQVNLPI 134
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLDGdaelraleaeleeleaklaepdedlerlaelqEEFEALGGWEAEA---RAEEILSGLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 135 SP-DTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLtEQETATLLAivRDLQNHDIACIYISHK---LNEVkaiSD 210
Cdd:COG0488 144 EDlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHL-DLESIEWLE--EFLKNYPGTVLVVSHDryfLDRV---AT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 211 TICVIRDGQ---HIG----------TRDASGMSE----DDII-----------------TMMVGR-------ELTALYPS 249
Cdd:COG0488 218 RILELDRGKltlYPGnysayleqraERLEQEAAAyakqQKKIakeeefirrfrakarkaKQAQSRikaleklEREEPPRR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 250 EPHAH---------GEEILRVEHLTAWHPvNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIF 320
Cdd:COG0488 298 DKTVEirfppperlGKKVLELEGLSKSYG-DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD-SGTVK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 321 IdGQPVSISNCQQaiaHGIAMVPEDRKKDGIVPVMAVGKNIT----LAALNqFTGAMsslddaaeqhciqqsiQRLKIKT 396
Cdd:COG0488 374 L-GETVKIGYFDQ---HQEELDPDKTVLDELRDGAPGGTEQEvrgyLGRFL-FSGDD----------------AFKPVGV 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 397 sspelaigrLSGGnqQKA--ILARCLLLNPRILILDEPTRGIDIGAKyEIykLINQLVQ-QGiAVIVIS--SELpeVLGL 471
Cdd:COG0488 433 ---------LSGG--EKArlALAKLLLSPPNVLLLDEPTNHLDIETL-EA--LEEALDDfPG-TVLLVShdRYF--LDRV 495
|
570
....*....|...
gi 489011807 472 SDRVLVMHEGRLK 484
Cdd:COG0488 496 ATRILEFEDGGVR 508
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-225 |
6.55e-22 |
|
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: 94.67 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAV-KAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGE-TLQANHIRDTERKG 82
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTS--GEIFIDGEdIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIihQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISP--DTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:cd03295 79 YVI--QQIGLFPHMTVEENIALVPKLLK---WPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 161 VRLLILDEPTASLTEQETATLLAIVRDLQ---NHDIacIYISHKLNEVKAISDTICVIRDG--QHIGTRD 225
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQqelGKTI--VFVTHDIDEAFRLADRIAIMKNGeiVQVGTPD 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-219 |
1.13e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKST----LMKVLcgiyphgSYEGEIIFAGETLQANHIRDT--ERKGIAIIHQE--L 90
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-------NSQGEIWFDGQPLHNLNRRQLlpVRHRIQVVFQDpnS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 91 ALVKHLTVLENIFLGAEIsRHGLLDYETMTLRCQKLLAQVNLpiSPDTR---VGDLGLGQQQLVEIAKALNKQVRLLILD 167
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRV-HQPTLSAAQREQQVIAVMEEVGL--DPETRhryPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489011807 168 EPTASLTEQETATLLAIVRDLQN-HDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQkHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
1.55e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.40 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGiYPHGSyEGEIIFAGETLQANHIRDTER 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-DPRAT-SGRIVFDGKDITDWQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKHLTVLENIFLGAEISRHGLldYETMTLRCQKLLAQvnLPISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQ--FQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 161 VRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-219 |
1.89e-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: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAvdNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIrdTERKgIA 84
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLP--PDSGRILWNGQDLTALPP--AERP-VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGaeISRHGLLDyETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLG--LRPGLKLT-AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 165 ILDEPTASL---TEQEtatLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG3840 152 LLDEPFSALdpaLRQE---MLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
277-485 |
1.92e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.90 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNcqqaiahgiamVPEDRKKDGIV---P 353
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ-SGEIKIDGITISKEN-----------LKEIRKKIGIIfqnP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 354 VmavgknitlaalNQFTGAmSSLDDAA---EQHCIQQSIQRLKIKTSSPELAIGR--------LSGGNQQKAILARCLLL 422
Cdd:PRK13632 93 D------------NQFIGA-TVEDDIAfglENKKVPPKKMKDIIDDLAKKVGMEDyldkepqnLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 423 NPRILILDEPTRGIDIGAKYEIYKLINQLVQQGI-AVIVISSELPEVLgLSDRVLVMHEGRLKA 485
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIA 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-219 |
1.97e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.31 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTERKgIAIIHQ--ELALVKhL 96
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA--GTITVGGMVLSEETVWDVRRQ-VGMVFQnpDNQFVG-A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 97 TVLENIFLGAE---ISRhglldyETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASL 173
Cdd:PRK13635 98 TVQDDVAFGLEnigVPR------EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSML 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489011807 174 TEQETATLLAIVRDL-QNHDIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:PRK13635 172 DPRGRREVLETVRQLkEQKGITVLSITHDLDEA-AQADRVIVMNKGE 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
259-483 |
2.75e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.80 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTaWHPVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSisncqqaiahg 338
Cdd:COG4619 1 LELEGLS-FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-SGEIYLDGKPLS----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 339 iAMVPED-RKKDGIV---PVM---AVGKNITLAalnqFTGAMSSLDDAAeqhcIQQSIQRLKIKTSSPELAIGRLSGGNQ 411
Cdd:COG4619 66 -AMPPPEwRRQVAYVpqePALwggTVRDNLPFP----FQLRERKFDRER----ALELLERLGLPPDILDKPVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 412 QKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-232 |
4.05e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.40 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGE--TLQANHIRdtERKG 82
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK--PDSGRIFLDGEdiTHLPMHKR--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLpispdTRVGD-LGL----GQQQLVEIAKAL 157
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRK---LSKKEREERLEELLEEFGI-----THLRKsKAYslsgGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 158 NKQVRLLILDEPTA-----SLTE-QEtatllaIVRDLQNHDIAcIYIS-HKLNEVKAISDTICVIRDGQHIgtrdASGMS 230
Cdd:COG1137 152 ATNPKFILLDEPFAgvdpiAVADiQK------IIRHLKERGIG-VLITdHNVRETLGICDRAYIISEGKVL----AEGTP 220
|
..
gi 489011807 231 ED 232
Cdd:COG1137 221 EE 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-219 |
4.10e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.84 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 20 VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgsYEGEIIFAGETLqanhiRDTE----RKGIAIIHQELALVkH 95
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP---YQGSLKINGIEL-----RELDpeswRKHLSWVGQNPQLP-H 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 96 LTVLENIFLGaeisRHGLLDYETMTLRCQkllAQVN-----LPISPDTRVGD----LGLGQQQLVEIAKALNKQVRLLIL 166
Cdd:PRK11174 437 GTLRDNVLLG----NPDASDEQLQQALEN---AWVSeflplLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489011807 167 DEPTASLTEQ-ETATLLAIVRDLQNHdiACIYISHKLNEVKAIsDTICVIRDGQ 219
Cdd:PRK11174 510 DEPTASLDAHsEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQ 560
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-225 |
4.62e-21 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 91.90 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGetlqaNHIRDTE----RKGIAIIHQELALVK 94
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDP--QKGQILIDG-----IDIRDISrkslRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 95 HlTVLENIFLGAEISRhglldyETMTLRCQKLLAQ----VNLPISPDTRVGD----LGLGQQQLVEIAKALNKQVRLLIL 166
Cdd:cd03254 91 G-TIMENIRLGRPNAT------DEEVIEAAKEAGAhdfiMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 167 DEPTASL-TEQETATLLAIVRDLQNHdiACIYISHKLNEVKAiSDTICVIRDGQHI--GTRD 225
Cdd:cd03254 164 DEATSNIdTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIeeGTHD 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
279-483 |
5.20e-21 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 92.01 E-value: 5.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGRwqGEIFIDGqpVSISNCQqAIAHGIAMVPEDRkkdGIVPVMAV 357
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPDS--GKILLNG--KDITNLP-PEKRDISYVPQNY---ALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 358 GKNITLAALNQftgamssLDDAAEqhciqqsIQRlKIKTSSPELAI--------GRLSGGNQQKAILARCLLLNPRILIL 429
Cdd:cd03299 89 YKNIAYGLKKR-------KVDKKE-------IER-KVLEIAEMLGIdhllnrkpETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 430 DEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
277-482 |
5.65e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.02 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWP--GRWQGEIFIDGQpvSISNCQQAI-----AHGIAMVPEDrKKD 349
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAanGRIGGSATFNGR--EILNLPEKElnklrAEQISMIFQD-PMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 350 GIVPVMAVGKNitLAALNQFTGAMSslddaaEQHCIQQSIQRL---KIktssPElAIGRL-------SGGNQQKAILARC 419
Cdd:PRK09473 109 SLNPYMRVGEQ--LMEVLMLHKGMS------KAEAFEESVRMLdavKM----PE-ARKRMkmyphefSGGMRQRVMIAMA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 420 LLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
279-483 |
6.65e-21 |
|
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: 91.20 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRrGEILGIAGLVGAGRTEAVQCLFGVW-PGRwqGEIFIDGQPVSISNcqqaiaHGIAMVPEDRKKdGIV----- 352
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEkPDG--GTIVLNGTVLFDSR------KKINLPPQQRKI-GLVfqqya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 --PVMAVGKNITLAalnqftgaMSSLDDAAEQHCIQQSIQRLKIkTSSPELAIGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:cd03297 86 lfPHLNVRENLAFG--------LKRKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489011807 431 EPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
232-500 |
8.44e-21 |
|
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: 96.06 E-value: 8.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 232 DDIITMMVGRELTALYPSEPHAHGEeiLRVEHLT-AWHPVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV 310
Cdd:COG2274 449 DDILDLPPEREEGRSKLSLPRLKGD--IELENVSfRYPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 311 WPGrWQGEIFIDGQPVS-ISncQQAIAHGIAMVPEDRK------KDgivpvmavgkNITLAALnQFTgaMSSLDDAAEQH 383
Cdd:COG2274 525 YEP-TSGRILIDGIDLRqID--PASLRRQIGVVLQDVFlfsgtiRE----------NITLGDP-DAT--DEEIIEAARLA 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 384 CIQQSIQRLkiktssP---ELAIG----RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGI 456
Cdd:COG2274 589 GLHDFIEAL------PmgyDTVVGeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGR 661
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489011807 457 AVIVISSELpEVLGLSDRVLVMHEGRlkanlVNQHLTQEQVMEA 500
Cdd:COG2274 662 TVIIIAHRL-STIRLADRIIVLDKGR-----IVEDGTHEELLAR 699
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-241 |
9.78e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.11 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTERKGI 83
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA--GNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLGAEISRHglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDD--LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 164 LILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIgtrdASGMSEDDIITMMVGR 241
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI----AHGTPTEILQDEHVKR 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-219 |
1.19e-20 |
|
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: 91.72 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTF--GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAG-ETLQANHIRDTeR 80
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPT---SGKVTVDGlDTLDEENLWEI-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQ--ELALVKhLTVLENIFLGAEisRHGlLDYETMTLRCQKLLAQVNL-------PISpdtrvgdLGLGQQQLV 151
Cdd:TIGR04520 77 KKVGMVFQnpDNQFVG-ATVEDDVAFGLE--NLG-VPREEMRKRVDEALKLVGMedfrdrePHL-------LSGGQKQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 152 EIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQN-HDIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEA-VLADRVIVMNKGK 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
258-486 |
1.28e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.09 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTawhpvnrhiKR------VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSisnc 331
Cdd:COG4152 1 MLELKGLT---------KRfgdktaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD-SGEVLWDGEPLD---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 332 qQAIAHGIAMVPEDRkkdGIVPVMAVGKNIT-LAALNQFTG--AMSSLDDAAEQHCIQQSIQRlKIKTsspelaigrLSG 408
Cdd:COG4152 67 -PEDRRRIGYLPEER---GLYPKMKVGEQLVyLARLKGLSKaeAKRRADEWLERLGLGDRANK-KVEE---------LSK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 409 GNQQKAILARCLLLNPRILILDEPTRGID-IGAKyEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKAN 486
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDpVNVE-LLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
259-483 |
1.91e-20 |
|
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: 88.43 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRHiKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQAIAHg 338
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDGADISQWDPNELGDH- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 339 IAMVPEDrkkdgivpvmavgknITLaalnqFTGAmsslddaaeqhcIQQSIqrlkiktsspelaigrLSGGNQQKAILAR 418
Cdd:cd03246 78 VGYLPQD---------------DEL-----FSGS------------IAENI----------------LSGGQRQRLGLAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 419 CLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSElPEVLGLSDRVLVMHEGRL 483
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
256-485 |
2.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 91.33 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLTAWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQaI 335
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGDLLTEENVWD-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 336 AHGIAMVPEDRKkdgivpvmavgknitlaalNQFTGAMSSlDDAA---EQHCI--QQSIQRLK----------IKTSSPe 400
Cdd:PRK13650 80 RHKIGMVFQNPD-------------------NQFVGATVE-DDVAfglENKGIphEEMKERVNealelvgmqdFKEREP- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 401 laiGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVlGLSDRVLVMH 479
Cdd:PRK13650 139 ---ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMK 214
|
....*.
gi 489011807 480 EGRLKA 485
Cdd:PRK13650 215 NGQVES 220
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-188 |
2.29e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 90.63 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKvlCGIYPHGSYEGEIIFAGETLQANHIRD-----TE 79
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLR--CINLLETPDSGEIRVGGEEIRLKPDRDgelvpAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALV-------KHLTVLENIFlgaEISRHGL-LDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLV 151
Cdd:COG4598 87 RRQLQRIRTRLGMVfqsfnlwSHMTVLENVI---EAPVHVLgRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 489011807 152 EIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDL 188
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDL 200
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-219 |
3.14e-20 |
|
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: 91.40 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 35 LCGENGSGKSTLMKVLCG-IYPHgsyEGEIIFAGETLQAnhiRDTERKGIAIIHQELALVKHLTVLENIFLGAEISRhgl 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGfEQPD---SGSIMLDGEDVTN---VPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 114 LDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNH-D 192
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlG 151
|
170 180
....*....|....*....|....*..
gi 489011807 193 IACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGK 178
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-187 |
3.46e-20 |
|
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: 88.57 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLqaNHIRDTERKGIA 84
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR--PDSGEVRWNGTPL--AEQRDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENI-FLgaeisrHGLLDYETMTlrCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:TIGR01189 77 YLGHLPGLKPELSALENLhFW------AAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170 180
....*....|....*....|....
gi 489011807 164 LILDEPTASLTEQETATLLAIVRD 187
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRA 172
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
259-482 |
3.94e-20 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 87.44 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPvNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGrWQGEIFIDGQPVSISNcQQAIAHG 338
Cdd:cd03228 1 IEFKNVSFSYP-GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP-TSGEILIDGVDLRDLD-LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 339 IAMVPEDrkkdgivPV---MAVGKNItlaalnqftgamsslddaaeqhciqqsiqrlkiktsspelaigrLSGGNQQKAI 415
Cdd:cd03228 78 IAYVPQD-------PFlfsGTIRENI--------------------------------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 416 LARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELpEVLGLSDRVLVMHEGR 482
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
277-486 |
4.67e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.66 E-value: 4.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGrwQGEIFIDGQPVsisncQQAIAHGIAmvpedRKkdGIVPV- 354
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPT--GGTILLRGQHI-----EGLPGHQIA-----RM--GVVRTf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 355 --------MAVGKNITLAALNQF-TGAMSSLDDA-----AEQHCIQQSIQRLKiKTSSPELA---IGRLSGGNQQKAILA 417
Cdd:PRK11300 87 qhvrlfreMTVIENLLVAQHQQLkTGLFSGLLKTpafrrAESEALDRAATWLE-RVGLLEHAnrqAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRLKAN 486
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-252 |
5.11e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 5.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGsyEGEIIFAGETLQANhiRDTERKGIA 84
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD--AGKITVLGVPVPAR--ARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAEISRHGLLDYETMTlrcQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVI---PSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIgtrdASGmSEDDIITMMVGRELT 244
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKI----AEG-RPHALIDEHIGCQVI 269
|
....*...
gi 489011807 245 ALYPSEPH 252
Cdd:PRK13536 270 EIYGGDPH 277
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-219 |
5.44e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKV---LCGIYPHGSYEGEIIFAGETLQANHIRDTERK 81
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 82 gIAIIHQELALVKHLTVLENIFLGAEI-----SRHGLLDYETMTLRCQKLLAQVNLPIspDTRVGDLGLGQQQLVEIAKA 156
Cdd:PRK14247 84 -VQMVFQIPNPIPNLSIFENVALGLKLnrlvkSKKELQERVRWALEKAQLWDEVKDRL--DAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 157 LNKQVRLLILDEPTASLTEQETATLLAIVRDLQNhDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQ 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
259-482 |
5.80e-20 |
|
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: 87.92 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTawhpVNRHIKRV-NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPvsISNCQQAIAH 337
Cdd:COG4133 3 LEAENLS----CRRGERLLfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP-PSAGEVLWNGEP--IRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 338 GIAMVPEDrkkDGIVPVMAVGKNITL-AALNQFTGAMSSLDDAAEQhciqQSIQRLKiktsspELAIGRLSGGNQQKAIL 416
Cdd:COG4133 76 RLAYLGHA---DGLKPELTVRENLRFwAALYGLRADREAIDEALEA----VGLAGLA------DLPVRQLSAGQKRRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 417 ARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGlsDRVLVMHEGR 482
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA--ARVLDLGDFK 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-218 |
1.03e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.04 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGETLQANHIRDTeRKGIAIIHQELalvkhltv 98
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI--EKVKSGEIFYNNQAITDDNFEKL-RKHIGIVFQNP-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 99 lENIFLGAEIS-------RHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTA 171
Cdd:PRK13648 93 -DNQFVGSIVKydvafglENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489011807 172 SLTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVkAISDTICVIRDG 218
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKsEHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-253 |
1.06e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.86 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGI-YPHGsyeGEIIFAGETL--QANHird 77
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDA---GSISLCGEPVpsRARH--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 tERKGIAIIHQELALVKHLTVLENIFLgaeISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:PRK13537 78 -ARQRVGVVPQFDNLDPDFTVRENLLV---FGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 158 NKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIgtrdASGmSEDDIITM 237
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI----AEG-APHALIES 228
|
250
....*....|....*.
gi 489011807 238 MVGRELTALYPSEPHA 253
Cdd:PRK13537 229 EIGCDVIEIYGPDPVA 244
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
260-484 |
1.11e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 87.31 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 260 RVEHLTawHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQAIAhgi 339
Cdd:cd03226 1 RIENIS--FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES-SGSILLNGKPIKAKERRKSIG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 340 aMVPEDRK----KDGIVPVMAVGKNITLAALNQFTGAMS--SLDDAAEQHciQQSiqrlkiktsspelaigrLSGGNQQK 413
Cdd:cd03226 75 -YVMQDVDyqlfTDSVREELLLGLKELDAGNEQAETVLKdlDLYALKERH--PLS-----------------LSGGQKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 414 AILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLK 484
Cdd:cd03226 135 LAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-219 |
1.16e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 88.27 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVL-------CGIYPHGSYEgeiIFAGETL--QANHI 75
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRVGDIT---IDTARSLsqQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 76 RDTeRKGIAIIHQELALVKHLTVLENIFLGAEISRHglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAK 155
Cdd:PRK11264 81 RQL-RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKG--EPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 156 ALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
277-483 |
1.19e-19 |
|
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: 88.85 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwqGEIFIDGQPVSISNCQQAIA---HGIAMVpedRKKDGIV 352
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRlIEPTS--GKVLIDGQDIAAMSRKELRElrrKKISMV---FQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 PVMAVGKNITLAALNQFTGAMSSLDDAAEQhciqqsIQRLKIKTSSPELaIGRLSGGNQQKAILARCLLLNPRILILDEP 432
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAEA------LELVGLEGWEHKY-PDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489011807 433 TRGIDIGAKYEIYKLINQLV-QQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
259-485 |
1.40e-19 |
|
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: 87.18 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRHIKrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwqGEIFIDGQpvSISNCQQAIAH 337
Cdd:cd03263 1 LQIRNLTKTYKKGTKPA-VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGeLRPTS--GTAYINGY--SIRTDRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 338 GIAMVPEDrkkDGIVPVMAVGKNITLAAlnQFTGamSSLDDaaeqhcIQQSIQRLKIKTSSPELA---IGRLSGGNQQKA 414
Cdd:cd03263 76 SLGYCPQF---DALFDELTVREHLRFYA--RLKG--LPKSE------IKEEVELLLRVLGLTDKAnkrARTLSGGMKRKL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 415 ILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQlVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-219 |
1.60e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 86.93 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 6 EMKNITKTFG-AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQanhiRDTERKGIA 84
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK--ESSGSILLNGKPIK----AKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELAlvKHL---TVLENIFLGAEISRHGLLDYETmtlrcqkLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:cd03226 75 YVMQDVD--YQLftdSVREELLLGLKELDAGNEQAET-------VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 162 RLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-226 |
1.83e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 89.38 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 16 AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETL---QANHIRDTeRKGIAIIHQE-LA 91
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK--ATDGEVAWLGKDLlgmKDDEWRAV-RSDIQMIFQDpLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 92 -LVKHLTVLENIflgAEISR--HGLLDYETMTLRCQKLLAQVNL-PISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILD 167
Cdd:PRK15079 110 sLNPRMTIGEII---AEPLRtyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 168 EPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQ--HIGTRDA 226
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHavELGTYDE 248
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
276-486 |
2.41e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 87.30 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 276 RVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGrwQGEIFIDGQPVS-ISNCQQAiaHGIAMVPEDRKKDGIVPV 354
Cdd:PRK03695 11 RLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAGQPLEaWSAAELA--RHRAYLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 355 MavgkniTLAALNQFTGAMSslddAAEQHCIQQSIQRLKI--KTSSPelaIGRLSGGNQQKAILARCLL-----LNP--R 425
Cdd:PRK03695 87 F------QYLTLHQPDKTRT----EAVASALNEVAEALGLddKLGRS---VNQLSGGEWQRVRLAAVVLqvwpdINPagQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 426 ILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKAN 486
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
259-483 |
2.45e-19 |
|
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: 90.97 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVS-ISncQQAIAH 337
Cdd:COG4988 337 IELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-SGSILINGVDLSdLD--PASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 338 GIAMVPEDrkkdgivPVMAVG---KNITLAALNqftGAMSSLDDAAEQHCIQQSIQRLkiktssP---ELAIG----RLS 407
Cdd:COG4988 412 QIAWVPQN-------PYLFAGtirENLRLGRPD---ASDEELEAALEAAGLDEFVAAL------PdglDTPLGeggrGLS 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 408 GGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELpEVLGLSDRVLVMHEGRL 483
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRL-ALLAQADRILVLDDGRI 549
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
278-483 |
2.97e-19 |
|
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: 86.79 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 278 NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSisncqqaiahgiAMVPED----RKKDGIV- 352
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD-SGEVLIDGEDIS------------GLSEAElyrlRRRMGMLf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 ------PVMAVGKNITLAaLNQFTgamsSLDDAaeqhcIQQSIQRLKIK----TSSPELAIGRLSGGNQQKAILARCLLL 422
Cdd:cd03261 84 qsgalfDSLTVFENVAFP-LREHT----RLSEE-----EIREIVLEKLEavglRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 423 NPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-219 |
3.33e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.13 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG-IYPhgsYEGEIIFAGETLqanhiRDTERkg 82
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSP---DSGEVRLNGRPL-----ADWSP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 iaiihQELAlvKHLTVL---ENI---FLGAEISRHGLLDYETMTLRCQKLLAQVnLpispdTRVGDLGL----------G 146
Cdd:PRK13548 72 -----AELA--RRRAVLpqhSSLsfpFTVEEVVAMGRAPHGLSRAEDDALVAAA-L-----AQVDLAHLagrdypqlsgG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 147 QQQLVEIAKAL------NKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13548 139 EQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGR 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
256-485 |
3.70e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.38 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLTAWHPvNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNcqqai 335
Cdd:PRK13635 3 EEIIRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-AGTITVGGMVLSEET----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 336 ahgiamVPEDRKKDGIV---PVmavgknitlaalNQFTGAMSSlDDAA---EQHCI---------QQSIQRLKIK---TS 397
Cdd:PRK13635 76 ------VWDVRRQVGMVfqnPD------------NQFVGATVQ-DDVAfglENIGVpreemvervDQALRQVGMEdflNR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 398 SPElaigRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLV-QQGIAVIVISSELPEVLGlSDRVL 476
Cdd:PRK13635 137 EPH----RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEAAQ-ADRVI 211
|
....*....
gi 489011807 477 VMHEGRLKA 485
Cdd:PRK13635 212 VMNKGEILE 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-219 |
4.52e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 88.42 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF----GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgsyEGEII------FAGETLQAN 73
Cdd:COG4170 3 LLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK----DNWHVtadrfrWNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 74 HIRDTER---KGIAIIHQE--------LALVKHLtvLENI----FLGAEISRHGlldyeTMTLRCQKLLAQVNlpISPDT 138
Cdd:COG4170 79 SPRERRKiigREIAMIFQEpsscldpsAKIGDQL--IEAIpswtFKGKWWQRFK-----WRKKRAIELLHRVG--IKDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 139 RVGD-----LGLGQQQLVEIAKALNKQVRLLILDEPTASLteqETATLLAIVRDL----QNHDIACIYISHKLNEVKAIS 209
Cdd:COG4170 150 DIMNsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAM---ESTTQAQIFRLLarlnQLQGTSILLISHDLESISQWA 226
|
250
....*....|
gi 489011807 210 DTICVIRDGQ 219
Cdd:COG4170 227 DTITVLYCGQ 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-218 |
4.86e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.95 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKvlCGIYPHGSYEGEIIFAGETLqaNHIRDTE----- 79
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLR--CINFLEKPSEGSIVVNGQTI--NLVRDKDgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 ---------RKGIAIIHQELALVKHLTVLENIfLGAEISRHGLLDYETMTlRCQKLLAQVNLPISPDTRV-GDLGLGQQQ 149
Cdd:PRK10619 82 adknqlrllRTRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGLSKQEARE-RAVKYLAKVGIDERAQGKYpVHLSGGQQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 150 LVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
241-485 |
6.59e-19 |
|
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: 89.81 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 241 RELTALYPSE------PHAHGEeiLRVEHLTAWHP-VNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPG 313
Cdd:COG4618 309 NELLAAVPAEpermplPRPKGR--LSVENLTVVPPgSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 314 RwQGEIFIDGQPVSISNcQQAIAHGIAMVPEDrkkdgivpvmavgknITLaalnqFTGA-------MSSLDD-----AAE 381
Cdd:COG4618 385 T-AGSVRLDGADLSQWD-REELGRHIGYLPQD---------------VEL-----FDGTiaeniarFGDADPekvvaAAK 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 382 QHCIQQSIQRLkiktssP---ELAIG----RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ 454
Cdd:COG4618 443 LAGVHEMILRL------PdgyDTRIGeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR 516
|
250 260 270
....*....|....*....|....*....|.
gi 489011807 455 GIAVIVIsSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:COG4618 517 GATVVVI-THRPSLLAAVDKLLVLRDGRVQA 546
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
255-485 |
8.08e-19 |
|
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: 85.80 E-value: 8.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 255 GEEILRVEHLTawhpvNRHIKRV--NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPVSisncq 332
Cdd:COG1127 2 SEPMIEVRNLT-----KSFGDRVvlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR-PDSGEILVDGQDIT----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 333 QAIAHGIAMVpedRKKDGIV-------PVMAVGKNITLAaLNQFTG--------------AMSSLDDAAEQhciqqsiqr 391
Cdd:COG1127 71 GLSEKELYEL---RRRIGMLfqggalfDSLTVFENVAFP-LREHTDlseaeirelvleklELVGLPGAADK--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 392 lkiktsSPelaiGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLG 470
Cdd:COG1127 138 ------MP----SELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFA 207
|
250
....*....|....*
gi 489011807 471 LSDRVLVMHEGRLKA 485
Cdd:COG1127 208 IADRVAVLADGKIIA 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
277-483 |
8.78e-19 |
|
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: 85.40 E-value: 8.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWP--GRWQGEIFIDGQPVSISNCQQAIAHgiamVPEDrkkDGIVPV 354
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEggGTTSGQILFNGQPRKPDQFQKCVAY----VRQD---DILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 355 MAVGKNITLAALNQFTGAMSS------LDDAAEQHCIQQSIQRLKIKTsspelaigrLSGGNQQKAILARCLLLNPRILI 428
Cdd:cd03234 96 LTVRETLTYTAILRLPRKSSDairkkrVEDVLLRDLALTRIGGNLVKG---------ISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 429 LDEPTRGIDIGAKYEIYKLINQLVQQGIAVIV-ISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
279-485 |
9.06e-19 |
|
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: 87.86 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVwPGRWQGEIFIDGQpvsisnCQQAIAHGIAMVPEDRKKdGIV------ 352
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGL-TRPDEGEIVLNGR------TLFDSRKGIFLPPEKRRI-GYVfqearl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 -PVMAVGKNItLAALNQFTGAMSSLDDAA--EQHCIQQSIQRLkiktsspelaIGRLSGGNQQKAILARCLLLNPRILIL 429
Cdd:TIGR02142 87 fPHLSVRGNL-RYGMKRARPSERRISFERviELLGIGHLLGRL----------PGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 430 DEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
259-496 |
1.04e-18 |
|
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: 89.05 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRHIkRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNcQQAIAHG 338
Cdd:COG4987 334 LELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ-SGSITLGGVDLRDLD-EDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 339 IAMVPEDrkkdgiVPVMA--VGKNITLAALNqftgamssLDDAAeqhcIQQSIQRLKIKT---SSPE---LAIG----RL 406
Cdd:COG4987 411 IAVVPQR------PHLFDttLRENLRLARPD--------ATDEE----LWAALERVGLGDwlaALPDgldTWLGeggrRL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 407 SGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPEvLGLSDRVLVMHEGRLKAN 486
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAG-LERMDRILVLEDGRIVEQ 550
|
250
....*....|
gi 489011807 487 LVNQHLTQEQ 496
Cdd:COG4987 551 GTHEELLAQN 560
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
266-483 |
1.11e-18 |
|
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: 86.01 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 266 AWHPVnrhikrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQ--AIAHGIAMVP 343
Cdd:TIGR02769 22 QRAPV------LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPA-QGTVSFRGQDLYQLDRKQrrAFRRDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 344 EDrKKDGIVPVMAVGKNITLAALNqftgaMSSLDDAAEQHCIQQSIQRLKIKTSSPELAIGRLSGGNQQKAILARCLLLN 423
Cdd:TIGR02769 95 QD-SPSAVNPRMTVRQIIGEPLRH-----LTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 424 PRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:TIGR02769 169 PKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-218 |
1.14e-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: 85.08 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 17 VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGI-YPHgsyEGEIIFAGETLQANHIRDTERKGIaIIHQELALVKH 95
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPT---SGEVRVAGLVPWKRRKKFLRRIGV-VFGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 96 LTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTE 175
Cdd:cd03267 110 LPVIDSFYLLAAIYD---LPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489011807 176 QETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:cd03267 187 VAQENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
15-251 |
1.38e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.51 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 15 GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGETLQA--NHIRDTERKGIAIIHQEL-- 90
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL--ESPSQGNVSWRGEPLAKlnRAQRKAFRRDIQMVFQDSis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 91 ALVKHLTVLENIflgAEISRHGL-LDYETMTLRCQKLLAQVNLPIS-PDTRVGDLGLGQQQLVEIAKALNKQVRLLILDE 168
Cdd:PRK10419 101 AVNPRKTVREII---REPLRHLLsLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 169 PTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQHIGTRDasgMSEDDIITMMVGREL-TAL 246
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP---VGDKLTFSSPAGRVLqNAV 254
|
....*
gi 489011807 247 YPSEP 251
Cdd:PRK10419 255 LPAFP 259
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-244 |
1.76e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.14 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGA-----VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGE--TLQANHIRd 77
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP--PDSGSILIDGKdvTKLPEYKR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 teRKGIAIIHQELAL--VKHLTVLENIFL----GAeisRHGLLDYETMTLR--CQKLLAQVNLPIS--PDTRVGDLGLGQ 147
Cdd:COG1101 79 --AKYIGRVFQDPMMgtAPSMTIEENLALayrrGK---RRGLRRGLTKKRRelFRELLATLGLGLEnrLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 148 QQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEvkAIS--DTICVIRDGQHIgtR 224
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQ--ALDygNRLIMMHEGRII--L 229
|
250 260
....*....|....*....|....*...
gi 489011807 225 DASG-----MSEDDIITM---MVGRELT 244
Cdd:COG1101 230 DVSGeekkkLTVEDLLELfeeIRGEELA 257
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
1.88e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.55 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVK---AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRD 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES--GQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 TERKgIAIIHQElalvkhltvLENIFLGAEIS---RHGL----LDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQL 150
Cdd:PRK13650 79 IRHK-IGMVFQN---------PDNQFVGATVEddvAFGLenkgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 151 VEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-219 |
2.27e-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: 84.20 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFG--AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTeRKG 82
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDS--GRILIDGHDVRDYTLASL-RRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVkHLTVLENIFLGaeisRHGLLDYETMTLRCQKLLAQV--NLPISPDTRVGDLGL----GQQQLVEIAKA 156
Cdd:cd03251 78 IGLVSQDVFLF-NDTVAENIAYG----RPGATREEVEEAARAANAHEFimELPEGYDTVIGERGVklsgGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 157 LNKQVRLLILDEPTASL-TEQETATLLAIVRDLQNHdiACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03251 153 LLKDPPILILDEATSALdTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGK 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-225 |
2.73e-18 |
|
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: 87.55 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF-----GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGETLQANHIRDT 78
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 79 ER----KGIAIIHQELALVKHLTVLENIF--LGAEISRHGLLDYETMTLRC---QKLLAQVNLPISPDTrvgdLGLGQQQ 149
Cdd:TIGR03269 359 GRgrakRYIGILHQEYDLYPHRTVLDNLTeaIGLELPDELARMKAVITLKMvgfDEEKAEEILDKYPDE----LSEGERH 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 150 LVEIAKALNKQVRLLILDEPTASL---TEQETATLLAIVRDLQNHDIacIYISHKLNEVKAISDTICVIRDGQHIGTRD 225
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMdpiTKVDVTHSILKAREEMEQTF--IIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
259-483 |
2.76e-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: 83.77 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPvNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW---PG-RWQGEIFIDGQPvsisncqqa 334
Cdd:cd03260 1 IELRDLNVYYG-DKHA--LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdliPGaPDEGEVLLDGKD--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 335 IAHGIAMVPEDRKKDGIV-----PV-MAVGKNITLAALNQFTGAMSSLDDAAEQhciqqsiqRLKIKTSSPE----LAIG 404
Cdd:cd03260 69 IYDLDVDVLELRRRVGMVfqkpnPFpGSIYDNVAYGLRLHGIKLKEELDERVEE--------ALRKAALWDEvkdrLHAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQgIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03260 141 GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
277-483 |
2.86e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 83.42 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQpvSISNCQQAIAHGIAMVPEdrkkDGIVPVMA 356
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD-SGEITFDGK--SYQKNIEALRRIGALIEA----PGFYPNLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNITLAALnqftgaMSSLDDAAeqhcIQQSIQRLKIKTsSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:cd03268 89 ARENLRLLAR------LLGIRKKR----IDEVLDVVGLKD-SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489011807 437 D-IGAKyEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03268 158 DpDGIK-ELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-189 |
3.60e-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: 83.64 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF----GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIyPHGSyEGEIIFAGETLQAnhiRDTE 79
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-DRPT-SGTVRLAGQDLFA---LDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 ------RKGIAIIHQELALVKHLTVLENIFLGAEISRHGllDYETmtlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEI 153
Cdd:COG4181 83 ararlrARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARA---RARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 489011807 154 AKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQ 189
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELN 193
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-219 |
4.12e-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: 81.88 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKA--VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHiRDTERKG 82
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS--GRVRLDGADISQWD-PNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHlTVLENIFLGaeisrhglldyetmtlrcqkllaqvnlpispdtrvgdlglGQQQLVEIAKALNKQVR 162
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENILSG----------------------------------------GQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 163 LLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLnEVKAISDTICVIRDGQ 219
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-219 |
4.12e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.47 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAV-DNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQA-NHirDTERKG 82
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP--LTEGEIRLDGRPLSSlSH--SVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQElALVKHLTVLENIFLGAEISRHGLLD-YETMTLrcqKLLAQvNLPISPDTRVGD----LGLGQQQLVEIAKAL 157
Cdd:PRK10790 417 VAMVQQD-PVVLADTFLANVTLGRDISEEQVWQaLETVQL---AELAR-SLPDGLYTPLGEqgnnLSVGQKQLLALARVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 158 NKQVRLLILDEPTASL---TEQETATLLAIVRDlqnhDIACIYISHKLNE-VKAisDTICVIRDGQ 219
Cdd:PRK10790 492 VQTPQILILDEATANIdsgTEQAIQQALAAVRE----HTTLVVIAHRLSTiVEA--DTILVLHRGQ 551
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
274-483 |
5.17e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.39 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 274 IKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVwPGRWQGEIFIDGQPVSISNCQQAIAHGIAMVPEDRKkdgIVP 353
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 354 VMAVGKNITLAALnqftgamsslddAAEQHCIQQSIQRlkIKTSSPELA------IGRLSGGNQQKAILARCLLLNPRIL 427
Cdd:PRK11614 94 RMTVEENLAMGGF------------FAERDQFQERIKW--VYELFPRLHerriqrAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 428 ILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-219 |
6.53e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.08 E-value: 6.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVK--AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHGSYEGEIIFAGETLQANHIRDTeRK 81
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlPDDNPNSKITVDGITLTAKTVWDI-RE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 82 GIAIIHQELalvkhltvlENIFLGAEIS---RHGL----LDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIA 154
Cdd:PRK13640 85 KVGIVFQNP---------DNQFVGATVGddvAFGLenraVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 155 KALNKQVRLLILDEPTASLTEQETATLLAIVRDLQN-HDIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGK 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-219 |
7.79e-18 |
|
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: 82.66 E-value: 7.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 18 KAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGETlqanhIRDTE----RKGIAIIHQELALV 93
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFY--DVSSGSILIDGQD-----IREVTldslRRAIGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 94 kHLTVLENIflgaeisRHGLLDY--ETMTLRCQKllAQ-----VNLPISPDTRVGDLGL----GQQQLVEIAKALNKQVR 162
Cdd:cd03253 88 -NDTIGYNI-------RYGRPDAtdEEVIEAAKA--AQihdkiMRFPDGYDTIVGERGLklsgGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 163 LLILDEPTASL---TEQEtatLLAIVRDLQNHDIAcIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03253 158 ILLLDEATSALdthTERE---IQAALRDVSKGRTT-IVIAHRLSTIVN-ADKIIVLKDGR 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
271-485 |
1.01e-17 |
|
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: 81.87 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 271 NRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGrwQGEIFIDGqpVSISNCQQA-IAHGIAMVPEDrkk 348
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPT--SGSVLLDG--TDIRQLDPAdLRRNIGYVPQD--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 349 dgivPVMAVGK---NITLAALnqftgamsSLDD-----AAEQHCIQQSIQRLKiktSSPELAIGR----LSGGNQQKAIL 416
Cdd:cd03245 87 ----VTLFYGTlrdNITLGAP--------LADDerilrAAELAGVTDFVNKHP---NGLDLQIGErgrgLSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 417 ARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPeVLGLSDRVLVMHEGRLKA 485
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSGRIVA 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
258-502 |
1.13e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTAWHPvNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQaIAH 337
Cdd:PRK11231 2 TLRTENLTVGYG-TKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ-SGTVFLGDKPISMLSSRQ-LAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 338 GIAMVPEdrkkdgivpVMAVGKNITLAAL--------NQFTGAMSSLDdaaeQHCIQQSIQRLKIKtsspELAIGR---L 406
Cdd:PRK11231 77 RLALLPQ---------HHLTPEGITVRELvaygrspwLSLWGRLSAED----NARVNQAMEQTRIN----HLADRRltdL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 407 SGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKAN 486
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
250
....*....|....*.
gi 489011807 487 lvnqhLTQEQVMEAAL 502
Cdd:PRK11231 220 -----GTPEEVMTPGL 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-186 |
1.27e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.39 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLqaNHIRDTERKGIA 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP--PLAGRVLLNGGPL--DFQRDSIARGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENI-FLGAEISRHGlldyetmtlrCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:cd03231 77 YLGHAPGIKTTLSVLENLrFWHADHSDEQ----------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPL 146
|
170 180
....*....|....*....|...
gi 489011807 164 LILDEPTASLTEQETATLLAIVR 186
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAMA 169
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-219 |
1.41e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.17 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 18 KAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTE-RKGIAIIHQ--ELALVK 94
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS--GKIIIDGVDITDKKVKLSDiRKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 95 HlTVLENIFLGAeiSRHGLLDYETMTlRCQKLLAQVNLPISP--DTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTAS 172
Cdd:PRK13637 99 E-TIEKDIAFGP--INLGLSEEEIEN-RVKRAMNIVGLDYEDykDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489011807 173 LTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13637 175 LDPKGRDEILNKIKELHkEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
281-482 |
1.63e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 81.72 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 281 SFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwqGEIFIDGQPVSisncqqaiahgiAMVPEDRkkdgivPV----- 354
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDS--GRILWNGQDLT------------ALPPAER------PVsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 355 -------MAVGKNITLaalnqftGAMSSLD-DAAEQHCIQQSIQRLKI---KTSSPelaiGRLSGGNQQKAILARCLLLN 423
Cdd:COG3840 79 ennlfphLTVAQNIGL-------GLRPGLKlTAEQRAQVEQALERVGLaglLDRLP----GQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 424 PRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
258-485 |
1.75e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.61 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLtawhpVNRHIKR--VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGrwQGEIFIDGQPVSisncqqa 334
Cdd:COG1137 3 TLEAENL-----VKSYGKRtvVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlVKPD--SGRIFLDGEDIT------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 335 iaH---------GIAMVPED----RKkdgivpvMAVGKNItLAALnQFTGamssLDDAAEQHCIQQ-----SIQRLKikt 396
Cdd:COG1137 69 --HlpmhkrarlGIGYLPQEasifRK-------LTVEDNI-LAVL-ELRK----LSKKEREERLEElleefGITHLR--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 397 SSPELAigrLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVL 476
Cdd:COG1137 131 KSKAYS---LSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAY 207
|
....*....
gi 489011807 477 VMHEGRLKA 485
Cdd:COG1137 208 IISEGKVLA 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-222 |
2.16e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.03 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIfAGETLQANHIRDTErkgia 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL--ETPSAGELL-AGTAPLAEAREDTR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAEisrhGllDYETMTLRCqklLAQVNLpispDTRVGD----LGLGQQQLVEIAKALNKQ 160
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGLK----G--QWRDAALQA---LAAVGL----ADRANEwpaaLSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 161 VRLLILDEPTA---SLTEQETATLlaIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQhIG 222
Cdd:PRK11247 152 PGLLLLDEPLGaldALTRIEMQDL--IESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK-IG 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
259-502 |
2.18e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 81.70 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTawhpVNRHIKRV-NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSiSNCQQAIAH 337
Cdd:COG4559 2 LEAENLS----VRLGGRTLlDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS-SGEVRLNGRPLA-AWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 338 GIAMVPEDrkkdgivpvmavgknitlAALN-QFT-------GAMS-SLDDAAEQHCIQQSIQRlkikTSSPELAiGR--- 405
Cdd:COG4559 76 RRAVLPQH------------------SSLAfPFTveevvalGRAPhGSSAAQDRQIVREALAL----VGLAHLA-GRsyq 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 -LSGGNQQKAILARCLL-------LNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLV 477
Cdd:COG4559 133 tLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILL 212
|
250 260
....*....|....*....|....*
gi 489011807 478 MHEGRLKAnlvnqHLTQEQVMEAAL 502
Cdd:COG4559 213 LHQGRLVA-----QGTPEEVLTDEL 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
277-484 |
2.26e-17 |
|
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: 81.00 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVS-ISncQQAIAHGIAMVPEDrkkdgivPVM 355
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS-SGSILIDGVDISkIG--LHDLRSRISIIPQD-------PVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVG---KNitLAALNQFTGAMssLDDAAEQHCIQQSIQRLKIKTSSPELAIGR-LSGGNQQKAILARCLLLNPRILILDE 431
Cdd:cd03244 90 FSGtirSN--LDPFGEYSDEE--LWQALERVGLKEFVESLPGGLDTVVEEGGEnLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 432 PTRGIDigakYEIYKLINQLVQQGIA---VIVISSELPEVLGlSDRVLVMHEGRLK 484
Cdd:cd03244 166 ATASVD----PETDALIQKTIREAFKdctVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-219 |
2.97e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.82 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTF----GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGE---TLQANHIRD 77
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTS--GSVLVDGVdltALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 tERKGIAIIHQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:COG1135 80 -ARRKIGMIFQHFNLLSSRTVAENVALPLEIAG---VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 158 NKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
257-483 |
3.67e-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: 79.52 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 257 EILRVEHLTAWHPVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRWQGEIFIDGQPVSISNCQQAI 335
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVSGEVLINGRPLDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 336 AhgiaMVPEDrkkDGIVPVMAVGKNITLAAlnqftgamsslddaaeqhciqqsiqRLKiktsspelaigRLSGGNQQKAI 415
Cdd:cd03213 85 G----YVPQD---DILHPTLTVRETLMFAA-------------------------KLR-----------GLSGGERKRVS 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 416 LARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVI----SSelpEVLGLSDRVLVMHEGRL 483
Cdd:cd03213 122 IALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSihqpSS---EIFELFDKLLLLSQGRV 190
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-219 |
4.17e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 81.13 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFA---GETLQANHIRD 77
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDA--GEVHYRmrdGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 TERKGIA-----IIHQELA--LVKHLTVLENI--FLGAEISRHglldYETMTLRCQKLLAQVNLPISpdtRVGDL----- 143
Cdd:PRK11701 81 AERRRLLrtewgFVHQHPRdgLRMQVSAGGNIgeRLMAVGARH----YGDIRATAGDWLERVEIDAA---RIDDLpttfs 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 144 GlGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11701 154 G-GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
259-485 |
4.83e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 79.82 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLT-AWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwqGEIFIDGQPVsisncqQAIA 336
Cdd:cd03293 1 LEVRNVSkTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGlERPTS--GEVLVDGEPV------TGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 337 HGIAMVPEDrkkDGIVPVMAVGKNITLAALNQFTG-------AMSSLD----DAAEQHCIQQsiqrlkiktsspelaigr 405
Cdd:cd03293 73 PDRGYVFQQ---DALLPWLTVLDNVALGLELQGVPkaearerAEELLElvglSGFENAYPHQ------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVM--HEGR 482
Cdd:cd03293 132 LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLsaRPGR 211
|
...
gi 489011807 483 LKA 485
Cdd:cd03293 212 IVA 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
267-486 |
4.92e-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: 80.45 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 267 WHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV-WPGrwQGEIFIDGqpvsisncqqaiahgiaMVPED 345
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPT--SGEVRVAG-----------------LVPWK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 346 RKKDGIVPVMAV-GKNITLA---------ALNQftgAMSSLDDAAEQHCIQQSIQRLKIktsSPEL--AIGRLSGGNQQK 413
Cdd:cd03267 88 RRKKFLRRIGVVfGQKTQLWwdlpvidsfYLLA---AIYDLPPARFKKRLDELSELLDL---EELLdtPVRQLSLGQRMR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 414 AILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRLKAN 486
Cdd:cd03267 162 AEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
277-480 |
5.59e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWpgrwqgeifidgQPVSiSNCQQAIAHGIAMVPEDRKKDGIVPvMA 356
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV------------APDE-GVIKRNGKLRIGYVPQKLYLDTTLP-LT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNITLAALNQFTGAMSSLDDAAEQHCIQQSIQRLkiktsspelaigrlSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:PRK09544 86 VNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKL--------------SGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489011807 437 DIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHE 480
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-219 |
8.25e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.60 E-value: 8.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF---------GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANH 74
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS--GELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 75 IRDTERKgIAIIHQELAlvKHLTVLENI--FLGAEISRHGLLDYETMTLRCQKLLAQVNL-PISPDTRVGDLGLGQQQLV 151
Cdd:PRK15112 82 YSYRSQR-IRMIFQDPS--TSLNPRQRIsqILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 152 EIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGE 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-236 |
9.18e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.06 E-value: 9.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTERKgIA 84
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS--GTVFLGDKPISMLSSRQLARR-LA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAE--ISRHGLLDYETMTLrCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVR 162
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGRSpwLSLWGRLSAEDNAR-VNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 163 LLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIgtrdASGmSEDDIIT 236
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM----AQG-TPEEVMT 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
259-483 |
9.76e-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: 79.07 E-value: 9.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLT-AWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV-WPGRwqGEIFIDGQPVS-ISNCQQAi 335
Cdd:cd03255 1 IELKNLSkTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTS--GEVRVDGTDISkLSEKELA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 336 ahgiamvPEDRKKDGIV-------PVMAVGKNITLAALnqFTGamSSLDDAAEQhcIQQSIQRLKIKTSSPELAiGRLSG 408
Cdd:cd03255 78 -------AFRRRHIGFVfqsfnllPDLTALENVELPLL--LAG--VPKKERRER--AEELLERVGLGDRLNHYP-SELSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 409 GNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSElPEVLGLSDRVLVMHEGRL 483
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
255-483 |
1.02e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.05 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 255 GEEILRVEHLTAW--HPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGR----WQGEIFIDGQPVSI 328
Cdd:PRK13631 18 DDIILRVKNLYCVfdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKygtiQVGDIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 329 SNCQQAIAHGIAMVPEDRKKDGIV---PVM-----AVGKNITLA--ALNQftgamsSLDDAAEQhcIQQSIQRLKIKTSS 398
Cdd:PRK13631 98 ELITNPYSKKIKNFKELRRRVSMVfqfPEYqlfkdTIEKDIMFGpvALGV------KKSEAKKL--AKFYLNKMGLDDSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 399 PELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVM 478
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVM 249
|
....*
gi 489011807 479 HEGRL 483
Cdd:PRK13631 250 DKGKI 254
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-219 |
1.03e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.39 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 6 EMKNITKTF----GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGI-YPHGsyeGEIIFAGE---TLQANHIRd 77
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLeRPTS---GRVLVDGQdltALSEKELR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 TERKGIAIIHQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:PRK11153 79 KARRQIGMIFQHFNLLSSRTVFDNVALPLELAG---TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 158 NKQVRLLILDEPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
259-478 |
1.12e-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: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRhiKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwqGEIFIDGQPVSISNcQQAIAH 337
Cdd:TIGR02857 322 LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGfVDPTE--GSIAVNGVPLADAD-ADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 338 GIAMVPEdrkkdgiVPVM---AVGKNITLAALNQfTGAMssLDDAAEQHCIQQSIQRLKIKTSSPelaIG----RLSGGN 410
Cdd:TIGR02857 397 QIAWVPQ-------HPFLfagTIAENIRLARPDA-SDAE--IREALERAGLDEFVAALPQGLDTP---IGeggaGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 411 QQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSElPEVLGLSDRVLVM 478
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHR-LALAALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
259-483 |
1.28e-16 |
|
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: 79.20 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLT-AWHPvnrHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFgvwpgRW----QGEIFIDGQPvsISNCQQ 333
Cdd:cd03253 1 IEFENVTfAYDP---GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-----RFydvsSGSILIDGQD--IREVTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 334 aiahgiamvPEDRKKDGIVPVMAVGKNITLAAlNQFTGAMSSLDD----AAEQHCIQQSIQRLKIKTSSpelAIG----R 405
Cdd:cd03253 71 ---------DSLRRAIGVVPQDTVLFNDTIGY-NIRYGRPDATDEevieAAKAAQIHDKIMRFPDGYDT---IVGerglK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPEVLGlSDRVLVMHEGRL 483
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
1.32e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFaGETLQanhirdterkgI 83
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE--PDSGTVKL-GETVK-----------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELA-LVKHLTVLENIFLGAEisrhgllDYETMTLRcqKLLAQVNLpiSPD---TRVGDLGLGQQQLVEIAKALNK 159
Cdd:COG0488 381 GYFDQHQEeLDPDKTVLDELRDGAP-------GGTEQEVR--GYLGRFLF--SGDdafKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 160 QVRLLILDEPT-----ASLTEQETAtllaivrdLQNHDIACIYISHK---LNevkAISDTICVIRDGQ 219
Cdd:COG0488 450 PPNVLLLDEPTnhldiETLEALEEA--------LDDFPGTVLLVSHDryfLD---RVATRILEFEDGG 506
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-221 |
1.37e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.65 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAGETLQANHIRDTeRKGIAIIHQElalvkhlt 97
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQ---SGEIKIDGITISKENLKEI-RKKIGIIFQN-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 98 vLENIFLGAEISRH---GL----LDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:PRK13632 92 -PDNQFIGATVEDDiafGLenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489011807 171 ASLTEQETATLLAIVRDLQNHDIAC-IYISHKLNEVkAISDTICVIRDGQHI 221
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKKTlISITHDMDEA-ILADKVIVFSEGKLI 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-219 |
1.44e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 79.07 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQanhIRDTE--RKGIAIIHQELALVKHl 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYV--PENGRVLVDGHDLA---LADPAwlRRQVGVVLQENVLFNR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 97 TVLENIFLGAE-ISRHGLLDYETMTLRCQKLLaqvNLPISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPTA 171
Cdd:cd03252 91 SIRDNIALADPgMSMERVIEAAKLAGAHDFIS---ELPEGYDTIVGEQGAglsgGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489011807 172 SL-TEQETatllAIVRDLqnHDI----ACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03252 168 ALdYESEH----AIMRNM--HDIcagrTVIIIAHRLSTVKN-ADRIIVMEKGR 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
277-497 |
1.92e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.65 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGRwqGEIFIDGQPVSiSNCQQAIAhGIAMVPEdrkKDGIVPVM 355
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTsPDA--GKITVLGVPVP-ARARLARA-RIGVVPQ---FDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVGKNITL------AALNQFTGAMSSLDDAAeqhciqqsiqRLKIKTSSPelaIGRLSGGNQQKAILARCLLLNPRILIL 429
Cdd:PRK13536 130 TVRENLLVfgryfgMSTREIEAVIPSLLEFA----------RLESKADAR---VSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 430 DEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKANLVNQHLTQEQV 497
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
277-485 |
1.97e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGrwQGEIFIDGQPVSiSNCQQAIAHGIAMVPEDRKKDGIVPVM 355
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtPT--AGTVLVAGDDVE-ALSARAASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVGKNITLAALNQFtGAMSSLDDAAeqhcIQQSIQRLKIkTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:PRK09536 96 QVVEMGRTPHRSRF-DTWTETDRAA----VERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489011807 436 IDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
277-485 |
2.37e-16 |
|
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: 78.18 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGqpvsisncqqaiaHGIAMVPED-RKKDGIVPVM 355
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT-SGRATVAG-------------HDVVREPREvRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVGKNITLAALNQFT-GAMSSLDDAAEQHCIQQSIQRLKIKTSSPELaIGRLSGGNQQKAILARCLLLNPRILILDEPTR 434
Cdd:cd03265 82 LSVDDELTGWENLYIhARLYGVPGAERRERIDELLDFVGLLEAADRL-VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489011807 435 GIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
275-505 |
2.40e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 275 KRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPVSISNCQQAIAHGIAMVPEDRK------- 347
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP-RDAGNIIIDDEDISLLPLHARARRGIGYLPQEASifrrlsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 348 KDGIVPVMAVGKNITlaalnqftgaMSSLDDAAEQHCIQQSIQRLKIKTSSPelaigrLSGGNQQKAILARCLLLNPRIL 427
Cdd:PRK10895 96 YDNLMAVLQIRDDLS----------AEQREDRANELMEEFHIEHLRDSMGQS------LSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 428 ILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKAN-LVNQHLTQEQVMEAALRSE 505
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHgTPTEILQDEHVKRVYLGED 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
278-483 |
2.56e-16 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 77.57 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 278 NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQqaiahgiamVPEDRKKDGIV----- 352
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD-SGTIIIDGLKLTDDKKN---------INELRQKVGMVfqqfn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 --PVMAVGKNITLAALNQFtgAMSslDDAAEQHCIQQsIQRLKI---KTSSPelaiGRLSGGNQQKAILARCLLLNPRIL 427
Cdd:cd03262 87 lfPHLTVLENITLAPIKVK--GMS--KAEAEERALEL-LEKVGLadkADAYP----AQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 428 ILDEPTRGID---IGakyEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03262 158 LFDEPTSALDpelVG---EVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
251-482 |
2.87e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.83 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 251 PHAH---GEEILRVEHLT-AWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLF-------------GVWPG 313
Cdd:PRK10261 2 PHSDeldARDVLAVENLNiAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMrlleqagglvqcdKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 314 RWQGEIfIDGQPVSISNCQQAIAHGIAMVPEDrKKDGIVPVMAVGKNITLAA-LNQFTGAMSSLDDAaeqhciQQSIQRL 392
Cdd:PRK10261 82 RRSRQV-IELSEQSAAQMRHVRGADMAMIFQE-PMTSLNPVFTVGEQIAESIrLHQGASREEAMVEA------KRMLDQV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 393 KIKTSSPELA--IGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVL 469
Cdd:PRK10261 154 RIPEAQTILSryPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVA 233
|
250
....*....|...
gi 489011807 470 GLSDRVLVMHEGR 482
Cdd:PRK10261 234 EIADRVLVMYQGE 246
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
279-485 |
3.87e-16 |
|
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: 79.76 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVsisncqQAIAHGIAMVPEDRKKdGIV------ 352
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD-SGRIRLGGEVL------QDSARGIFLPPHRRRI-GYVfqearl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 -PVMAVGKNITLAALNQFTGAM-SSLDDAaeqhciqqsIQRLKIktsSPELA--IGRLSGGNQQKAILARCLLLNPRILI 428
Cdd:COG4148 89 fPHLSVRGNLLYGRKRAPRAERrISFDEV---------VELLGI---GHLLDrrPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 429 LDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
254-483 |
4.41e-16 |
|
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: 77.51 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 254 HGEEILRVEHLTAWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPvsISNCQQ 333
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-GGQVLLDGKP--ISQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 334 AIAHG-IAMVPEDrkkdgivPVM---AVGKNITLAALNQFTGAMSSLDDAAEQHCIQQSIQrLKIKTSSPElAIGRLSGG 409
Cdd:cd03248 84 KYLHSkVSLVGQE-------PVLfarSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELA-SGYDTEVGE-KGSQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 410 NQQKAILARCLLLNPRILILDEPTRGIDIgakyEIYKLINQLVQQGI---AVIVISSELPEVlGLSDRVLVMHEGRL 483
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDA----ESEQQVQQALYDWPerrTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
259-482 |
4.46e-16 |
|
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: 77.61 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRHikRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPV---SISNCQQAI 335
Cdd:cd03256 1 IEVENLSKTYPNGKK--ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-SGSVLIDGTDInklKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 336 AHgIAMVPEDRkkdGIVPVMAVGKNITLAALNQ---FTGAMSSLDDAAEQHCIQqSIQRLKIKTSSPELAiGRLSGGNQQ 412
Cdd:cd03256 78 RQ-IGMIFQQF---NLIERLSVLENVLSGRLGRrstWRSLFGLFPKEEKQRALA-ALERVGLLDKAYQRA-DQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 413 KAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-219 |
5.04e-16 |
|
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: 77.13 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 22 NVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTERKgIAIIHQELALVKHlTVLEN 101
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ--PQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 102 IflgaeisRHGLLDYETMTLR--CQKLLAQVN---LPISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPTAS 172
Cdd:cd03248 108 I-------AYGLQSCSFECVKeaAQKAHAHSFiseLASGYDTEVGEKGSqlsgGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489011807 173 L-TEQETATLLAIVRDLQNHDIacIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03248 181 LdAESEQQVQQALYDWPERRTV--LVIAHRLSTVER-ADQILVLDGGR 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-219 |
6.13e-16 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 76.76 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 24 SLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANhirDTERKGIAIIHQELALVKHLTVLENIF 103
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS--GRVLINGVDVTAA---PPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 104 LGAEisrHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLA 183
Cdd:cd03298 93 LGLS---PGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 489011807 184 IVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03298 170 LVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
257-502 |
6.55e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.83 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 257 EILRVEHLTAWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPVSISNCQQaIA 336
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-EFEGKVKIDGELLTAENVWN-LR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 337 HGIAMVPEDRKkdgivpvmavgknitlaalNQFTGAMSSlDDAA---EQHCI--QQSIQR----------LKIKTSSPel 401
Cdd:PRK13642 81 RKIGMVFQNPD-------------------NQFVGATVE-DDVAfgmENQGIprEEMIKRvdeallavnmLDFKTREP-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 402 aiGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGlSDRVLVMHE 480
Cdd:PRK13642 139 --ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKA 215
|
250 260
....*....|....*....|....
gi 489011807 481 GRLKANLVNQHL--TQEQVMEAAL 502
Cdd:PRK13642 216 GEIIKEAAPSELfaTSEDMVEIGL 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
277-483 |
1.00e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQAIA--HGIAMVPEDrkkdgivPV 354
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPS-QGNVSWRGEPLAKLNRAQRKAfrRDIQMVFQD-------SI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 355 MAVGKNITLAA-LNQFTGAMSSLDDAAEQHCIQQSIQRLKIKTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPT 433
Cdd:PRK10419 100 SAVNPRKTVREiIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489011807 434 RGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-218 |
1.11e-15 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 75.91 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKN-----ITKTFgAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLcGIYPHGSyEGEIIFAGETL------QA 72
Cdd:NF038007 1 MLNMQNaekcyITKTI-KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNII-GMFDSLD-SGSLTLAGKEVtnlsysQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 73 NHIRdteRKGIAIIHQELALVKHLTVLENIFLgaEISRHGLLDYETMTlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVE 152
Cdd:NF038007 78 IILR---RELIGYIFQSFNLIPHLSIFDNVAL--PLKYRGVAKKERIE-RVNQVLNLFGIDNRRNHKPMQLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 153 IAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKlNEVKAISDTICVIRDG 218
Cdd:NF038007 152 IARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDG 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-170 |
1.19e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.17 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 6 EMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIrDTeRKGIAI 85
Cdd:NF033858 268 EARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP--ASEGEAWLFGQPVDAGDI-AT-RRRVGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 86 IHQELALVKHLTVLENIFLGAEISRhglLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLI 165
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELHARLFH---LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
....*
gi 489011807 166 LDEPT 170
Cdd:NF033858 421 LDEPT 425
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-219 |
1.36e-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: 74.66 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFG--AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQAnhIRDTERKG 82
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLK--PQQGEITLDGVPVSD--LEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELalvkHL---TVLENifLGAEISRhglldyetmtlrcqkllaqvnlpispdtrvgdlglGQQQLVEIAKALNK 159
Cdd:cd03247 77 ISVLNQRP----YLfdtTLRNN--LGRRFSG-----------------------------------GERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 160 QVRLLILDEPTASL---TEQETATLLAIVrdLQNHDIacIYISHKLNEVKAIsDTICVIRDGQ 219
Cdd:cd03247 116 DAPIVLLDEPTVGLdpiTERQLLSLIFEV--LKDKTL--IWITHHLTGIEHM-DKILFLENGK 173
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-219 |
1.37e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF--GAVKA--VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLqaNHIRDTE 79
Cdd:PRK11629 5 LLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTS--GDVIFNGQPM--SKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 R-----KGIAIIHQELALVKHLTVLENIFLGAEIsrhGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIA 154
Cdd:PRK11629 81 KaelrnQKLGFIYQFHHLLPDFTALENVAMPLLI---GKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 155 KALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTIcVIRDGQ 219
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGR 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
277-483 |
2.04e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 75.74 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGvWPGRWQGEIFIDGQPvsisncqqaiahgIAMVPEDRKKDGIV---- 352
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG-FETPTSGEILLDGKD-------------ITNLPPHKRPVNTVfqny 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 ---PVMAVGKNITlaalnqFTGAMSSLDDAAEQHCIQQSIQRLKIKtsspELA---IGRLSGGNQQKAILARCLLLNPRI 426
Cdd:cd03300 82 alfPHLTVFENIA------FGLRLKKLPKAEIKERVAEALDLVQLE----GYAnrkPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 427 LILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-193 |
2.10e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.89 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANhirDTERkgi 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH--GSITLDGKPVEGP---GAER--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLGAEISRHGLLDYETmtlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRL 163
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLE---IAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489011807 164 LILDEPTASLT----EQETATLLAIVRD------LQNHDI 193
Cdd:PRK11248 150 LLLDEPFGALDaftrEQMQTLLLKLWQEtgkqvlLITHDI 189
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
277-482 |
2.21e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.77 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV-WPGrwQGEIFIDGQPVSiSNCQQAIAHgIAMVPEdrkKDGIVPVM 355
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPD--AGSISLCGEPVP-SRARHARQR-VGVVPQ---FDNLDPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVGKNitLAALNQFTGAMSSLDDAAEQHCIQqsIQRLKIKTSSPelaIGRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:PRK13537 96 TVREN--LLVFGRYFGLSAAAARALVPPLLE--FAKLENKADAK---VGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489011807 436 IDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
277-496 |
2.28e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.61 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEIL-----------GIAGLVG---AGRTEAVQCLFGVWPgrWQ-GEIFIDGQPVSiSNCQQAIAHGIAM 341
Cdd:PRK10790 343 IDNVSFAYRDDNLVlqninlsvpsrGFVALVGhtgSGKSTLASLLMGYYP--LTeGEIRLDGRPLS-SLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 342 VPEDrkkdgivPVMAVGK---NITLAAlnqftgamssldDAAEQHCIQ--QSIQRLKIKTSSPE---LAIG----RLSGG 409
Cdd:PRK10790 420 VQQD-------PVVLADTflaNVTLGR------------DISEEQVWQalETVQLAELARSLPDglyTPLGeqgnNLSVG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 410 NQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLInQLVQQGIAVIVISSELPEVLGlSDRVLVMHEGRLKANLVN 489
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTH 558
|
....*..
gi 489011807 490 QHLTQEQ 496
Cdd:PRK10790 559 QQLLAAQ 565
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-219 |
2.28e-15 |
|
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: 75.22 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTeRKGIAIIHQElALVKHLTV 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE--LSSGSILIDGVDISKIGLHDL-RSRISIIPQD-PVLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 99 LENIFLGAEISRHGLLDY-ETMTLR--CQKLLAQVNLPISPDTrvGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLtE 175
Cdd:cd03244 95 RSNLDPFGEYSDEELWQAlERVGLKefVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALLRKSKILVLDEATASV-D 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489011807 176 QETATLLAIVrdLQNHDIAC--IYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03244 172 PETDALIQKT--IREAFKDCtvLTIAHRLDTIID-SDRILVLDKGR 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-226 |
2.69e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 17 VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGE---TLQANHIRDTeRKGIAIIHQE--LA 91
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE--SQGGEIIFNGQridTLSPGKLQAL-RRDIQFIFQDpyAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 92 LVKHLTVLENIFLGAEIsrHGLLDYETMTLRCQKLLAQVNLPISPDTRV-GDLGLGQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRV--HGLLPGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 171 ASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQ--HIGTRDA 226
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQivEIGPRRA 550
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
275-482 |
2.85e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 76.24 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 275 KRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGqpVSISNCQqaiahgiAMVPEDRKKDGIV-- 352
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT-SGKIIIDG--VDITDKK-------VKLSDIRKKVGLVfq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 -PVM-----AVGKNITLAALNQftgamsSLDDAAEQHCIQQSIQRLKI-----KTSSPelaiGRLSGGNQQKAILARCLL 421
Cdd:PRK13637 91 yPEYqlfeeTIEKDIAFGPINL------GLSEEEIENRVKRAMNIVGLdyedyKDKSP----FELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 422 LNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
258-506 |
3.09e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.04 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTAWHPVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSIS-----NCQ 332
Cdd:PRK13636 5 ILKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPS-SGRILFDGKPIDYSrkglmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 333 QAIAhgiaMVPEDrkKDGIVPVMAVGKNITLAALNqftgaMSSLDDAaeqhcIQQSIQRLKIKTSSPEL---AIGRLSGG 409
Cdd:PRK13636 82 ESVG----MVFQD--PDNQLFSASVYQDVSFGAVN-----LKLPEDE-----VRKRVDNALKRTGIEHLkdkPTHCLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 410 NQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGR--LKAN 486
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRviLQGN 225
|
250 260
....*....|....*....|
gi 489011807 487 LVNQHLTQEQVMEAALRSER 506
Cdd:PRK13636 226 PKEVFAEKEMLRKVNLRLPR 245
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
277-483 |
3.27e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 78.28 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPV-SISncQQAIAHGIAMVPEDrkkdgiVPVM 355
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT-SGRILIDGVDIrDLT--LESLRRQIGVVPQD------TFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 A--VGKNITLAALNQftgAMSSLDDAAEQHCIQQSIQRLkiktssPE---LAIG----RLSGGNQQK-AIlARCLLLNPR 425
Cdd:COG1132 427 SgtIRENIRYGRPDA---TDEEVEEAAKAAQAHEFIEAL------PDgydTVVGergvNLSGGQRQRiAI-ARALLKDPP 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 426 ILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPEVLGlSDRVLVMHEGRL 483
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRI 552
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-221 |
3.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTF---GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGETLQANHIRD 77
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE--FEGKVKIDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 TERKGIAIIHQELALVKHLTVLENIFLGAEisRHGlLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:PRK13642 79 LRRKIGMVFQNPDNQFVGATVEDDVAFGME--NQG-IPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 158 NKQVRLLILDEPTASLTEQETATLLAIVRDLQN-HDIACIYISHKLNEVkAISDTICVIRDGQHI 221
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkYQLTVLSITHDLDEA-ASSDRILVMKAGEII 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-184 |
3.63e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.07 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 21 DNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANhiRDTerkgiaiIHQELALVKH----- 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR--PDAGEVLWQGEPIRRQ--RDE-------YHQDLLYLGHqpgik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 96 --LTVLENI-FLGAEisrHGLLDYEtmtlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTAS 172
Cdd:PRK13538 87 teLTALENLrFYQRL---HGPGDDE----ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170
....*....|..
gi 489011807 173 LTEQETATLLAI 184
Cdd:PRK13538 160 IDKQGVARLEAL 171
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-221 |
5.17e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.89 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGA-----VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGETLQANHIRDTE 79
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 ---------------------RKGIAIIHQ--ELALVKHlTVLENIFLGAeISrHGLLDYETMTlRCQKLLAQVNLPISP 136
Cdd:PRK13651 83 vleklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGP-VS-MGVSKEEAKK-RAAKYIELVGLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 137 DTRVG-DLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVI 215
Cdd:PRK13651 159 LQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
....*.
gi 489011807 216 RDGQHI 221
Cdd:PRK13651 239 KDGKII 244
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-212 |
5.57e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.98 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG-IYPHgsyEGEIIFAGETLqANHIRDTERKG 82
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASlISPT---SGTLLFEGEDI-STLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHlTVLENIFLGAEIsRHGLLDYETMtlrcQKLLAQVNLPISP-DTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:PRK10247 83 VSYCAQTPTLFGD-TVYDNLIFPWQI-RNQQPDPAIF----LDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489011807 162 RLLILDEPTASLTEQETATLLAIV-RDLQNHDIACIYISHKLNEVKAISDTI 212
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIhRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
277-483 |
5.70e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.30 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGrwQGEIFIDGQPVSISNCQQaiaHGIAMVPEDRkkdGIVPVM 355
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEkPT--EGQIFIDGEDVTHRSIQQ---RDICMVFQSY---ALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVGKNIT--LAALNQftgamssldDAAEQHciqqsiQRLKIKTSSPELA------IGRLSGGNQQKAILARCLLLNPRIL 427
Cdd:PRK11432 94 SLGENVGygLKMLGV---------PKEERK------QRVKEALELVDLAgfedryVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 428 ILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-212 |
5.79e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.42 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 14 FGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyegeiifaGETLQANHIRdterkgIAIIHQELALV 93
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS--------GTVRRAGGAR------VAYVPQRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 94 KHL--TVLENIFLGAeISRHGLLDYETM--TLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEP 169
Cdd:NF040873 68 DSLplTVRDLVAMGR-WARRGLWRRLTRddRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489011807 170 TASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTI 212
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-221 |
5.88e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.25 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 18 KAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANhirdTERKGIAIIHQELALVKHL- 96
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSS--GTITIAGYHITPE----TGNKNLKKLRKKVSLVFQFp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 97 -------TVLENIFLGAEisRHGLLDYETMTlRCQKLLAQVNLPIS-PDTRVGDLGLGQQQLVEIAKALNKQVRLLILDE 168
Cdd:PRK13641 95 eaqlfenTVLKDVEFGPK--NFGFSEDEAKE-KALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489011807 169 PTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-255 |
8.02e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 8.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 23 VSLRLNAGEVVSLCGENGSGKSTLMKVLcGIYpHGSYEGEIIFAGETLQANHIRDTERKgIAIIHQELALVKHLTVLENI 102
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKML-GRH-QPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 103 FLG-----AEISRHGLLDYEtmtlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQE 177
Cdd:PRK10575 107 AIGrypwhGALGRFGAADRE----KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 178 TATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDIITMMVGRELTALypsePHAHG 255
Cdd:PRK10575 183 QVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGIL----PHPAG 257
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
259-465 |
8.78e-15 |
|
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: 76.63 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSiSNCQQAIAHG 338
Cdd:TIGR02868 335 LELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-QGEVTLDGVPVS-SLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 339 IAMVPEDrkkdgiVPVMA--VGKNITLAALNqftGAMSSLDDAAEQHCIQQSIQRLK--IKTSSPELAIgRLSGGNQQKA 414
Cdd:TIGR02868 411 VSVCAQD------AHLFDttVRENLRLARPD---ATDEELWAALERVGLADWLRALPdgLDTVLGEGGA-RLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489011807 415 ILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQlVQQGIAVIVISSEL 465
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
5-250 |
9.76e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 9.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAG---ETLQANHIRDTERK 81
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE--PTRGQVLIDGvdiAKISDAELREVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 82 GIAIIHQELALVKHLTVLENIFLGAEISRHGLLDYETMTLRCqklLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDA---LRQVGLENYAHSYPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 162 RLLILDEPTASLTEQ-ETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ--HIGTRDA--SGMSEDDIIT 236
Cdd:PRK10070 184 DILLMDEAFSALDPLiRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEvvQVGTPDEilNNPANDYVRT 263
|
250
....*....|....
gi 489011807 237 MMVGRELTALYPSE 250
Cdd:PRK10070 264 FFRGVDISQVFSAK 277
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-229 |
9.79e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 9.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVL---CGIYPHGSYEGEIIFAGETLQANHIRDTE- 79
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEVTITGSIVYNGHNIYSPRTDTVDl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALVKhLTVLENIFLGAEISrhGLLDYETMTLRCQKLLAQVNLPISPDTRVGD--LGL--GQQQLVEIAK 155
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLK--GIKDKQVLDEAVEKSLKGASIWDEVKDRLHDsaLGLsgGQQQRVCIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 156 ALNKQVRLLILDEPTASL----TEQETATLLAIvrdlqNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGM 229
Cdd:PRK14239 162 VLATSPKIILLDEPTSALdpisAGKIEETLLGL-----KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
259-485 |
1.08e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.04 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTawhpVNRHIKRV-NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGrwQGEIFIDGQPVSisncqqaia 336
Cdd:PRK13548 3 LEARNLS----VRLGGRTLlDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPD--SGEVRLNGRPLA--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 337 hgiAMVPEDRKKdgivpvmavgkniTLAALNQ-------FT-------GAMS-SLDDAAEQHCIQQSIQRlkikTSSPEL 401
Cdd:PRK13548 68 ---DWSPAELAR-------------RRAVLPQhsslsfpFTveevvamGRAPhGLSRAEDDALVAAALAQ----VDLAHL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 402 AiGR----LSGGNQQKAILARCLL------LNPRILILDEPTRGIDIGAKYEIYKLINQLV-QQGIAVIVISSElpevLG 470
Cdd:PRK13548 128 A-GRdypqLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHD----LN 202
|
250
....*....|....*....
gi 489011807 471 L----SDRVLVMHEGRLKA 485
Cdd:PRK13548 203 LaaryADRIVLLHQGRLVA 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-219 |
1.13e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.36 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 9 NITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGS---YEGEIIFAGETLqaNHIRDTE--RKGI 83
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSgyrYSGDVLLGGRSI--FNYRDVLefRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKhLTVLENIFLGaeISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGD----LGLGQQQLVEIAKALNK 159
Cdd:PRK14271 104 GMLFQRPNPFP-MSIMDNVLAG--VRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 160 QVRLLILDEPTASLTEQETATLLAIVRDLQNHdIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGR 239
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-219 |
1.22e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.78 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFG----AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGI--YPHGSYEGEIIFAGETLQAnhIRD 77
Cdd:PRK11022 3 LLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGRVMAEKLEFNGQDLQR--ISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 TERKGI-----AIIHQE--LALVKHLTVLENIFLGAEISRHGllDYETMTLRCQKLLAQVNLPiSPDTRVG----DLGLG 146
Cdd:PRK11022 81 KERRNLvgaevAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGG--NKKTRRQRAIDLLNQVGIP-DPASRLDvyphQLSGG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 147 QQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQN-HDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
256-486 |
1.28e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 73.15 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLTAWHPVNRHIKRV-NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV-WPgrWQGEIFIDGQPVSisncqq 333
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTAlRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRP--TSGEVLIDGQDIS------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 334 aiahgiAMVPED-----RKKDGIV-------PVMAVGKNITLAALnqFTGAmsSLDDAAEQhcIQQSIQRLKI---KTSS 398
Cdd:COG1136 74 ------SLSERElarlrRRHIGFVfqffnllPELTALENVALPLL--LAGV--SRKERRER--ARELLERVGLgdrLDHR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 399 PelaiGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSElPEVLGLSDRVLV 477
Cdd:COG1136 142 P----SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIR 216
|
....*....
gi 489011807 478 MHEGRLKAN 486
Cdd:COG1136 217 LRDGRIVSD 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-255 |
1.37e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.76 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF----GAVKAVDNVSLRLNAGEVVSLCGENGSGKS----TLMKVLCGiypHGSYEGEIIFAGETL----- 70
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA---NGRIGGSATFNGREIlnlpe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 71 -QANHIRDTErkgIAIIHQE--LALVKHLTVLENifLGAEISRHGLLDYETMTLRCQKLLAQVNLPiSPDTRVG----DL 143
Cdd:PRK09473 89 kELNKLRAEQ---ISMIFQDpmTSLNPYMRVGEQ--LMEVLMLHKGMSKAEAFEESVRMLDAVKMP-EARKRMKmyphEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 144 GLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQhig 222
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR--- 239
|
250 260 270
....*....|....*....|....*....|....
gi 489011807 223 trdasgmseddiiTMMVGRELTALY-PSEPHAHG 255
Cdd:PRK09473 240 -------------TMEYGNARDVFYqPSHPYSIG 260
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
272-481 |
1.50e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.67 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 272 RHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQAiAHGIAMVPEDrKKDGI 351
Cdd:PRK15112 24 QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLHFGDYSYR-SQRIRMIFQD-PSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 352 VPVMAVGKNITLA-ALNqftgamSSLDDAAEQHCIQQSIQRLKIKTSSPELAIGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:PRK15112 101 NPRQRISQILDFPlRLN------TDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489011807 431 EPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
258-483 |
1.72e-14 |
|
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: 73.00 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLT-AWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV-WPGrwQGEIFIDGQPVS-ISNCQ-Q 333
Cdd:cd03258 1 MIELKNVSkVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPT--SGSVLVDGTDLTlLSGKElR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 334 AIAHGIAMVPE-----DRKKdgivpvmaVGKNITLAAlnqftgamsSLDDAAEQHCIQQSIQRLKI------KTSSPela 402
Cdd:cd03258 79 KARRRIGMIFQhfnllSSRT--------VFENVALPL---------EIAGVPKAEIEERVLELLELvgledkADAYP--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 403 iGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:cd03258 139 -AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
..
gi 489011807 482 RL 483
Cdd:cd03258 218 EV 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-219 |
2.29e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.44 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTF-GAVK-AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGETLQANHIRDTeRKG 82
Cdd:PRK11176 342 IEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY--DIDEGEILLDGHDLRDYTLASL-RNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELalvkHL---TVLENI-------FLGAEISRHGLLDYETMTLRcqkllaqvNLPISPDTRVGDLGL----GQQ 148
Cdd:PRK11176 419 VALVSQNV----HLfndTIANNIayarteqYSREQIEEAARMAYAMDFIN--------KMDNGLDTVIGENGVllsgGQR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 149 QLVEIAKALNKQVRLLILDEPTASL-TEQETATLLAIvRDLQNhDIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALdTESERAIQAAL-DELQK-NRTSLVIAHRLSTIEK-ADEILVVEDGE 555
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
277-484 |
2.52e-14 |
|
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: 71.84 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGeILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISncQQAIAHGIAMVPEDrkkdgivpvMA 356
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGQDVLKQ--PQKLRRRIGYLPQE---------FG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNITLAALNQFTGAMSSLDDAAEQHCIQQSIQRLKIKTSSPElAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:cd03264 83 VYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKK-KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489011807 437 DIGakyEIYKLINQLVQQGIAVIVI-SSELPE-VLGLSDRVLVMHEGRLK 484
Cdd:cd03264 162 DPE---ERIRFRNLLSELGEDRIVIlSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-200 |
2.54e-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: 70.65 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 20 VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEtlqanhirdterkgiaiihqelalvkhltvl 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGS--GRIGMPEG------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 100 ENIFLgaeISRHGLLdyETMTLRCqkllaQVNLPISpdtRVgdLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETA 179
Cdd:cd03223 64 EDLLF---LPQRPYL--PLGTLRE-----QLIYPWD---DV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|.
gi 489011807 180 TLLAIVRDlqnHDIACIYISH 200
Cdd:cd03223 129 RLYQLLKE---LGITVISVGH 146
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
2.64e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.30 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF-GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTeRKG 82
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS--GSVLIRGEPITKENIREV-RKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELA-LVKHLTVLENIFLGAeiSRHGLlDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:PRK13652 80 VGLVFQNPDdQIFSPTVEQDIAFGP--INLGL-DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 162 RLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQHIG 222
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
256-483 |
2.71e-14 |
|
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: 75.11 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLTAWHPVNRHIKR-VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRW---QGEIFIDGQP-VSISN 330
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEaVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpSGSILFDGQDlLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 331 CQ-QAI-AHGIAMV---PedrkkdgIV---PVMAVGKNI--TLAALNQFTGAmsslddAAEQHCIQqSIQRLKIKtsSPE 400
Cdd:COG4172 84 RElRRIrGNRIAMIfqeP-------MTslnPLHTIGKQIaeVLRLHRGLSGA------AARARALE-LLERVGIP--DPE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 401 LAIGR----LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRV 475
Cdd:COG4172 148 RRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRV 227
|
....*...
gi 489011807 476 LVMHEGRL 483
Cdd:COG4172 228 AVMRQGEI 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
253-484 |
2.99e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 71.67 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 253 AHGEeiLRVEHLTA-WHPvnrHIKRV-NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFgvwpgRW----QGEIFIDGQPV 326
Cdd:cd03369 3 EHGE--IEVENLSVrYAP---DLPPVlKNVSFKVKAGEKIGIVGRTGAGKSTLILALF-----RFleaeEGKIEIDGIDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 327 SISNCQqAIAHGIAMVPEDrkkdgivPVMavgknitlaalnqFTGAMSSLDDAAEQHCIQQSIQRLKIKTSSPELaigrl 406
Cdd:cd03369 73 STIPLE-DLRSSLTIIPQD-------PTL-------------FSGTIRSNLDPFDEYSDEEIYGALRVSEGGLNL----- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 407 SGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPEVLGLsDRVLVMHEGRLK 484
Cdd:cd03369 127 SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
277-483 |
3.16e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.42 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPG---RWQGEIFIDGQPVSISNCQQAIAHGIAMVPedRKKDGIVP 353
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrQTAGRVLLDGKPVAPCALRGRKIATIMQNP--RSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 354 VMAVGKNITLAALNQFTgamsslDDAAEQHCIQ----QSIQRLkiktssPELAIGRLSGGNQQKAILARCLLLNPRILIL 429
Cdd:PRK10418 97 TMHTHARETCLALGKPA------DDATLTAALEavglENAARV------LKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 430 DEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQkRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-219 |
3.74e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 23 VSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAGETLqanhirDTERKGIAIIHQELALV-------- 93
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ---KGAVLWQGKPL------DYSKRGLLALRQQVATVfqdpeqqi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 94 -------------KHLTVLEniflgAEISRHglLDyETMTL-RCQKLLAQvnlPISPdtrvgdLGLGQQQLVEIAKALNK 159
Cdd:PRK13638 91 fytdidsdiafslRNLGVPE-----AEITRR--VD-EALTLvDAQHFRHQ---PIQC------LSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 160 QVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-219 |
4.14e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.14 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 22 NVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHGsyeGEIIFAGETL-QANHirDTERKGIAIIHQELALVKHlTVL 99
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTG---GQVLLDGVPLvQYDH--HYLHRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 100 ENIflgaeisRHGLLDYETMTLRCQKLLAQV-----NLPISPDTRVGDLG----LGQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:TIGR00958 573 ENI-------AYGLTDTPDEEIMAAAKAANAhdfimEFPNGYDTEVGEKGsqlsGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489011807 171 ASLTEQETATLLAivrDLQNHDIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:TIGR00958 646 SALDAECEQLLQE---SRSRASRTVLLIAHRLSTVER-ADQILVLKKGS 690
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
258-483 |
4.48e-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: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTAWHPVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwqGEIFIDGQPVS-ISNcqqai 335
Cdd:COG2884 1 MIRFENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPTS--GQVLVNGQDLSrLKR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 336 ahgiAMVPEDRKKDGIV-------PVMAVGKNITLAAlnQFTGAmsSLDDAAEQhcIQQSIQRL----KIKTSSPELaig 404
Cdd:COG2884 72 ----REIPYLRRRIGVVfqdfrllPDRTVYENVALPL--RVTGK--SRKEIRRR--VREVLDLVglsdKAKALPHEL--- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 405 rlSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:COG2884 139 --SGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-188 |
4.50e-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: 74.70 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 15 GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHiRDTERKGIAIIHQElALVK 94
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD--PLQGEVTLDGVPVSSLD-QDEVRRRVSVCAQD-AHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 95 HLTVLENIFLGAE----------ISRHGLLDYetmtLRcqkllaqvNLPISPDTRVGDLGL----GQQQLVEIAKALNKQ 160
Cdd:TIGR02868 422 DTTVRENLRLARPdatdeelwaaLERVGLADW----LR--------ALPDGLDTVLGEGGArlsgGERQRLALARALLAD 489
|
170 180
....*....|....*....|....*...
gi 489011807 161 VRLLILDEPTASLteqETATLLAIVRDL 188
Cdd:TIGR02868 490 APILLLDEPTEHL---DAETADELLEDL 514
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
253-485 |
4.71e-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: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 253 AHGEEILRVEHLTAWHPVNRHIKRV-NDVSFSLRRGE---ILG------------IAGLVGAGRteavqclfgvwpgrwq 316
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTAlDDVSLTVAAGEfvaLVGpsgcgkstllrlIAGLEKPTS---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 317 GEIFIDGQPVSisncqqAIAHGIAMVPEDrkkDGIVPVMAVGKNITLAAlnQFTGAmsSLDDAAEQhcIQQSIQRLKIK- 395
Cdd:COG1116 66 GEVLVDGKPVT------GPGPDRGVVFQE---PALLPWLTVLDNVALGL--ELRGV--PKAERRER--ARELLELVGLAg 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 396 --TSSPelaiGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLS 472
Cdd:COG1116 131 feDAYP----HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLA 206
|
250
....*....|....*
gi 489011807 473 DRVLVMHE--GRLKA 485
Cdd:COG1116 207 DRVVVLSArpGRIVE 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-236 |
5.69e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.91 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF----GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGETLQANHIRDTE 79
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RK-----GIAIIHQE----LALVKHL--TVLENI----FLGAEISRHGLldyetMTLRCQKLLAQVNLPISPDTRVG--- 141
Cdd:PRK15093 83 RRklvghNVSMIFQEpqscLDPSERVgrQLMQNIpgwtYKGRWWQRFGW-----RKRRAIELLHRVGIKDHKDAMRSfpy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 142 DLGLGQQQLVEIAKALNKQVRLLILDEPTASLteqETATLLAIVRDL----QNHDIACIYISHKLNEVKAISDTICVIRD 217
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAM---EPTTQAQIFRLLtrlnQNNNTTILLISHDLQMLSQWADKINVLYC 234
|
250
....*....|....*....
gi 489011807 218 GQHIgtrdASGMSEDDIIT 236
Cdd:PRK15093 235 GQTV----ETAPSKELVTT 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-219 |
6.95e-14 |
|
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: 74.66 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 7 MKNITKTF--GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANhiRDTERKGIA 84
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLVGGKDIETN--LDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAEISRHgllDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLL 164
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGR---SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDLQNHDiACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKYRSGR-TIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
258-483 |
7.16e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 72.82 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTawhpvnrhiKR------VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSisnc 331
Cdd:COG3842 5 ALELENVS---------KRygdvtaLDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD-SGRILLDGRDVT---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 332 qqaiahgiAMVPEDRkkD-GIV-------PVMAVGKNItlaalnqftgA----MSSLDDAAEQHCIQQSIQRLKIktssP 399
Cdd:COG3842 71 --------GLPPEKR--NvGMVfqdyalfPHLTVAENV----------AfglrMRGVPKAEIRARVAELLELVGL----E 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 400 ELA---IGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRV 475
Cdd:COG3842 127 GLAdryPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRI 206
|
....*...
gi 489011807 476 LVMHEGRL 483
Cdd:COG3842 207 AVMNDGRI 214
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
281-484 |
1.05e-13 |
|
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: 70.28 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 281 SFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGrwQGEIFIDGQPVSISNCQQaiaHGIAMVPEDrkkDGIVPVMAVGK 359
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGfIEPA--SGSIKVNDQSHTGLAPYQ---RPVSMLFQE---NNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 360 NITLaalnqftGAMSSLD-DAAEQHCIQQSIQRLKIKTSSPELAiGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDI 438
Cdd:TIGR01277 90 NIGL-------GLHPGLKlNAEQQEKVVDAAQQVGIADYLDRLP-EQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489011807 439 GAKYEIYKLINQLV-QQGIAVIVISSELPEVLGLSDRVLVMHEGRLK 484
Cdd:TIGR01277 162 LLREEMLALVKQLCsERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
258-482 |
1.10e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 70.79 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTAW---HPVnrhikrVNDVSFSLRRGEILGIAGLVGAGRT---------EAVQclfgvwpgrwQGEIFIDGQP 325
Cdd:COG1126 1 MIEIENLHKSfgdLEV------LKGISLDVEKGEVVVIIGPSGSGKStllrcinllEEPD----------SGTITVDGED 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 326 VSISNCQqaiahgiamVPEDRKKDGIV-------PVMAVGKNITLA-----------ALNQftgAMSSLD-----DAAEQ 382
Cdd:COG1126 65 LTDSKKD---------INKLRRKVGMVfqqfnlfPHLTVLENVTLApikvkkmskaeAEER---AMELLErvglaDKADA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 383 HciqqsiqrlkiktssPelaiGRLSGGNQQK-AIlARCLLLNPRILILDEPTRGID---IGakyEIYKLINQLVQQGIAV 458
Cdd:COG1126 133 Y---------------P----AQLSGGQQQRvAI-ARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTM 189
|
250 260
....*....|....*....|....*..
gi 489011807 459 IVISSELP---EVlglSDRVLVMHEGR 482
Cdd:COG1126 190 VVVTHEMGfarEV---ADRVVFMDGGR 213
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
279-498 |
1.16e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.11 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFI---DGQPVSIsncqqaiahgIAMVPEDRK-------- 347
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD-AGEVHYrmrDGQLRDL----------YALSEAERRrllrtewg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 348 ------KDGIVPVMAVGKNI--TLAALnqftGA--MSSLDDAAeqhciQQSIQRLKIKTSSPELAIGRLSGGNQQKAILA 417
Cdd:PRK11701 93 fvhqhpRDGLRMQVSAGGNIgeRLMAV----GArhYGDIRATA-----GDWLERVEIDAARIDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLV-QQGIAVIVISSELPEVLGLSDRVLVMHEGRlkanLVNQHLTqEQ 496
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVrELGLAVVIVTHDLAVARLLAHRLLVMKQGR----VVESGLT-DQ 238
|
..
gi 489011807 497 VM 498
Cdd:PRK11701 239 VL 240
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
277-482 |
1.44e-13 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 70.34 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLfgvwPGRW---QGEIFIDGQPVSISNCQQAIAHgIAMVPEDRkkdgIVP 353
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLI----PRFYdvdSGRILIDGHDVRDYTLASLRRQ-IGLVSQDV----FLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 354 VMAVGKNITLAALNQftgAMSSLDDAAEQHCIQQSIQRLkiktssPE---LAIG----RLSGGNQQKAILARCLLLNPRI 426
Cdd:cd03251 89 NDTVAENIAYGRPGA---TREEVEEAARAANAHEFIMEL------PEgydTVIGergvKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 427 LILDEPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELPEVLGlSDRVLVMHEGR 482
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGK 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-113 |
1.55e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.11 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTF----------------------GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgS 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE--P 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 59 YEGEIifagetlqanhirdtERKGI--------AIIHQElalvkhLTVLENIFLGAEIsrHGL 113
Cdd:COG1134 79 TSGRV---------------EVNGRvsallelgAGFHPE------LTGRENIYLNGRL--LGL 118
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-219 |
1.61e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 6 EMKNITKTF----------GAVK-----------AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGI-YPHGsyeGEI 63
Cdd:COG4586 3 EVENLSKTYrvyekepglkGALKglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIlVPTS---GEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 64 IFAGETLQANhiRDTERKGIAIIH-QELALVKHLTVLENIFLGAEIsrHGL--------LDYETMTLRCQKLLaqvnlpi 134
Cdd:COG4586 80 RVLGYVPFKR--RKEFARRIGVVFgQRSQLWWDLPAIDSFRLLKAI--YRIpdaeykkrLDELVELLDLGELL------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 135 spDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASL--TEQETatllaiVRDL-----QNHDIACIYISHKLNEVKA 207
Cdd:COG4586 149 --DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLdvVSKEA------IREFlkeynRERGTTILLTSHDMDDIEA 220
|
250
....*....|..
gi 489011807 208 ISDTICVIRDGQ 219
Cdd:COG4586 221 LCDRVIVIDHGR 232
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-200 |
1.68e-13 |
|
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: 68.99 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 15 GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHGsyeGEIIFAGETLqanhirDTERKGIAIIHQELALV 93
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLrPQS---GAVLIDGEPL------DYSRKGLLERRQRVGLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 94 KH--------LTVLENIFLGAeisRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLI 165
Cdd:TIGR01166 74 FQdpddqlfaADVDQDVAFGP---LNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 489011807 166 LDEPTASLTEQETATLLAIVRDLQNHDIACIYISH 200
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
1.91e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.49 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF-GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRDTE-RK 81
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTS--GEVLIKGEPIKYDKKSLLEvRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 82 GIAIIHQE-----LAlvkhLTVLENIFLGaeiSRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:PRK13639 79 TVGIVFQNpddqlFA----PTVEEDVAFG---PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 157 LNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGT 223
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
267-482 |
2.07e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 71.28 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 267 WHPvNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWP---GR--WQGEIFIDGQPVSIsncqQAIAHGIAM 341
Cdd:PRK15079 28 WQP-PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKatdGEvaWLGKDLLGMKDDEW----RAVRSDIQM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 342 VPEDrKKDGIVPVMAVGkNITLAALNQFTGAMSSLDdaaeqhcIQQSIQRLKIKTSSPELAIGR----LSGGNQQKAILA 417
Cdd:PRK15079 103 IFQD-PLASLNPRMTIG-EIIAEPLRTYHPKLSRQE-------VKDRVKAMMLKVGLLPNLINRypheFSGGQCQRIGIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
255-483 |
2.12e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 71.30 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 255 GEEILRVEHLTAWHPVNR--------HIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPV 326
Cdd:COG4608 4 AEPLLEVRDLKKHFPVRGglfgrtvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPT-SGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 327 sisncqqAIAHGIAMVPEdRKKDGIV---------PVMAVGKNITLAALNQftgamsSLDDAAEQhciQQSIQRLKIKTS 397
Cdd:COG4608 83 -------TGLSGRELRPL-RRRMQMVfqdpyaslnPRMTVGDIIAEPLRIH------GLASKAER---RERVAELLELVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 398 SPELAIGR----LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLS 472
Cdd:COG4608 146 LRPEHADRypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHIS 225
|
250
....*....|.
gi 489011807 473 DRVLVMHEGRL 483
Cdd:COG4608 226 DRVAVMYLGKI 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
279-483 |
2.52e-13 |
|
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: 69.44 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGqpvsisncqqaiaHGIAMVPED--RKKDGIVPVMA 356
Cdd:cd03252 20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-NGRVLVDG-------------HDLALADPAwlRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNITLA---ALNQFTGAMSSLDDAAEQHCIQQSIQRLKI--KTSSPELAIGrLSGGNQQKAILARCLLLNPRILILDE 431
Cdd:cd03252 86 VLFNRSIRdniALADPGMSMERVIEAAKLAGAHDFISELPEgyDTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 432 PTRGIDigakYEIYKLINQLVQQ---GIAVIVISSELPEVLGlSDRVLVMHEGRL 483
Cdd:cd03252 165 ATSALD----YESEHAIMRNMHDicaGRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
277-481 |
2.70e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.17 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQqaiahgiamvpEDRKKDGIV---P 353
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-SGEIFYNNQAITDDNFE-----------KLRKHIGIVfqnP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 354 VmavgknitlaalNQFTGAMSSLDDA--AEQHCIQQSIQRLKIKTSSPELAI--------GRLSGGNQQKAILARCLLLN 423
Cdd:PRK13648 93 D------------NQFVGSIVKYDVAfgLENHAVPYDEMHRRVSEALKQVDMleradyepNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 424 PRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGlSDRVLVMHEG 481
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-219 |
2.82e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFG----AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIyPHGSyEGEIIFAGETLqanHIRDTE 79
Cdd:PRK10584 6 IVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL-DDGS-SGEVSLVGQPL---HQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 R------KGIAIIHQELALVKHLTVLENIFLGAEIsrHGLLDYETMTlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEI 153
Cdd:PRK10584 81 AraklraKHVGFVFQSFMLIPTLNALENVELPALL--RGESSRQSRN-GAKALLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 154 AKALNKQVRLLILDEPTASLTEQETATLLAIVRDLqNHDIAC--IYISHKlNEVKAISDTICVIRDGQ 219
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL-NREHGTtlILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
3.64e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.76 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTF-GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTe 79
Cdd:PRK13647 1 MDNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYL--PQRGRVKVMGREVNAENEKWV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELA-LVKHLTVLENIFLGAeisRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:PRK13647 78 RSKVGLVFQDPDdQVFSSTVWDDVAFGP---VNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 159 KQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDII 235
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-218 |
3.94e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.83 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 7 MKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIyphgsyegEIIFAGETL----QANHIRDTERkG 82
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL--------EDITSGDLFigekRMNDVPPAER-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHLTVLENIFLG--------AEISRHglLDYETMTLRCQKLLaqvnlpispDTRVGDLGLGQQQLVEIA 154
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGlklagakkEEINQR--VNQVAEVLQLAHLL---------DRKPKALSGGQRQRVAIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 155 KALNKQVRLLILDEP----TASLTEQETATLLAIVRDLQNhdiACIYISHKLNEVKAISDTICVIRDG 218
Cdd:PRK11000 146 RTLVAEPSVFLLDEPlsnlDAALRVQMRIEISRLHKRLGR---TMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
274-483 |
3.99e-13 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 68.59 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 274 IKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV-WPGRwqGEIFIDGQPVSIsncqqaiAHGIAmVPEDRKKDGIV 352
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTS--GTIRVNGQDVSD-------LRGRA-IPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 -------PVMAVGKNITLAAlnQFTGAmsSLDDAAEQhcIQQSIQRLKIKTSSPELAIGrLSGGNQQKAILARCLLLNPR 425
Cdd:cd03292 84 fqdfrllPDRNVYENVAFAL--EVTGV--PPREIRKR--VPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 426 ILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-219 |
4.79e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.46 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 24 SLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGEtlqaNHIRDT-ERKGIAIIHQELALVKHLTVLENI 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPAS--GSLTLNGQ----DHTTTPpSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 103 FLGAEisrHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLT---EQETA 179
Cdd:PRK10771 93 GLGLN---PGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489011807 180 TLLAIVrdLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK10771 170 TLVSQV--CQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-219 |
4.91e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.31 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 22 NVSLRLNAGEVVSLCGENGSGKSTLMKVL---CGIYPHG-SYEGEIIFAGETL-QANHIRdtERKGIAIIHQELALVKHL 96
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSKiKVDGKVLYFGKDIfQIDAIK--LRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 97 TVLENIflGAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRV----GDLGLGQQQLVEIAKALNKQVRLLILDEPTAS 172
Cdd:PRK14246 106 SIYDNI--AYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspaSQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489011807 173 LTEQETATLLAIVRDLQNhDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK14246 184 IDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGE 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-218 |
5.46e-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: 67.94 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGiypHGSYE---GEIIFAGETLQANHIRDTERK 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---HPKYEvteGEILFKGEDITDLPPEERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 82 GIAIIHQ---ELALVKHLTVLENI---FLGAEISRhglldyetmtlrcqkllaqvnlpispdtrvgdlglgqqqlVEIAK 155
Cdd:cd03217 78 GIFLAFQyppEIPGVKNADFLRYVnegFSGGEKKR----------------------------------------NEILQ 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 156 ALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHK---LNEVKAisDTICVIRDG 218
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIKP--DRVHVLYDG 181
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
264-482 |
5.49e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.99 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 264 LTAWHPVNR-------HIKRVNDVSFSLRRGEILGIAGLVGAGR-TEAVQCLFGVWPGrwQGEIFIDGQPVSISN--CQQ 333
Cdd:PRK11308 11 LKKHYPVKRglfkperLVKALDGVSFTLERGKTLAVVGESGCGKsTLARLLTMIETPT--GGELYYQGQDLLKADpeAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 334 AIAHGIAMVPED-------RKKdgivpvmaVGKniTLA---ALNqftgamSSLDDAAEQHCIQQSIQRLKIKtssPELAi 403
Cdd:PRK11308 89 LLRQKIQIVFQNpygslnpRKK--------VGQ--ILEeplLIN------TSLSAAERREKALAMMAKVGLR---PEHY- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 404 GR----LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVM 478
Cdd:PRK11308 149 DRyphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVM 228
|
....
gi 489011807 479 HEGR 482
Cdd:PRK11308 229 YLGR 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-225 |
5.65e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.36 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF-GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGETLqaNHIRDTE--- 79
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI--ERPSAGKIWFSGHDI--TRLKNREvpf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 -RKGIAIIHQELALVKHLTVLENIFLGAEISRHGLldyETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALN 158
Cdd:PRK10908 77 lRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASG---DDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 159 KQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRD 225
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-219 |
5.90e-13 |
|
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: 66.32 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETlqanhirdterkGIA 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE--PDEGIVTWGSTV------------KIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQelalvkhltvleniflgaeisrhglldyetmtlrcqkllaqvnlpispdtrvgdLGLGQQQLVEIAKALNKQVRLL 164
Cdd:cd03221 67 YFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 165 ILDEPTASLteqETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03221 93 LLDEPTNHL---DLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-200 |
5.99e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 20 VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIF-AGETL----QANHI-----RDterkgiAIIHQE 89
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGS--GRIARpAGARVlflpQRPYLplgtlRE------ALLYPA 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 90 LAlvkhltvleniflgAEISRHglldyetmtlRCQKLLAQVNLPiSPDTRVGD-------LGLGQQQLVEIAKALNKQVR 162
Cdd:COG4178 451 TA--------------EAFSDA----------ELREALEAVGLG-HLAERLDEeadwdqvLSLGEQQRLAFARLLLHKPD 505
|
170 180 190
....*....|....*....|....*....|....*...
gi 489011807 163 LLILDEPTASLTEQETATLLAIVRDlQNHDIACIYISH 200
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-221 |
7.21e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.01 E-value: 7.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF--GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAGETLQANHiRDTER 80
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWdPQ---QGEILLNGQPIADYS-EAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKHlTVLENIFLGA-EISRHGLLDyetmtlrcqkLLAQVNL------PISPDTRVGDLGL----GQQQ 149
Cdd:PRK11160 414 QAISVVSQRVHLFSA-TLRDNLLLAApNASDEALIE----------VLQQVGLeklledDKGLNAWLGEGGRqlsgGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 150 LVEIAKALNKQVRLLILDEPTASL---TEQEtatllaIVRDLQNH--DIACIYISHKLNEVKAIsDTICVIRDGQHI 221
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLdaeTERQ------ILELLAEHaqNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
280-500 |
9.49e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.28 E-value: 9.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 280 VSFSLRRGEILGIAGLVGAGRTEAVQCLfgvwpGRWQ----GEIFIDGQPVSISNcQQAIAHGIAMVPED-RKKDGIV-- 352
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKML-----GRHQppseGEILLDAQPLESWS-SKAFARKVAYLPQQlPAAEGMTvr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 PVMAVGKNITLAALNQFTgamsslddAAEQHCIQQSIQRLKIKTSSPELaIGRLSGGNQQKAILARCLLLNPRILILDEP 432
Cdd:PRK10575 104 ELVAIGRYPWHGALGRFG--------AADREKVEEAISLVGLKPLAHRL-VDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 433 TRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRLKANLVNQHLTQEQVMEA 500
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQ 243
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-232 |
1.01e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.94 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 20 VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgsYEGEIIFAGETL------QANHIRdterkgiAIIHQELALV 93
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP---GQGEILLNGRPLsdwsaaELARHR-------AYLSQQQSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 94 KHLTVLENIFLgaeiSRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKAL-------NKQVRLLIL 166
Cdd:COG4138 82 FAMPVFQYLAL----HQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 167 DEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIgtrdASGMSED 232
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV----ASGETAE 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
267-483 |
1.14e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.96 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 267 WHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV-WPGrwQGEIFIDGqpvsisncqqaiahgiaMVPED 345
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIlVPT--SGEVRVLG-----------------YVPFK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 346 RKKdgivpvmAVGKNIT------------LAALNQFT--GAMSSLDDAAEQHCIQQSIQRLKIKtsspEL---AIGRLSG 408
Cdd:COG4586 89 RRK-------EFARRIGvvfgqrsqlwwdLPAIDSFRllKAIYRIPDAEYKKRLDELVELLDLG----ELldtPVRQLSL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 409 GNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-173 |
1.17e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETlqanhIRDTE-RKGI 83
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP--PAAGTIKLDGGD-----IDDPDvAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AII-HQElALVKHLTVLENI-----FLGAEisrhglldyETMTLRCqklLAQVNLPISPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:PRK13539 76 HYLgHRN-AMKPALTVAENLefwaaFLGGE---------ELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLL 142
|
170
....*....|....*.
gi 489011807 158 NKQVRLLILDEPTASL 173
Cdd:PRK13539 143 VSNRPIWILDEPTAAL 158
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
248-500 |
1.50e-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: 69.75 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 248 PSEPHAHGEEILRVE------HLTAWHPvNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCL--FgVWPGrwQGEI 319
Cdd:TIGR02203 314 PPEKDTGTRAIERARgdvefrNVTFRYP-GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIprF-YEPD--SGQI 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 320 FIDGQPVSISNCQQAIAHgIAMVPEDrkkdgivpVM----AVGKNITLAALNQFtgAMSSLDDAAEQHCIQQSIQRLKIK 395
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQ-VALVSQD--------VVlfndTIANNIAYGRTEQA--DRAEIERALAAAYAQDFVDKLPLG 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 396 TSSPelaIG----RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELPEVLGl 471
Cdd:TIGR02203 459 LDTP---IGengvLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEK- 533
|
250 260
....*....|....*....|....*....
gi 489011807 472 SDRVLVMHEGRLKanlvnQHLTQEQVMEA 500
Cdd:TIGR02203 534 ADRIVVMDDGRIV-----ERGTHNELLAR 557
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-221 |
1.61e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 67.95 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLqanhirDTERKGIAIIHQELALVKH--- 95
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS--GRILFDGKPI------DYSRKGLMKLRESVGMVFQdpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 96 -----LTVLENIFLGAeiSRHGLLDYETMTlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:PRK13636 93 nqlfsASVYQDVSFGA--VNLKLPEDEVRK-RVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489011807 171 ASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-219 |
1.68e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.69 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 22 NVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGS-YEGEIIFAGETLQANHIrdteRKGIAIIHQELALVKHLTVLE 100
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPIDAKEM----RAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 101 NIFLGAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGL------GQQQLVEIAKALNKQVRLLILDEPTASLT 174
Cdd:TIGR00955 119 HLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkglsgGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489011807 175 EQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:TIGR00955 199 SFMAYSVVQVLKGLaQKGKTIICTIHQPSSELFELFDKIILMAEGR 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-200 |
2.86e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGsyEGEIIFAGET----LQANHIRDTE 79
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLD--DGRIIYEQDLivarLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 -------RKGIA-------IIHQELALV------KHLTVLENifLGAEISRHGLLDYETmtlRCQKLLAQVNLpiSPDTR 139
Cdd:PRK11147 81 gtvydfvAEGIEeqaeylkRYHDISHLVetdpseKNLNELAK--LQEQLDHHNLWQLEN---RINEVLAQLGL--DPDAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 140 VGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNhdiACIYISH 200
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISH 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
256-500 |
3.07e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 66.65 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLTawhpVNRHIKRV-NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwQGEIFIDGQPvsisncqq 333
Cdd:COG1119 1 DPLLELRNVT----VRRGGKTIlDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTY-GNDVRLFGER-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 334 aiaHGIAMVPEDRKKDGIV--------PVMAVGKNITLaalnqfTGAMSSLD-----DAAEQHCIQQSIQRLKIKtsspE 400
Cdd:COG1119 68 ---RGGEDVWELRKRIGLVspalqlrfPRDETVLDVVL------SGFFDSIGlyrepTDEQRERARELLELLGLA----H 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 401 LA---IGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQG-IAVIVISSELPEVLGLSDRVL 476
Cdd:COG1119 135 LAdrpFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVL 214
|
250 260
....*....|....*....|....*
gi 489011807 477 VMHEGRLKAN-LVNQHLTQEQVMEA 500
Cdd:COG1119 215 LLKDGRVVAAgPKEEVLTSENLSEA 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
277-483 |
3.38e-12 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 65.74 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVsisNCQQAIAHGIAMVPEDRkkdGIVPVMA 356
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-SGRIYIGGRDV---TDLPPKDRDIAMVFQNY---ALYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNITLAaLNQFTGAMSSLD----DAAEQHCIQQSIQRLkiktssPElaigRLSGGNQQKAILARCLLLNPRILILDEP 432
Cdd:cd03301 89 VYDNIAFG-LKLRKVPKDEIDervrEVAELLQIEHLLDRK------PK----QLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489011807 433 TRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-214 |
3.43e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTF----------GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGE-T 69
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIET--PTGGELYYQGQdL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 70 LQANHI-RDTERKGIAIIHQ----ELALVKHL-TVLE-----NIFLGAEISRHglldyetmtlRCQKLLAQVNLPISPDT 138
Cdd:PRK11308 80 LKADPEaQKLLRQKIQIVFQnpygSLNPRKKVgQILEeplliNTSLSAAERRE----------KALAMMAKVGLRPEHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 139 RV-----GdlglGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTI 212
Cdd:PRK11308 150 RYphmfsG----GQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEV 225
|
..
gi 489011807 213 CV 214
Cdd:PRK11308 226 MV 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-233 |
4.08e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.71 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQA--NHIRDTERK 81
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH--GEILFDGENIPAmsRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 82 GIAIIHQELALVKHLTVLENIflGAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQV 161
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNV--AYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 162 RLLILDEPtasLTEQETATLLAIVR--DLQNH--DIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDD 233
Cdd:PRK11831 163 DLIMFDEP---FVGQDPITMGVLVKliSELNSalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
256-482 |
4.45e-12 |
|
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: 65.53 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLT---AWHpvNRHIKR---VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGrwQGEIFI--DGQPV 326
Cdd:COG4778 2 TTLLEVENLSktfTLH--LQGGKRlpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYlPD--SGSILVrhDGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 327 SISncqQAIAHGIAMVpedRKKdgivpvmavgkniTLAALNQFTGAM---SSLD-----------DAAEQHCIQQSI-QR 391
Cdd:COG4778 78 DLA---QASPREILAL---RRR-------------TIGYVSQFLRVIprvSALDvvaepllergvDREEARARARELlAR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 392 LKIKTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGL 471
Cdd:COG4778 139 LNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAV 218
|
250
....*....|.
gi 489011807 472 SDRVLVMHEGR 482
Cdd:COG4778 219 ADRVVDVTPFS 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
257-492 |
5.08e-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: 68.89 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 257 EILRVEHLTAWHPVNRHiKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVwPGRWQGEIFIDGQPV--SISNCQQA 334
Cdd:TIGR01257 1936 DILRLNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGD-TTVTSGDATVAGKSIltNISDVHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 335 IAHgiamVPEdrkKDGIVPVMAVGKNITLAAlnqftgAMSSLDDAAEQHCIQQSIQRLKIKTSSPELAiGRLSGGNQQKA 414
Cdd:TIGR01257 2014 MGY----CPQ---FDAIDDLLTGREHLYLYA------RLRGVPAEEIEKVANWSIQSLGLSLYADRLA-GTYSGGNKRKL 2079
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 415 ILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKANLVNQHL 492
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
256-501 |
5.12e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.30 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLTAWHPVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQaI 335
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ-RGRVKVMGREVNAENEKW-V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 336 AHGIAMVPEDrkKDGIVPVMAVGKNITLAALNQFTGAmSSLDDAAEQHCIQQSIQRLKIKtsspelAIGRLSGGNQQKAI 415
Cdd:PRK13647 78 RSKVGLVFQD--PDDQVFSSTVWDDVAFGPVNMGLDK-DEVERRVEEALKAVRMWDFRDK------PPYHLSYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 416 LARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKANLVNQHLTQE 495
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
....*.
gi 489011807 496 QVMEAA 501
Cdd:PRK13647 229 DIVEQA 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-173 |
5.36e-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: 65.37 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 17 VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG-IYPHGSYEGEIIFAGETLQanhiRDTERKGIAIIHQELALVKH 95
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTTSGQILFNGQPRK----PDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 96 LTVLE-----NIFLGAEISRHGLLDYETMTLRcqklLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:cd03234 96 LTVREtltytAILRLPRKSSDAIRKKRVEDVL----LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
...
gi 489011807 171 ASL 173
Cdd:cd03234 172 SGL 174
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
279-513 |
5.81e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGvWPGRWQGEIFIDGQPVsisncQQAIAHG-IAMVPEDRKKDGIVPVMAv 357
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMG-FVRLASGKISILGQPT-----RQALQKNlVAYVPQSEEVDWSFPVLV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 358 gKNITLAALNQFTGAMSsLDDAAEQHCIQQSIQRLKIkTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGID 437
Cdd:PRK15056 98 -EDVVMMGRYGHMGWLR-RAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 438 IGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKANLVNQHLTQEQVMEAALRSERHV-----EEHV 512
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFSGVLRHValngsEESI 254
|
.
gi 489011807 513 V 513
Cdd:PRK15056 255 I 255
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-219 |
6.93e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.47 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGiypHGSYE---GEIIFAGETLqanhirdTE-- 79
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG---HPKYEvtsGSILLDGEDI-------LEls 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 -----RKGIAIIHQELALVKHLTVLEniFLGAEIS--RHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGL--GQQQL 150
Cdd:COG0396 71 pderaRAGIFLAFQYPVEIPGVSVSN--FLRTALNarRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEGFsgGEKKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 151 VEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHK---LNEVKAisDTICVIRDGQ 219
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYIKP--DFVHVLVDGR 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
277-485 |
7.21e-12 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 63.87 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSisNCQQAIAHGIAMVPedrkkdgivpvma 356
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ-QGEITLDGVPVS--DLEKALSSLISVLN------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 vgknitlaalnqftgamsslddaaeqhciqqsiQRLKIKTSSPELAIG-RLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:cd03247 82 ---------------------------------QRPYLFDTTLRNNLGrRFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489011807 436 IDIGAKYEIYKLINQlVQQGIAVIVISSELpevLGLS--DRVLVMHEGRLKA 485
Cdd:cd03247 129 LDPITERQLLSLIFE-VLKDKTLIWITHHL---TGIEhmDKILFLENGKIIM 176
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
275-483 |
1.01e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 65.62 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 275 KRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGRwqGEIFIDGQPVSISNCQQAIAhgiamvpEDRKKDGIV- 352
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkPSS--GTITIAGYHITPETGNKNLK-------KLRKKVSLVf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 --PVMAVGKNITLAALNQFTGAMSSLDDAAEQHCIQQsIQRLKIKTSSPELAIGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:PRK13641 92 qfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKW-LKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489011807 431 EPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-219 |
1.33e-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: 64.09 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 15 GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIfagetlqanhirdTERKGIAIIHQELALVK 94
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDS--GTVT-------------VRGRVSSLLGLGGGFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 95 HLTVLENIFLGAEIsrHGLLDYEtMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTAS-- 172
Cdd:cd03220 98 ELTGRENIYLNGRL--LGLSRKE-IDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVgd 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489011807 173 LTEQETAtlLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03220 175 AAFQEKC--QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
277-481 |
1.52e-11 |
|
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: 64.02 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV-WPGrwQGEIFIDGQPVSISNCQQAIAHgiamvpedrKKDGIVPVM 355
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPT--SGGVILEGKQITEPGPDRMVVF---------QNYSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVGKNITLAAlnqfTGAMSSLDDAAEQHCIQQSIQRLKIkTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:TIGR01184 70 TVRENIALAV----DRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489011807 436 IDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
278-482 |
1.53e-11 |
|
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: 64.48 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 278 NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFgvwpgRW----QGEIFIDGQPVSISNCQQAIAHgIAMVPEDrkkdgivP 353
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLE-----RFydptSGEILLDGVDIRDLNLRWLRSQ-IGLVSQE-------P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 354 V---MAVGKNITLAAlnqFTGAMSSLDDAAEQHCIQQSIQRLKIKTSSPelaIG----RLSGGNQQKAILARCLLLNPRI 426
Cdd:cd03249 87 VlfdGTIAENIRYGK---PDATDEEVEEAAKKANIHDFIMSLPDGYDTL---VGergsQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 427 LILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPEVLGlSDRVLVMHEGR 482
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-201 |
1.65e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 20 VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANhiRDTERKGIAIIHQELALVKHLTVL 99
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEK--GEILFERQSIKKD--LCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 100 ENIFLGAEISRHGLLDYETMTLRcqKLLAQVNLPispdtrVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETA 179
Cdd:PRK13540 93 ENCLYDIHFSPGAVGITELCRLF--SLEHLIDYP------CGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 489011807 180 TLLAIVRDLQNHDIACIYISHK 201
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
277-483 |
1.82e-11 |
|
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: 64.28 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQaiaHGIAMVPEDRkkdGIVPVMA 356
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD-SGTILFGGEDATDVPVQE---RNVGFVFQHY---ALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNITLAALNQFTGAMSSLDDAAEQ-HCIQQSIQRLKIKTSSPElaigRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:cd03296 91 VFDNVAFGLRVKPRSERPPEAEIRAKvHELLKLVQLDWLADRYPA----QLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489011807 436 IDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
278-482 |
1.82e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.61 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 278 NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPG--RWQGEIFIDGQPVSiSNCQQAIAhgiAMVPEDrkkDGIVPVM 355
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvKGSGSVLLNGMPID-AKEMRAIS---AYVQQD---DLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVGKNITLAALNQFTGAMSSlddAAEQHCIQQSIQRL------KIKTSSPELAIGrLSGGNQQKAILARCLLLNPRILIL 429
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTK---KEKRERVDEVLQALglrkcaNTRIGVPGRVKG-LSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489011807 430 DEPTRGIDIGAKYEIYKLINQLVQQG-IAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGkTIICTIHQPSSELFELFDKIILMAEGR 244
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
276-485 |
1.94e-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: 63.67 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 276 RVNDVSFSLR-----------RGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSisncqqaiahgiAMVPE 344
Cdd:cd03298 2 RLDKIRFSYGeqpmhfdltfaQGEITAIVGPSGSGKSTLLNLIAGFETPQ-SGRVLINGVDVT------------AAPPA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 345 DR------KKDGIVPVMAVGKNITLaalnqftGAMSSLD-DAAEQHCIQQSIQRLKIKTSSPELAiGRLSGGNQQKAILA 417
Cdd:cd03298 69 DRpvsmlfQENNLFAHLTVEQNVGL-------GLSPGLKlTAEDRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
281-502 |
1.99e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.83 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 281 SFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPvsisncqqaiaHgIAMVPEDR------KKDGIVPV 354
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA-SGSLTLNGQD-----------H-TTTPPSRRpvsmlfQENNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 355 MAVGKNITLaalnqftGAMSSLDDAAEQHCIQQSI-QRLKIKTSSPELAiGRLSGGNQQKAILARCLLLNPRILILDEPT 433
Cdd:PRK10771 86 LTVAQNIGL-------GLNPGLKLNAAQREKLHAIaRQMGIEDLLARLP-GQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 434 RGIDIGAKYEIYKLINQLV-QQGIAVIVISSELPEVLGLSDRVLVMHEGRLKANLVNQHLTQEQVMEAAL 502
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCqERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
259-483 |
2.37e-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: 63.86 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRhiKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLfgvwpGRW----QGEIFIDGQPVSISN---C 331
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-----NRLieptSGEIFIDGEDIREQDpveL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 332 QQAIAHGIAMVpedrkkdGIVPVMAVGKNITLaalnqftgaMSSLDDAAEQHCIQQSIQRLKIKTSSPELAIGR----LS 407
Cdd:cd03295 74 RRKIGYVIQQI-------GLFPHMTVEENIAL---------VPKLLKWPKEKIRERADELLALVGLDPAEFADRypheLS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 408 GGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03295 138 GGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-221 |
2.44e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 63.05 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPH-GSYEGEIIFAGETLQANHirDTE 79
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnVSVEGDIHYNGIPYKEFA--EKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALVKHLTVLEniflgaeisrhgLLDYetmTLRCQKllaqvnlpispDTRVGDLGLGQQQLVEIAKALNK 159
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLTVRE------------TLDF---ALRCKG-----------NEFVRGISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 160 QVRLLILDEPTASLteqETATLLAIVRDLQNhdiaciyISHKLNEVKAIS------------DTICVIRDGQHI 221
Cdd:cd03233 136 RASVLCWDNSTRGL---DSSTALEILKCIRT-------MADVLKTTTFVSlyqasdeiydlfDKVLVLYEGRQI 199
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
2.55e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.09 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKV---LCGIYPHGSYEGEIIFAGETLQANHIRD 77
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 TE-RKGIAIIHQELALVKHLTVLENIFLGAEISrhGLL-DYETMTLRCQKLLAQVNLPISPDTRVGD----LGLGQQQLV 151
Cdd:PRK14267 81 IEvRREVGMVFQYPNPFPHLTIYDNVAIGVKLN--GLVkSKKELDERVEWALKKAALWDEVKDRLNDypsnLSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 152 EIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNhDIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-238 |
2.61e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.58 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 18 KAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGiyphGSY----EGEIIFAGETLQANHIRDTERKGIAII---HQEL 90
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG----RSYgrniSGTVFKDGKEVDVSTVSDAIDAGLAYVtedRKGY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 91 ALVKHLTVLENIFLGA--EISRHGLLD----------Y-ETMTLRCQkllaqvnlpiSPDTRVGDLGLGQQQLVEIAKAL 157
Cdd:NF040905 350 GLNLIDDIKRNITLANlgKVSRRGVIDeneeikvaeeYrKKMNIKTP----------SVFQKVGNLSGGNQQKVVLSKWL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 158 NKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIGTRDASGMSEDDIITM 237
Cdd:NF040905 420 FTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRL 499
|
.
gi 489011807 238 M 238
Cdd:NF040905 500 I 500
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
406-483 |
2.66e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.93 E-value: 2.66e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-219 |
2.69e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.38 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGA-----VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAGETLQAnhirDTE 79
Cdd:PRK13649 3 INLQNVSYTYQAgtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL--HVPTQGSVRVDDTLITS----TSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALVKHL--------TVLENIFLGAEisRHGLLDYETMTLRCQKLLAqvnLPISPDTRVG---DLGLGQQ 148
Cdd:PRK13649 77 NKDIKQIRKKVGLVFQFpesqlfeeTVLKDVAFGPQ--NFGVSQEEAEALAREKLAL---VGISESLFEKnpfELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 149 QLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
277-478 |
3.27e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 62.25 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgrwqgeifidgqPVSISnCQQAIAHGIAMVPEDRKKDGIVPVMA 356
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR------------PTSGT-VRRAGGARVAYVPQRSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGknitLAALNQF--TGAMSSLDdAAEQHCIQQSIQRLKIKtsspELA---IGRLSGGNQQKAILARCLLLNPRILILDE 431
Cdd:NF040873 75 RD----LVAMGRWarRGLWRRLT-RDDRAAVDDALERVGLA----DLAgrqLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489011807 432 PTRGIDIGAKYEIYKLINQLVQQGIAVIVISSElPEVLGLSDRVLVM 478
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
279-483 |
3.39e-11 |
|
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: 63.01 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVS-ISncQQAIAHGIAMVPEDrkkdgivPVMAV 357
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-KGQILIDGIDIRdIS--RKSLRSMIGVVLQD-------TFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 358 G---KNITLAALNqftGAMSSLDDAAEQHCIQQSIQRLK--IKTSSPELAiGRLSGGNQQKAILARCLLLNPRILILDEP 432
Cdd:cd03254 91 GtimENIRLGRPN---ATDEEVIEAAKEAGAHDFIMKLPngYDTVLGENG-GNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489011807 433 TRGIDIGAKYEIYKLInQLVQQGIAVIVISSELPEVLGlSDRVLVMHEGRL 483
Cdd:cd03254 167 TSNIDTETEKLIQEAL-EKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
405-483 |
3.45e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.03 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
252-481 |
3.49e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.60 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 252 HAHGEEILRVEHLTAWHPVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgrW-QGEIFI-DGQpvsis 329
Cdd:COG4178 356 ETSEDGALALEDLTLRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP--YgSGRIARpAGA----- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 330 ncqqaiahGIAMVPEDrkkdgivPVMAVGkniTLAALNQFTGAMSSLDDAA-----EQHCIQQSIQRLKIKTSSPElaig 404
Cdd:COG4178 427 --------RVLFLPQR-------PYLPLG---TLREALLYPATAEAFSDAElrealEAVGLGHLAERLDEEADWDQ---- 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSElPEVLGLSDRVLVMHEG 481
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREEL-PGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
405-483 |
3.53e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 63.49 E-value: 3.53e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:COG4161 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-210 |
3.69e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 63.65 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKV---LCGIYPHGSYEGEIIFAGETLQANHIRDTE- 79
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRVEGKVTFHGKNLYAPDVDPVEv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALVKHlTVLENIFLGAEISRH-GLLDyETMtlrcQKLLAQVNLPISPDTRVGDLGL----GQQQLVEIA 154
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYGARINGYkGDMD-ELV----ERSLRQAALWDEVKDKLKQSGLslsgGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 155 KALNKQVRLLILDEPTASLTEQETATLLAIVRDLQnHDIACIYISHKLNEVKAISD 210
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
278-483 |
3.72e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.94 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 278 NDVSFSLRRGEILGIAGLVGAGRTEavqcLFGVWPGRWQ---GEIFIDGQPVSISNcqqaiahgiAMVPEDRKKDGIV-- 352
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKST----LFLHFNGILKptsGEVLIKGEPIKYDK---------KSLLEVRKTVGIVfq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 ----PVMA--VGKNITLAALNQftgamsSLDDAAEQHCIQQSIQRLKIKtSSPELAIGRLSGGNQQKAILARCLLLNPRI 426
Cdd:PRK13639 86 npddQLFAptVEEDVAFGPLNL------GLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 427 LILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
275-483 |
3.88e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.38 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 275 KRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV--WPGRWQGEIFI----DGQPVSISNCQQAIAHGIAMVPEDrKK 348
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGRVMAEKLEfngqDLQRISEKERRNLVGAEVAMIFQD-PM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 349 DGIVPVMAVGKNItLAALNQFTGAmssldDAAEQHciQQSIQRLKI-----KTSSPELAIGRLSGGNQQKAILARCLLLN 423
Cdd:PRK11022 100 TSLNPCYTVGFQI-MEAIKVHQGG-----NKKTRR--QRAIDLLNQvgipdPASRLDVYPHQLSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 424 PRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-218 |
4.17e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 20 VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG-----IYPHG-SYEGEIIFAGETLQANHIRDTERKGiAIIHQELALV 93
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltggGAPRGaRVTGDVTLNGEPLAAIDAPRLARLR-AVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 94 KHLTVLENIFLG--AEISRHGLLDYETMTLRCQKL-LAQVNLPISPDtrVGDLGLGQQQLVEIAKALNK---------QV 161
Cdd:PRK13547 96 FAFSAREIVLLGryPHARRAGALTHRDGEIAWQALaLAGATALVGRD--VTTLSGGELARVQFARVLAQlwpphdaaqPP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 162 RLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDG 218
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADG 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
278-482 |
4.30e-11 |
|
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: 65.23 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 278 NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFgvwpgR----WQGEIFIDGQPvsISNCQQAIAHG-IAMVPEDrkkdgiv 352
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLF-----RfydvTSGRILIDGQD--IRDVTQASLRAaIGIVPQD------- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 PVM---AVGKNITLAALnqftGA-MSSLDDAAEQHCIQQSIQRLkiktssP---ELAIG----RLSGGNQQKAILARCLL 421
Cdd:COG5265 441 TVLfndTIAYNIAYGRP----DAsEEEVEAAARAAQIHDFIESL------PdgyDTRVGerglKLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 422 LNPRILILDEPTRGIDIGAKYEIYKLINQlVQQGIAVIVISSELPEVLGlSDRVLVMHEGR 482
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALRE-VARGRTTLVIAHRLSTIVD-ADEILVLEAGR 569
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
273-483 |
4.53e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.95 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 273 HIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGrwQGEI---FIDGQP----------VSISNCQQAIAHG 338
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlPD--TGTIewiFKDEKNkkktkekekvLEKLVIQKTRFKK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 339 IAMVPEDRKKDGIVPVMA--------VGKNITLAALNQFTGAMSSLDDAAEQhciqqsIQRLKIKTSSPELAIGRLSGGN 410
Cdd:PRK13651 97 IKKIKEIRRRVGVVFQFAeyqlfeqtIEKDIIFGPVSMGVSKEEAKKRAAKY------IELVGLDESYLQRSPFELSGGQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 411 QQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-221 |
4.62e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWLLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyegeiifagetlqaNHIRDTER 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE--------------GVIKRNGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALvkhltvleNIFLGAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQ 160
Cdd:PRK09544 67 LRIGYVPQKLYL--------DTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 161 VRLLILDEPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIrdGQHI 221
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL--NHHI 198
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-217 |
4.80e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 21 DNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIifageTLQANHirdterkgiaiIHQELALVKHLTVLE 100
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----DVPDNQ-----------FGREASLIDAIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 101 NIFLGAEI-SRHGLLDYETMtLRcqkllaqvnlpispdtRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLtEQETA 179
Cdd:COG2401 111 DFKDAVELlNAVGLSDAVLW-LR----------------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL-DRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489011807 180 TLLA-IVRDL-QNHDIACIYISHKLNEVKAISDTICVIRD 217
Cdd:COG2401 173 KRVArNLQKLaRRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
277-483 |
4.87e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 64.01 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwqGEIFIDGQPVSIsncqqaiahgiAMVPEDRKKdGIV--- 352
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPDS--GRIVLNGRDLFT-----------NLPPRERRV-GFVfqh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 ----PVMAVGKNItlaalnQFTGAMSSLDDAAEQHCIQQSIQRLKIktssPELAiGR----LSGGNQQKAILARCLLLNP 424
Cdd:COG1118 84 yalfPHMTVAENI------AFGLRVRPPSKAEIRARVEELLELVQL----EGLA-DRypsqLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 425 RILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-509 |
4.90e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.58 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQgIAVIVISSELPEVLGLSDRVLVMHEGRlk 484
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGR-- 239
|
90 100
....*....|....*....|....*
gi 489011807 485 anlvnqhLTQEQVMEAALRSERHVE 509
Cdd:PRK14271 240 -------LVEEGPTEQLFSSPKHAE 257
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-219 |
5.27e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.47 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF-GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAG-ETLQANHIRDTeR 80
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQ---KGKVLVSGiDTGDFSKLQGI-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQ--ELALVKHlTVLENIFLGAEisrHGLLDYETMTLRCQKLLAQVNLPI----SPDTRVGdlglGQQQLVEIA 154
Cdd:PRK13644 77 KLVGIVFQnpETQFVGR-TVEEDLAFGPE---NLCLPPIEIRKRVDRALAEIGLEKyrhrSPKTLSG----GQGQCVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 155 KALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGK 212
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
279-502 |
6.99e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 64.74 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGrwQGEIFIDGQPVSISNCqqaiaHGIamvpedRKKDGIV---PV 354
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPT--GGQVLLDGVPLVQYDH-----HYL------HRQVALVgqePV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 355 M---AVGKNITLAaLNQFTgaMSSLDDAAEQHCIQQSIQRLK--IKTSSPElAIGRLSGGNQQKAILARCLLLNPRILIL 429
Cdd:TIGR00958 566 LfsgSVRENIAYG-LTDTP--DEEIMAAAKAANAHDFIMEFPngYDTEVGE-KGSQLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 430 DEPTRGIDIGAKYEIYKLINqlvQQGIAVIVISSELPEVLGlSDRVLVMHEGRLKANLVNQHLTQEQVMEAAL 502
Cdd:TIGR00958 642 DEATSALDAECEQLLQESRS---RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-219 |
8.96e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 18 KAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYP--HGSYE-GEIIFAGETlQANHIRdTERKGIAIIHQ--ELAL 92
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKptTGTVTvDDITITHKT-KDKYIR-PVRKRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 93 VKHlTVLENIFLGaeiSRHGLLDYETMTLRCQKLLAQVNLP-----ISPDTRVGdlglGQQQLVEIAKALNKQVRLLILD 167
Cdd:PRK13646 99 FED-TVEREIIFG---PKNFKMNLDEVKNYAHRLLMDLGFSrdvmsQSPFQMSG----GQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489011807 168 EPTASLTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGS 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
274-485 |
9.52e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.51 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 274 IKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQaIAHGIAMVPEDRKKDGIVP 353
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT-SGSVLIRGEPITKENIRE-VRKFVGLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 354 vmAVGKNITLAALNQftgamsSLDDAAEQHCIQQSIQRLKI---KTSSPElaigRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:PRK13652 95 --TVEQDIAFGPINL------GLDEETVAHRVSSALHMLGLeelRDRVPH----HLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 431 EPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-464 |
1.08e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 24 SLRLNAGEVVSLCGENGSGKSTLMKVLCGIYP--HGSYEGE----IIFAGETLQAnhirdterkgiaIIHQELALVKH-- 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPllSGERQSQfshiTRLSFEQLQK------------LVSDEWQRNNTdm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 96 LTVLENIF--LGAEISRHGLLDYEtmtlRCQKLLAQvnLPISP--DTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTA 171
Cdd:PRK10938 91 LSPGEDDTgrTTAEIIQDEVKDPA----RCEQLAQQ--FGITAllDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 172 SLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQ--HIGTRDASgMSEDDIITMMVGRELTALYPS 249
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTlaETGEREEI-LQQALVAQLAHSEQLEGVQLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 250 EPhahgEEILRVEHLTAWHP--------VNRHIKRV-NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPG------- 313
Cdd:PRK10938 244 EP----DEPSARHALPANEPrivlnngvVSYNDRPIlHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgysndlt 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 314 -----RWQGEIFIDgqpvsisncqqaIAHGIAMVPEDRKKDGIVPVMAvgKNITLAALNQFTGAMSSLDDaAEQHCIQQS 388
Cdd:PRK10938 320 lfgrrRGSGETIWD------------IKKHIGYVSSSLHLDYRVSTSV--RNVILSGFFDSIGIYQAVSD-RQQKLAQQW 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 389 IQRLKIKTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDigakyeiyKLINQLVQQGIAVIVISSE 464
Cdd:PRK10938 385 LDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD--------PLNRQLVRRFVDVLISEGE 452
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
249-513 |
1.42e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 249 SEPHAHGEEILRVEHLTAWHPVNRHiKRVNDVSFSLRRGEILGIAGLVGAGRT---EAVQCLFGVWpgrwQGEIFIDGQP 325
Cdd:PRK10789 304 SEPVPEGRGELDVNIRQFTYPQTDH-PALENVNFTLKPGQMLGICGPTGSGKStllSLIQRHFDVS----EGDIRFHDIP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 326 VSIsncqqaiahgiAMVPEDRKKDGIVPVM------AVGKNItlaALNQFTGAMSSLDDAAEQHCIQQSIQRLK--IKTS 397
Cdd:PRK10789 379 LTK-----------LQLDSWRSRLAVVSQTpflfsdTVANNI---ALGRPDATQQEIEHVARLASVHDDILRLPqgYDTE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 398 SPELAIgRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQgiAVIVISSELPEVLGLSDRVLV 477
Cdd:PRK10789 445 VGERGV-MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTEASEILV 521
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489011807 478 MHEGRLKANLVNQHLTQE----------QVMEAALRSERHVEEHVV 513
Cdd:PRK10789 522 MQHGHIAQRGNHDQLAQQsgwyrdmyryQQLEAALDDAPEIREEAV 567
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
279-483 |
1.49e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.06 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQAIAhgiamvpEDRKKDGIV---PVM 355
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPT-EGKVTVGDIVVSSTSKQKEIK-------PVRKKVGVVfqfPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVGKNITLAALnQFTGAMSSLDDAAEQHCIQQSIQRLKIKTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:PRK13643 96 QLFEETVLKDV-AFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489011807 436 IDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-210 |
1.53e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGS---YEGEIIFAGETLQANHIR-DTER 80
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrVEGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 81 KGIAIIHQELALVKhLTVLENIFLGAEI----SRHGLLDYETMTLRCQKLLAQVNLPISPDTRvgDLGLGQQQLVEIAKA 156
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwrPKLEIDDIVESALKDADLWDEIKHKIHKSAL--DLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 157 LNKQVRLLILDEPTASLTEQETATLLAIVRDLQ-NHDIACIYISHKLNEVKAISD 210
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
279-487 |
1.78e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.98 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVwPGRWQGEIFIDGQPVSisncqQAIAHGIAMVpedrkkdgivpvmavg 358
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPMS-----KLSSAAKAEL---------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 359 KNITLAALNQFTGAM---SSLDDAAEQHCIQQSiQRLKIKTSSPEL--AIG----------RLSGGNQQKAILARCLLLN 423
Cdd:PRK11629 85 RNQKLGFIYQFHHLLpdfTALENVAMPLLIGKK-KPAEINSRALEMlaAVGlehranhrpsELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 424 PRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELpEVLGLSDRVLVMHEGRLKANL 487
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAEL 227
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-70 |
2.02e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.20 E-value: 2.02e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGiypHGSY---EGEIIFAGETL 70
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---HPAYkilEGDILFKGESI 73
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-169 |
2.26e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.72 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIF-----AGETlqanhIRDT 78
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFgrrrgSGET-----IWDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 79 ERKgIAIIHQELalvkHL-----TVLENIFLGAEISRHGLldYETMTLRCQKLLAQVNLPISPDTRVGD-----LGLGQQ 148
Cdd:PRK10938 335 KKH-IGYVSSSL----HLdyrvsTSVRNVILSGFFDSIGI--YQAVSDRQQKLAQQWLDILGIDKRTADapfhsLSWGQQ 407
|
170 180
....*....|....*....|.
gi 489011807 149 QLVEIAKALNKQVRLLILDEP 169
Cdd:PRK10938 408 RLALIVRALVKHPTLLILDEP 428
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-221 |
2.47e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.56 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 12 KTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQAN--HIRDTE--RKGIAIIH 87
Cdd:PRK13645 19 KTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLII--SETGQTIVGDYAIPANlkKIKEVKrlRKEIGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 88 Q--ELALVKHlTVLENIFLGaeiSRHGLLDYETMTLRCQKLLAQVNLPISPDTRVG-DLGLGQQQLVEIAKALNKQVRLL 164
Cdd:PRK13645 97 QfpEYQLFQE-TIEKDIAFG---PVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-483 |
2.55e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.22 E-value: 2.55e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQgIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK14246 153 QLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
274-481 |
2.64e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.85 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 274 IKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRWQ---GEIFIDGQPVsisncqqaiahgIAMVPEDRKKdg 350
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHvtaDRFRWNGIDL------------LKLSPRERRK-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 351 ivpvmAVGKNITLAalnqFTGAMSSLDDAAE----------------------QHCIQQSIQRL---------KIKTSSP 399
Cdd:COG4170 86 -----IIGREIAMI----FQEPSSCLDPSAKigdqlieaipswtfkgkwwqrfKWRKKRAIELLhrvgikdhkDIMNSYP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 400 ElaigRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVM 478
Cdd:COG4170 157 H----ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVL 232
|
...
gi 489011807 479 HEG 481
Cdd:COG4170 233 YCG 235
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-477 |
2.69e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 30 GEVVSLCGENGSGKSTLMKVLCG-IYPH-GSYEG-----EII--FAGETLQaNHIRDTERKGIAIIH--QELALV-KHL- 96
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGeLIPNlGDYEEepswdEVLkrFRGTELQ-NYFKKLYNGEIKVVHkpQYVDLIpKVFk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 97 -TVLEnifLGAEISRHGLLDYetmtlrcqkLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTE 175
Cdd:PRK13409 178 gKVRE---LLKKVDERGKLDE---------VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 176 QETATLLAIVRDLQNhDIACIYISHKLNEVKAISDTIcvirdgqHI--GTRDASGmseddIITMMVG-RE-----LTALY 247
Cdd:PRK13409 246 RQRLNVARLIRELAE-GKYVLVVEHDLAVLDYLADNV-------HIayGEPGAYG-----VVSKPKGvRVgineyLKGYL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 248 PSE------------PHAHGEEILRvEHLTAWHPVnrhIKRVNDvsFSL-------RRGEILGIAGLVGAGRTEAVQCLF 308
Cdd:PRK13409 313 PEEnmrirpepiefeERPPRDESER-ETLVEYPDL---TKKLGD--FSLeveggeiYEGEVIGIVGPNGIGKTTFAKLLA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 309 GVW-PGrwQGEIFIDgqpVSISNCQQAIahgiamvpedrKKDGIVPVMAVGKNITlaalnqftgamSSLDDAAEQHCIqq 387
Cdd:PRK13409 387 GVLkPD--EGEVDPE---LKISYKPQYI-----------KPDYDGTVEDLLRSIT-----------DDLGSSYYKSEI-- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 388 sIQRLKIKTSSpELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLV-QQGIAVIVISSELP 466
Cdd:PRK13409 438 -IKPLQLERLL-DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDHDIY 515
|
490
....*....|.
gi 489011807 467 EVLGLSDRVLV 477
Cdd:PRK13409 516 MIDYISDRLMV 526
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-219 |
2.82e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.88 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 27 LNAGEVVSLCGENGSGKSTLMKVLCG-IYPHgsyEGEIIFAGETlqanhirdterkgIAIIHQELALVKHLTVLEniFLG 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGvLKPD---EGDIEIELDT-------------VSYKPQYIKADYEGTVRD--LLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 106 AEISRHGLLDY---ETMT-LRCQKLLaqvnlpispDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASL-TEQETAT 180
Cdd:cd03237 84 SITKDFYTHPYfktEIAKpLQIEQIL---------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLdVEQRLMA 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 489011807 181 LLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIrDGQ 219
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGE 192
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-77 |
3.07e-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: 62.51 E-value: 3.07e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 5 LEMKNITKTFGAVK-----AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAGETLQANHIRD 77
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYrPE---SGEILLDGQPVTADNREA 403
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-221 |
3.09e-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: 59.49 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKT-----FGAVKAV-DNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGETLqanhIRDT 78
Cdd:cd03213 4 LSFRNLTVTvksspSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPL----DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 79 ERKGIAIIHQELALVKHLTVLENIFLGAEisrhglldyetmtLRCqkllaqvnlpISpdtrvGdlglGQQQLVEIAKALN 158
Cdd:cd03213 80 FRKIIGYVPQDDILHPTLTVRETLMFAAK-------------LRG----------LS-----G----GERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 159 KQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKL-NEVKAISDTICVIRDGQHI 221
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-218 |
3.10e-10 |
|
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: 60.04 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 17 VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGiyPHGSYEGEIIFAGETLQANHIRDTE---RKGIAIIHQELALV 93
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWSNKNESEPSFEATRsrnRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 94 kHLTVLENIFLGAEISRHgllDYETMTLRCQkLLAQVN-LPISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDE 168
Cdd:cd03290 92 -NATVEENITFGSPFNKQ---RYKAVTDACS-LQPDIDlLPFGDQTEIGERGInlsgGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489011807 169 PTASLTEQETATLL--AIVRDLQNHDIACIYISHKLNEVKAiSDTICVIRDG 218
Cdd:cd03290 167 PFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-200 |
3.69e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGiyPHGSYEGEIIFaGETLQANHIrDTERKgia 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG--QEQPDSGTIEI-GETVKLAYV-DQSRD--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 iihqelALVKHLTVLENIFLGAEISRHGllDYETMTlrcQKLLAQVNLPiSPD--TRVGDLGLGQQQLVEIAKALNKQVR 162
Cdd:TIGR03719 396 ------ALDPNKTVWEEISGGLDIIKLG--KREIPS---RAYVGRFNFK-GSDqqKKVGQLSGGERNRVHLAKTLKSGGN 463
|
170 180 190
....*....|....*....|....*....|....*...
gi 489011807 163 LLILDEPTASLteqETATLLAIVRDLQNHDIACIYISH 200
Cdd:TIGR03719 464 VLLLDEPTNDL---DVETLRALEEALLNFAGCAVVISH 498
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
277-482 |
3.73e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.50 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGvWPGRWQGEIFIDGQPVSisncqqaiahgiaMVPEDRKKDGIV---- 352
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-FETPDSGRIMLDGQDIT-------------HVPAENRHVNTVfqsy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 ---PVMAVGKNITLAALNQFTG------------AMSSLDDAAEQHCIQqsiqrlkiktsspelaigrLSGGNQQKAILA 417
Cdd:PRK09452 96 alfPHMTVFENVAFGLRMQKTPaaeitprvmealRMVQLEEFAQRKPHQ-------------------LSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 418 RCLLLNPRILILDEPTRGIDigakyeiYKL-------INQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALD-------YKLrkqmqneLKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
280-509 |
4.08e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.17 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 280 VSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgrWQGEIFIDGQPVSISNCQQAIAHgIAMVPEDRKkdgiVPVMAVGK 359
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP--YQGSLKINGIELRELDPESWRKH-LSWVGQNPQ----LPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 360 NITLAAlnqftgamSSLDDAAeqhcIQQSIQRLKIKTSSPELAIG----------RLSGGNQQKAILARCLLLNPRILIL 429
Cdd:PRK11174 442 NVLLGN--------PDASDEQ----LQQALENAWVSEFLPLLPQGldtpigdqaaGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 430 DEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELpEVLGLSDRVLVMHEGRlkanLVNQH----LTQEQVMEAALRSE 505
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQL-EDLAQWDQIWVMQDGQ----IVQQGdyaeLSQAGGLFATLLAH 583
|
....
gi 489011807 506 RHVE 509
Cdd:PRK11174 584 RQEE 587
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-231 |
4.10e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.67 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQanhiRDTERKGIAIIHQELALVKHLTV 98
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLAS--GKISILGQPTR----QALQKNLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 99 L-ENIFLGAEISRHGLLDYETMTLR--CQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTE 175
Cdd:PRK15056 96 LvEDVVMMGRYGHMGWLRRAKKRDRqiVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 176 QETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRdgqhiGTRDASGMSE 231
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-----GTVLASGPTE 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
259-483 |
4.15e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 60.26 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRHIKRV-NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGrwQGEIFIDGQPVSISNCQQAIA 336
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPAlQDVSLTIESGEFVVALGASGCGKTTLLNLIAGfLAPS--SGEITLDGVPVTGPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 337 HgiamvpedrKKDGIVPVMAVGKNITLAAlnQFTGAmssldDAAEQHCI-QQSIQRLKIKTSSpELAIGRLSGGNQQKAI 415
Cdd:COG4525 82 F---------QKDALLPWLNVLDNVAFGL--RLRGV-----PKAERRARaEELLALVGLADFA-RRRIWQLSGGMRQRVG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 416 LARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVM--HEGRL 483
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
258-485 |
4.24e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.58 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTAWHPvNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVwpgrwqgeIFIDGQPVSISNCQqAIAH 337
Cdd:PRK13640 5 IVEFKHVSFTYP-DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--------LLPDDNPNSKITVD-GITL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 338 GIAMVPEDRKKDGIVpvmavGKNITlaalNQFTGAMSSlDDAA---EQHCIQQSiQRLKI-------------KTSSPEl 401
Cdd:PRK13640 75 TAKTVWDIREKVGIV-----FQNPD----NQFVGATVG-DDVAfglENRAVPRP-EMIKIvrdvladvgmldyIDSEPA- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 402 aigRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVlGLSDRVLVMHE 480
Cdd:PRK13640 143 ---NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDD 218
|
....*
gi 489011807 481 GRLKA 485
Cdd:PRK13640 219 GKLLA 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
406-496 |
4.50e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.03 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
90
....*....|.
gi 489011807 486 NLVNQHLTQEQ 496
Cdd:PRK11124 222 QGDASCFTQPQ 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
277-483 |
4.59e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.59 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwqGEIFIDG---QPVSISNCQQAIAHGIAMVPEDRkkdGIV 352
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPTR--GQVLIDGvdiAKISDAELREVRRKKIAMVFQSF---ALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 PVMAVGKNITlaalnqFTGAMSSLDDAAEQHCIQQSIQRLKIKTSS---PElaigRLSGGNQQKAILARCLLLNPRILIL 429
Cdd:PRK10070 119 PHMTVLDNTA------FGMELAGINAEERREKALDALRQVGLENYAhsyPD----ELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 430 DEPTRGIDIGAKYEIY-KLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK10070 189 DEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-221 |
4.98e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 16 AVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY--PHGSYEGEIIFAGETLQANHIRDTERK-GIAIIHQELAL 92
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqpTEGKVTVGDIVVSSTSKQKEIKPVRKKvGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 93 VKHlTVLENIFLGAEisRHGLLDYETMTLRCQKL----LAQVNLPISPdtrvGDLGLGQQQLVEIAKALNKQVRLLILDE 168
Cdd:PRK13643 98 FEE-TVLKDVAFGPQ--NFGIPKEKAEKIAAEKLemvgLADEFWEKSP----FELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489011807 169 PTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHI 221
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
406-484 |
5.85e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.98 E-value: 5.85e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLK 484
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
249-483 |
6.29e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 59.67 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 249 SEPHAHGEEILRVEHLTAWHpVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW---PG-RWQGEIFIDGQ 324
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYY-GDKQA--LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdliPGaRVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 325 PVSISNCQqaiahgiamVPEDRKKDGIV---PV---MAVGKNITLAA-LNQFTGAmSSLDDAAEQhCIQQSIQ------R 391
Cdd:COG1117 79 DIYDPDVD---------VVELRRRVGMVfqkPNpfpKSIYDNVAYGLrLHGIKSK-SELDEIVEE-SLRKAALwdevkdR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 392 LKiktsspELAIGrLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQgIAVIVISSELPEVLGL 471
Cdd:COG1117 148 LK------KSALG-LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARV 219
|
250
....*....|..
gi 489011807 472 SDRVLVMHEGRL 483
Cdd:COG1117 220 SDYTAFFYLGEL 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-232 |
6.33e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDN----VSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgsYEGEIIFAGETLQANHIRDTERKGIAIIHQELAL-- 92
Cdd:PRK03695 7 AVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP---GSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 93 --VKHLTVLENIFLGAEISRHGLLDYETMTLRCQKLLAqvnlpispdTRVGDLGLGQQQLVEIA-------KALNKQVRL 163
Cdd:PRK03695 84 mpVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLG---------RSVNQLSGGEWQRVRLAavvlqvwPDINPAGQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 164 LILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDGQHIgtrdASGMSED 232
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL----ASGRRDE 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
405-482 |
7.16e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 7.16e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-219 |
8.45e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.72 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-PHgsyEGEIIFAG-ETLQANHIRDTERK-GIAIIHQELALVKH 95
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPS---EGKVYVDGlDTSDEENLWDIRNKaGMVFQNPDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 96 LtVLENIFLGAEisRHGLLDYETMTlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTE 175
Cdd:PRK13633 102 I-VEEDVAFGPE--NLGIPPEEIRE-RVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489011807 176 QETATLLAIVRDL-QNHDIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:PRK13633 178 SGRREVVNTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGK 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
275-483 |
8.49e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.02 E-value: 8.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 275 KRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWpgrwqgeIFIDGQPVSISNCQQAIAHGIAMVPEDRKKDGIV-- 352
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-------ISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVfq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 -PVM-----AVGKNITLAALNQftgamsslddAAEQHCIQQSIQRLKIKTSSPELAIGR----LSGGNQQKAILARCLLL 422
Cdd:PRK13645 98 fPEYqlfqeTIEKDIAFGPVNL----------GENKQEAYKKVPELLKLVQLPEDYVKRspfeLSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 423 NPRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-477 |
1.02e-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: 60.95 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 30 GEVVSLCGENGSGKSTLMKVLCG-IYPH-GSYEG-----EII--FAGETLQaNHIRDTERKGIAIIH--QELALV-KHL- 96
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGeLKPNlGDYDEepswdEVLkrFRGTELQ-DYFKKLANGEIKVAHkpQYVDLIpKVFk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 97 -TVLEnifLGAEISRHGLLDYetmtlrcqkLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTE 175
Cdd:COG1245 178 gTVRE---LLEKVDERGKLDE---------LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 176 QETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTIcvirdgqHI--GTRDASGmseddIITMMVG-RE-----LTALY 247
Cdd:COG1245 246 YQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYV-------HIlyGEPGVYG-----VVSKPKSvRVginqyLDGYL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 248 PSE------------PHAHGEEILRVEhLTAWHPVnrhIKRVNDvsFSL-------RRGEILGIAGLVGAGRTEAVQCLF 308
Cdd:COG1245 314 PEEnvrirdepiefeVHAPRREKEEET-LVEYPDL---TKSYGG--FSLeveggeiREGEVLGIVGPNGIGKTTFAKILA 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 309 GVW-PGrwQGEIFIDgqpVSISNCQQAIAHGIAMvpedrkkdgivPVMAVgknitLAALNQftgamSSLDDAAEQHCIqq 387
Cdd:COG1245 388 GVLkPD--EGEVDED---LKISYKPQYISPDYDG-----------TVEEF-----LRSANT-----DDFGSSYYKTEI-- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 388 sIQRLKIKtssP--ELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLV-QQGIAVIVISSE 464
Cdd:COG1245 440 -IKPLGLE---KllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDHD 515
|
490
....*....|...
gi 489011807 465 LPEVLGLSDRVLV 477
Cdd:COG1245 516 IYLIDYISDRLMV 528
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-205 |
1.14e-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: 61.11 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 22 NVSLRLNAGEVVSLCGENGSGKSTLmkVLCGIYPHGSYEGEIIFAGETLQANHIRDTeRKGIAIIHQELALVKHlTVLEN 101
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGLNIAKIGLHDL-RFKITIIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 102 IFLGAEISRHGLLdyetMTLRCQKLLAQVN-LPISPDTRVGD----LGLGQQQLVEIAKALNKQVRLLILDEPTASLtEQ 176
Cdd:TIGR00957 1380 LDPFSQYSDEEVW----WALELAHLKTFVSaLPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAV-DL 1454
|
170 180
....*....|....*....|....*....
gi 489011807 177 ETATLLAIVRDLQNHDIACIYISHKLNEV 205
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFEDCTVLTIAHRLNTI 1483
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
277-483 |
1.15e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.75 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGrwQGEIFIDGQPVSISNcQQAIAHGIAMVPED-----RKkdg 350
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQ--SGRILIDGTDIRTVT-RASLRRNIAVVFQDaglfnRS--- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 351 IVPVMAVGK-NITLAALnqftgaMSSLDDAAEQHCIQQSIQRLkiktsspELAIG----RLSGGNQQKAILARCLLLNPR 425
Cdd:PRK13657 425 IEDNIRVGRpDATDEEM------RAAAERAQAHDFIERKPDGY-------DTVVGergrQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 426 ILILDEPTRGIDIGAKYEIYKLINQlVQQGIAVIVISSELPEVLGlSDRVLVMHEGRL 483
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDE-LMKGRTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
275-483 |
1.21e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.89 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 275 KRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVwpGRWQGEIFIDGQ-----------PVSISNCQQAIAhgiaMVp 343
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM--NELESEVRVEGRveffnqniyerRVNLNRLRRQVS----MV- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 344 edRKKDGIVPvMAVGKNITLAAlnQFTGAMSSLD-DAAEQHCIQQSIQRLKIKTSSPELAIgRLSGGNQQKAILARCLLL 422
Cdd:PRK14258 94 --HPKPNLFP-MSVYDNVAYGV--KIVGWRPKLEiDDIVESALKDADLWDEIKHKIHKSAL-DLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 423 NPRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMH--EGRL 483
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQVSRLSDFTAFFKgnENRI 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
287-482 |
1.31e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 287 GEILGIAGLVGAGRTEAVQCLfgvwPGRWQGEIFIDGQPVSISNCQQAIAHGIAMVPEDrkkDGIVPVMAVGKNITLAAL 366
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNAL----AGRIQGNNFTGTILANNRKPTKQILKRTGFVTQD---DILYPHLTVRETLVFCSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 367 NQFTGAMSSLDD--AAEQhciqqSIQRLKIkTSSPELAIGR-----LSGGNQQKAILARCLLLNPRILILDEPTRGIDIG 439
Cdd:PLN03211 167 LRLPKSLTKQEKilVAES-----VISELGL-TKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489011807 440 AKYEIYKLINQLVQQGiAVIVISSELP--EVLGLSDRVLVMHEGR 482
Cdd:PLN03211 241 AAYRLVLTLGSLAQKG-KTIVTSMHQPssRVYQMFDSVLVLSEGR 284
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-214 |
1.38e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGavkavdNVSLR-----LNAGEVVSLCGENGSGKSTLMKVLCG-IYPHgsyEGEIifagetlqanhirD 77
Cdd:PRK13409 340 LVEYPDLTKKLG------DFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGvLKPD---EGEV-------------D 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 78 TERKgIAIIHQELALVKHLTV---LENI-------FLGAEISRhglldyetmTLRCQKLLaqvnlpispDTRVGDLGLGQ 147
Cdd:PRK13409 398 PELK-ISYKPQYIKPDYDGTVedlLRSItddlgssYYKSEIIK---------PLQLERLL---------DKNVKDLSGGE 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 148 QQLVEIAKALNKQVRLLILDEPTASL-TEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICV 214
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLdVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
9-232 |
1.47e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.50 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 9 NITKTFGAVKAvdNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG-IYPHgsyEGEIIFAGETL--QANHIR-DTERKGIA 84
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGlTRPQ---KGRIVLNGRVLfdAEKGIClPPEKRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLGAEISRHGLLDYETMTLRCQKLLAQvnLPISpdtrvgdLGLGQQQLVEIAKALNKQVRLL 164
Cdd:PRK11144 80 YVFQDARLFPHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDR--YPGS-------LSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 165 ILDEPTASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAISDTICVIRDGQHIgtrdASGMSED 232
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVK----AFGPLEE 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
406-483 |
1.64e-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: 57.54 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVIsSELPEVLGL--SDRVLVMHEGRL 483
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLII-THYQRLLDYikPDRVHVLYDGRI 183
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
280-483 |
1.76e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.39 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 280 VSFSLRRGEILGIAGLVGAGRTEAVQC---LFGVWP-GRWQGEIFIDGQPV---SISNCQQAIaHGIAMVPEDrkkdgiV 352
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPeARVSGEVYLDGQDIfkmDVIELRRRV-QMVFQIPNP------I 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 PVMAVGKNITLA-ALNQFTGAMSSLDDAAEQHCIQ-QSIQRLKIKTSSPElaiGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:PRK14247 95 PNLSIFENVALGlKLNRLVKSKKELQERVRWALEKaQLWDEVKDRLDAPA---GKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489011807 431 EPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
258-483 |
1.83e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.85 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTAWHPVNrhIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGqpvsISNCQqaiah 337
Cdd:PRK13644 1 MIRLENVSYSYPDG--TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ-KGKVLVSG----IDTGD----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 338 gIAMVPEDRKKDGIVpvmavGKNITlaalNQFTGAMSSLDDA--AEQHCIQQSIQRLKIKTSSPELAIGR--------LS 407
Cdd:PRK13644 69 -FSKLQGIRKLVGIV-----FQNPE----TQFVGRTVEEDLAfgPENLCLPPIEIRKRVDRALAEIGLEKyrhrspktLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 408 GGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEvLGLSDRVLVMHEGRL 483
Cdd:PRK13644 139 GGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKI 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
404-485 |
2.57e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.73 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 404 GRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGK 206
|
...
gi 489011807 483 LKA 485
Cdd:PRK11144 207 VKA 209
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
280-485 |
2.78e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.09 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 280 VSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISN-CQQAIAHGIAMVPEDrkKDGIVPVMAVG 358
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ-KGAVLWQGKPLDYSKrGLLALRQQVATVFQD--PEQQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 359 KNITLAALNQFTGA---MSSLDDAAE----QHCIQQSIQRLkiktsspelaigrlSGGNQQKAILARCLLLNPRILILDE 431
Cdd:PRK13638 97 SDIAFSLRNLGVPEaeiTRRVDEALTlvdaQHFRHQPIQCL--------------SHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489011807 432 PTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-248 |
2.83e-09 |
|
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: 60.03 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 2 TWLLEMKNITKTFGAVK--AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANhirdte 79
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTS--GDATVAGKSILTN------ 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 rkgIAIIHQELALVKHLTVLENIFLGAE----ISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAK 155
Cdd:TIGR01257 2007 ---ISDVHQNMGYCPQFDAIDDLLTGREhlylYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAI 2083
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 156 ALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICVIRDG--------QHIGTRDAS 227
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafqclgtiQHLKSKFGD 2163
|
250 260
....*....|....*....|.
gi 489011807 228 GMseddIITMMVGRELTALYP 248
Cdd:TIGR01257 2164 GY----IVTMKIKSPKDDLLP 2180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
277-482 |
2.96e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQaiaHGIAMVPEDRkkdGIVPVMA 356
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT-AGQIMLDGVDLSHVPPYQ---RPINMMFQSY---ALFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNITLAaLNQFTGAMSSLDDAAEQHCIQQSIQRLKIKTSSpelaigRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:PRK11607 108 VEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPH------QLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489011807 437 DIGAKYEI-YKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:PRK11607 181 DKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-219 |
3.12e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 57.04 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGA--VKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTeRKG 82
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE--AEEGKIEIDGIDISTIPLEDL-RSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIHQELALVKHlTVLEN-----------IFLGAEISRHGLldyetmtlrcqkllaqvnlpispdtrvgDLGLGQQQLV 151
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNldpfdeysdeeIYGALRVSEGGL----------------------------NLSQGQRQLL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 152 EIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNhDIACIYISHKLNEVkAISDTICVIRDGQ 219
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTI-IDYDKILVMDAGE 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
280-459 |
3.25e-09 |
|
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: 56.73 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 280 VSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPVSISncQQAIAHGIAMVPEdrkKDGIVPVMAVGK 359
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP-PLAGRVLLNGGPLDFQ--RDSIARGLLYLGH---APGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 360 NIT-LAALNQFTGAMSSLDDAAeqhciqqsiqrlkiKTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDI 438
Cdd:cd03231 93 NLRfWHADHSDEQVEEALARVG--------------LNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|.
gi 489011807 439 GAKYEIYKLINQLVQQGIAVI 459
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVV 179
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
406-483 |
5.07e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.45 E-value: 5.07e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
406-483 |
6.57e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 56.64 E-value: 6.57e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
277-483 |
7.08e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 57.39 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGE---ILG------------IAGLvgagrtEAVQclfgvwpgrwQGEIFIDGQPVSisncQQAIAH-GIA 340
Cdd:COG3839 19 LKDIDLDIEDGEflvLLGpsgcgkstllrmIAGL------EDPT----------SGEILIGGRDVT----DLPPKDrNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 341 MVPEDrkkDGIVPVMAVGKNITLAALNQFTgamssldDAAEqhcIQQSIQR----LKIKtsspELAiGR----LSGGNQQ 412
Cdd:COG3839 79 MVFQS---YALYPHMTVYENIAFPLKLRKV-------PKAE---IDRRVREaaelLGLE----DLL-DRkpkqLSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 413 KAILARCLLLNPRILILDEPTRGIDigAK------YEIYKLINQLvqqGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLD--AKlrvemrAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-240 |
7.90e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 21 DNVSLRlNAGEVvSLCGENGSGK-STLMKvlcgiyphgsYEGEIIFAGETLQANHIRDTeRKGIAIIHQELALVkHLTVL 99
Cdd:PTZ00265 1248 QNVGMK-NVNEF-SLTKEGGSGEdSTVFK----------NSGKILLDGVDICDYNLKDL-RNLFSIVSQEPMLF-NMSIY 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 100 ENIFLGAEISRHglldyETMTLRCQklLAQVN-----LPISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:PTZ00265 1314 ENIKFGKEDATR-----EDVKRACK--FAAIDefiesLPNKYDTNVGPYGKslsgGQKQRIAIARALLREPKILLLDEAT 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 171 ASLTEQETATLLAIVRDLQNH-DIACIYISHKLNEVKAiSDTICVIRDGQHIGTRDASGMSEDDIITMMVG 240
Cdd:PTZ00265 1387 SSLDSNSEKLIEKTIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFNNPDRTGSFVQAHGTHEELLSVQDG 1456
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
279-484 |
1.01e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.50 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGR-WQGEI-----------FIDGQPVSISNCQQAiahGIAMVPEDr 346
Cdd:TIGR03269 18 NISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEpTSGRIiyhvalcekcgYVERPSKVGEPCPVC---GGTLEPEE- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 347 kKDGIVPVMAVGKNIT--LAALNQFTGA-----------MSSLDDAA--EQHCIQQSIQRLK-IKTSSPELAIGR-LSGG 409
Cdd:TIGR03269 94 -VDFWNLSDKLRRRIRkrIAIMLQRTFAlygddtvldnvLEALEEIGyeGKEAVGRAVDLIEmVQLSHRITHIARdLSGG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 410 NQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLG-LSDRVLVMHEGRLK 484
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEdLSDKAIWLENGEIK 248
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
406-476 |
1.14e-08 |
|
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: 1.14e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLvqqGIAVIVISSElPEVLGLSDRVL 476
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHR-PSLWKFHDRVL 158
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
404-502 |
1.16e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.81 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 404 GRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSElPEVLGLSDRVLVMHEGRL 483
Cdd:PRK10535 143 SQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
90
....*....|....*....
gi 489011807 484 KANLVNQHLTQEQVMEAAL 502
Cdd:PRK10535 222 VRNPPAQEKVNVAGGTEPV 240
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1-195 |
1.29e-08 |
|
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: 54.94 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 1 MTWllemKNITKTFGAVKA----VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGETLQANHir 76
Cdd:cd03232 4 LTW----KNLNYTVPVKGGkrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDKNF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 77 dteRKGIAIIHQELALVKHLTVLENIFLGAeisrhglldyetmTLRcqkllaqvnlpispdtrvgDLGLGQQQLVEIAKA 156
Cdd:cd03232 78 ---QRSTGYVEQQDVHSPNLTVREALRFSA-------------LLR-------------------GLSVEQRKRLTIGVE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489011807 157 LNKQVRLLILDEPTASLTEQETATLLAIVRDLQNH--DIAC 195
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSgqAILC 163
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
256-501 |
1.41e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.55 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLTAWHpvNRHiKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVwpGRWQGEIFIDGqpvSISNCQQAI 335
Cdd:PRK14239 3 EPILQVSDLSVYY--NKK-KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRM--NDLNPEVTITG---SIVYNGHNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 336 AHGIAMVPEDRKKDGIV-----PV-MAVGKNITLAALNQFTGAMSSLDDAAEQHCIQQSIQRlKIKTSSPELAIGrLSGG 409
Cdd:PRK14239 75 YSPRTDTVDLRKEIGMVfqqpnPFpMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWD-EVKDRLHDSALG-LSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 410 NQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSeLPEVLGLSDRVLVMHEGrlkaNLVN 489
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRS-MQQASRISDRTGFFLDG----DLIE 227
|
250
....*....|..
gi 489011807 490 QHLTQEQVMEAA 501
Cdd:PRK14239 228 YNDTKQMFMNPK 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
271-496 |
1.51e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 271 NRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwqGEIFIDGQPV-SISNCQqaiahgiamVPEDRKK 348
Cdd:PRK11831 19 NRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGqIAPDH--GEILFDGENIpAMSRSR---------LYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 349 dgivpvmavgknitLAALNQfTGA----MSSLDDAA---EQHC-----IQQSIQRLKIKT----SSPELAIGRLSGGNQQ 412
Cdd:PRK11831 86 --------------MSMLFQ-SGAlftdMNVFDNVAyplREHTqlpapLLHSTVMMKLEAvglrGAAKLMPSELSGGMAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 413 KAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRLKANLVNQH 491
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
....*
gi 489011807 492 LTQEQ 496
Cdd:PRK11831 231 LQANP 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
279-490 |
1.59e-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: 57.65 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGqpVSISNCQ-QAIAHGIAMVPEDrkkdgivPVMAV 357
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA-EGEIIIDG--LNIAKIGlHDLRFKITIIPQD-------PVLFS 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 358 GK-NITLAALNQFT--------------GAMSSLDDAAEQHCIQQSiqrlkiktsspelaiGRLSGGNQQKAILARCLLL 422
Cdd:TIGR00957 1374 GSlRMNLDPFSQYSdeevwwalelahlkTFVSALPDKLDHECAEGG---------------ENLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 423 NPRILILDEPTRGIDIgakyEIYKLINQLVQ---QGIAVIVISSELPEVLGLSdRVLVMHEGRLK-----ANLVNQ 490
Cdd:TIGR00957 1439 KTKILVLDEATAAVDL----ETDNLIQSTIRtqfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAefgapSNLLQQ 1509
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
405-483 |
1.60e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.53 E-value: 1.60e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
258-481 |
1.70e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.48 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTAWHPVNRHIKrvnDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQAIAH 337
Cdd:PRK11248 1 MLQISHLYADYGGKPALE---DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPVEGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 338 giamvpedrKKDGIVPVMAVGKNITlaalnqFTGAMSSLDDAAEQHCIQQSIQRLKIKTSSPELaIGRLSGGNQQKAILA 417
Cdd:PRK11248 77 ---------QNEGLLPWRNVQDNVA------FGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRY-IWQLSGGQRQRVGIA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 418 RCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQeTGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
259-483 |
1.73e-08 |
|
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: 57.06 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVNRHIkrVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPvsISNCQQAIAHG 338
Cdd:TIGR01193 474 IVINDVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNGFS--LKDIDRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 339 -IAMVPEDrkkdgivPVMAVG---KNITLAALNQFTGAMssLDDAAEQHCIQQSIQRLKIKTSSpELAI--GRLSGGNQQ 412
Cdd:TIGR01193 549 fINYLPQE-------PYIFSGsilENLLLGAKENVSQDE--IWAACEIAEIKDDIENMPLGYQT-ELSEegSSISGGQKQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 413 KAILARCLLLNPRILILDEPTRGIDIGAKYEIYKliNQLVQQGIAVIVISSELpEVLGLSDRVLVMHEGRL 483
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITEKKIVN--NLLNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
278-484 |
1.79e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 278 NDVSFSLRRGEILGIAGLVGAGRTEAVQCLfgvwpGRW----QGEIFIDG---QPVSISNCQQAIAhgiaMVPEDrkkdg 350
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLL-----TRFydidEGEILLDGhdlRDYTLASLRNQVA----LVSQN----- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 351 iVPVM--AVGKNITLAALNQFTGAmsSLDDAAEQHCIQQSIQRLK--IKTsspelAIGR----LSGGNQQKAILARCLLL 422
Cdd:PRK11176 426 -VHLFndTIANNIAYARTEQYSRE--QIEEAARMAYAMDFINKMDngLDT-----VIGEngvlLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 423 NPRILILDEPTRGIDIGAKYEIYKLINQLvQQGIAVIVISSELPEVLGlSDRVLVMHEGRLK 484
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
406-485 |
1.95e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.80 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGRLK 484
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
.
gi 489011807 485 A 485
Cdd:PRK13634 226 L 226
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-215 |
2.21e-08 |
|
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: 55.07 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 30 GEVVSLCGENGSGKSTLMKVLCG-IYPH-GSYEG-----EII--FAGETLQaNHIRDTERKGIAIIHQelalVKHLTVLE 100
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKPNlGKFDDppdwdEILdeFRGSELQ-NYFTKLLEGDVKVIVK----PQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 101 NIFLGAEISrhgLLDYETMTLRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETAT 180
Cdd:cd03236 101 KAVKGKVGE---LLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190
....*....|....*....|....*....|....*
gi 489011807 181 LLAIVRDLQNHDIACIYISHKLNEVKAISDTICVI 215
Cdd:cd03236 178 AARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-219 |
2.26e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.63 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNIT-----KTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG---------------IYPHGSYEGEI 63
Cdd:PRK13631 21 ILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGlikskygtiqvgdiyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 64 IFAGEtlqaNHIRDTE--RKGIAIIHQ--ELALVKHlTVLENIFLG------AEISRHGLLDY--ETMTLRcqkllaQVN 131
Cdd:PRK13631 101 TNPYS----KKIKNFKelRRRVSMVFQfpEYQLFKD-TIEKDIMFGpvalgvKKSEAKKLAKFylNKMGLD------DSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 132 LPISPdtrvGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDT 211
Cdd:PRK13631 170 LERSP----FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADE 245
|
....*...
gi 489011807 212 ICVIRDGQ 219
Cdd:PRK13631 246 VIVMDKGK 253
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-218 |
2.46e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.51 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTF-GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLcgiypHGSYE---GEIIFAGEtlqanHIRDTE 79
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-----QRVFDpqsGRILIDGT-----DIRTVT 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKG----IAIIHQElALVKHLTVLENIFLGaeisRHGLLDYETMTL--RCQKLLAQVNLPISPDTRVGDLGL----GQQQ 149
Cdd:PRK13657 404 RASlrrnIAVVFQD-AGLFNRSIEDNIRVG----RPDATDEEMRAAaeRAQAHDFIERKPDGYDTVVGERGRqlsgGERQ 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 150 LVEIAKALNKQVRLLILDEPTASL-TEQETATLLAIvrDLQNHDIACIYISHKLNEVKAiSDTICVIRDG 218
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALdVETEAKVKAAL--DELMKGRTTFIIAHRLSTVRN-ADRILVFDNG 545
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-232 |
2.66e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.41 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 18 KAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIY-P-HGSyegeiIFAGETLQANHIRDTE----RKGIAIIHQ--E 89
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPtSGT-----VTIGERVITAGKKNKKlkplRKKVGIVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 90 LALVKHlTVLENIFLGAeiSRHGLLDYETMtLRCQKLLAQVNLPISPDTRVG-DLGLGQQQLVEIAKALNKQVRLLILDE 168
Cdd:PRK13634 96 HQLFEE-TVEKDICFGP--MNFGVSEEDAK-QKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 169 PTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIrdgqHIGTRDASGMSED 232
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVM----HKGTVFLQGTPRE 232
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
259-482 |
3.62e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.19 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTAWHPVnrhiKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRWQgeifidgqpVSISNCQQAIAHG 338
Cdd:PRK15093 9 LTIEFKTSDGWV----KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWR---------VTADRMRFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 339 IAMVPEDRKKdgivpvmAVGKNITLAalnqFTGAMSSLDDAAE-QHCIQQSI----------QRLKI-KTSSPEL----- 401
Cdd:PRK15093 76 LRLSPRERRK-------LVGHNVSMI----FQEPQSCLDPSERvGRQLMQNIpgwtykgrwwQRFGWrKRRAIELlhrvg 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 402 -----AIGR-----LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLG 470
Cdd:PRK15093 145 ikdhkDAMRsfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQ 224
|
250
....*....|..
gi 489011807 471 LSDRVLVMHEGR 482
Cdd:PRK15093 225 WADKINVLYCGQ 236
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
274-482 |
3.64e-08 |
|
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: 53.81 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 274 IKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRWQ--GEIFIDGQPVSI--SNCQqaiaHGIAMVPEDrkkD 349
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSveGDIHYNGIPYKEfaEKYP----GEIIYVSEE---D 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 350 GIVPVMAVGKNITLAAL---NQFtgamsslddaaeqhciqqsiqrlkiktsspelaIGRLSGGNQQKAILARCLLLNPRI 426
Cdd:cd03233 93 VHFPTLTVRETLDFALRckgNEF---------------------------------VRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 427 LILDEPTRGIDIGAKYEIYKLINQLVQQ--GIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVlkTTTFVSLYQASDEIYDLFDKVLVLYEGR 197
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
406-462 |
3.75e-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: 52.45 E-value: 3.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAkyeIYKLINQLVQQGIAVIVIS 462
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES---IEALEEALKEYPGTVILVS 124
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
277-459 |
3.79e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.95 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwqGEIFIDGQPVS----------ISNCQQAiahgiamvped 345
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASlISPTS--GTLLFEGEDIStlkpeiyrqqVSYCAQT----------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 346 rkkdgivPVM---AVGKNITLAALNQftgamsslDDAAEQHCIQQSIQRLKIKTSSPELAIGRLSGGNQQKAILARCLLL 422
Cdd:PRK10247 90 -------PTLfgdTVYDNLIFPWQIR--------NQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 489011807 423 NPRILILDEPTRGIDIGAKYEIYKLINQLV-QQGIAVI 459
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVL 192
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
278-482 |
4.92e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 53.92 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 278 NDVSFSLRRGEILGIAGLVGAGRTEavqcLFGVWPGRW-----QGEIFIDGQpvSISNcqqaiahgiaMVPEDRKKDGI- 351
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKST----LAKVLMGHPkyevtSGSILLDGE--DILE----------LSPDERARAGIf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 352 ------VPVMAVgKNITL--AALNQFTGAMSSLDDAAEQhcIQQSIQRLKIKTS--SPELAIGrLSGGNQQKAILARCLL 421
Cdd:COG0396 81 lafqypVEIPGV-SVSNFlrTALNARRGEELSAREFLKL--LKEKMKELGLDEDflDRYVNEG-FSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 422 LNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVIsSELPEVLGL--SDRVLVMHEGR 482
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILII-THYQRILDYikPDFVHVLVDGR 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-438 |
5.17e-08 |
|
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: 55.33 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 7 MKNITKTFGAVKAV-DNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIypHGSYEGEIIFAgetlqanhirdterKGIAI 85
Cdd:TIGR03719 7 MNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV--DKDFNGEARPQ--------------PGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 86 --IHQELALVKHLTVLENIFLGAEISRHGLLDYETMTL-----------------RCQKLLAQVN--------------- 131
Cdd:TIGR03719 71 gyLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAkyaepdadfdklaaeqaELQEIIDAADawdldsqleiamdal 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 132 -LPiSPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLlaiVRDLQNHDIACIYISHK---LNEV-- 205
Cdd:TIGR03719 151 rCP-PWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL---ERHLQEYPGTVVAVTHDryfLDNVag 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 206 ---------------------------------------KAISDTICVIRDG---------------QHIGTRDASGMSE 231
Cdd:TIGR03719 227 wileldrgrgipwegnysswleqkqkrleqeekeesarqKTLKRELEWVRQSpkgrqakskarlaryEELLSQEFQKRNE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 232 DDIITMMVGRELtalypsephahGEEILRVEHLTawhpvnrhiKR------VNDVSFSLRRGEILGIAGLVGAGRTeavq 305
Cdd:TIGR03719 307 TAEIYIPPGPRL-----------GDKVIEAENLT---------KAfgdkllIDDLSFKLPPGGIVGVIGPNGAGKS---- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 306 CLFGVWPGRWQ---GEIFIdGQPVSisncqqaiahgIAMVpeDRKKDGIVPVMAVGKNIT----LAALNQFTgaMSSldd 378
Cdd:TIGR03719 363 TLFRMITGQEQpdsGTIEI-GETVK-----------LAYV--DQSRDALDPNKTVWEEISggldIIKLGKRE--IPS--- 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 379 aaeqhciQQSIQRLKIKTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDI 438
Cdd:TIGR03719 424 -------RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
277-484 |
5.69e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.32 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGR-TEAVQCLFGVWPGrwQGEIFIDGQPVSISNCQQAIAHGIAMV---PEDRKKDGIV 352
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKsTIAKHMNALLIPS--EGKVYVDGLDTSDEENLWDIRNKAGMVfqnPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 353 PV-MAVG-KNITLAALNqftgAMSSLDDAAEqhciqqSIQRLKIKTSSPELaigrLSGGNQQKAILARCLLLNPRILILD 430
Cdd:PRK13633 104 EEdVAFGpENLGIPPEE----IRERVDESLK------KVGMYEYRRHAPHL----LSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 431 EPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGlSDRVLVMHEGRLK 484
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
259-459 |
5.84e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 53.25 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 259 LRVEHLTawhpVNRHIKR-VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPG--RWQGEIFIDGQPVsisNCQQAI 335
Cdd:COG4136 2 LSLENLT----ITLGGRPlLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafSASGEVLLNGRRL---TALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 336 AHGIAMVPEDrkkDGIVPVMAVGKNITLAALNQFTGAmsslddaAEQHCIQQSIQRLkiktsspELA------IGRLSGG 409
Cdd:COG4136 75 QRRIGILFQD---DLLFPHLSVGENLAFALPPTIGRA-------QRRARVEQALEEA-------GLAgfadrdPATLSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489011807 410 NQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLI-NQLVQQGIAVI 459
Cdd:COG4136 138 QRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPAL 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-214 |
6.14e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.18 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGavkavdNVSLR-----LNAGEVVSLCGENGSGKSTLMKVLCGI-------------------YPHGSY 59
Cdd:COG1245 341 LVEYPDLTKSYG------GFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVlkpdegevdedlkisykpqYISPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 60 EGEIifagETLQANHIRDTerkgiaiihqelalvkhltvLENIFLGAEISRHglldyetmtLRCQKLLaqvnlpispDTR 139
Cdd:COG1245 415 DGTV----EEFLRSANTDD--------------------FGSSYYKTEIIKP---------LGLEKLL---------DKN 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 140 VGDLGLGQQQLVEIAKALNKQVRLLILDEPTASL-TEQETATLLAIVRDLQNHDIACIYISHKLNEVKAISDTICV 214
Cdd:COG1245 453 VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLdVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-219 |
6.63e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.27 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 30 GEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGETLQANHIRDTerkgiAIIHQELALVKHLTVLENIFLGAEIS 109
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRT-----GFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 110 RHGLLDYETMTLRCQKLLAQVNLPISPDTRVGD-----LGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAI 184
Cdd:PLN03211 169 LPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190
....*....|....*....|....*....|....*.
gi 489011807 185 VRDLQNHDIACIYISHK-LNEVKAISDTICVIRDGQ 219
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
281-479 |
7.25e-08 |
|
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: 53.52 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 281 SFSLRR------GEILGIAGLVGAGRTEAVQCLFG-VWP--GRWQGEifidgqpvsiSNCQQAIAH--GIAMVP--EDRK 347
Cdd:cd03236 14 SFKLHRlpvpreGQVLGLVGPNGIGKSTALKILAGkLKPnlGKFDDP----------PDWDEILDEfrGSELQNyfTKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 348 KDGIVPVMAVgKNITLAAlNQFTGAMSS-LDDAAEQHCIQQSIQRLKIKtSSPELAIGRLSGGNQQKAILARCLLLNPRI 426
Cdd:cd03236 84 EGDVKVIVKP-QYVDLIP-KAVKGKVGElLKKKDERGKLDELVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489011807 427 LILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMH 479
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
256-511 |
7.66e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.48 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLTAwhpVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRWQGEIFID--GQPVsisNCQQ 333
Cdd:PRK09984 2 QTIIRVEKLAK---TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIEllGRTV---QREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 334 AIAHGIAmvpEDRKKDG-------IVPVMAVGKNITLAALNQ---FTGAMSSLDDAAEQHCIQqSIQRLKIKTSSPElAI 403
Cdd:PRK09984 76 RLARDIR---KSRANTGyifqqfnLVNRLSVLENVLIGALGStpfWRTCFSWFTREQKQRALQ-ALTRVGMVHFAHQ-RV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 404 GRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAK---YEIYKLINQlvQQGIAVIVISSELPEVLGLSDRVLVMHE 480
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESArivMDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQ 228
|
250 260 270
....*....|....*....|....*....|.
gi 489011807 481 GRLKANLVNQHLTQEQvMEAALRSERHVEEH 511
Cdd:PRK09984 229 GHVFYDGSSQQFDNER-FDHLYRSINRVEEN 258
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
277-485 |
7.77e-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: 52.92 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSIsncqqaIAHGIAMVPEdrkkdgivpvMA 356
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD-SGTVTVRGRVSSL------LGLGGGFNPE----------LT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNITlaalnqFTGAMSSLDDAaeqhCIQQSIQR------------LKIKTSSpelaigrlSGgnqQKAILARCL--LL 422
Cdd:cd03220 101 GRENIY------LNGRLLGLSRK----EIDEKIDEiiefselgdfidLPVKTYS--------SG---MKARLAFAIatAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 423 NPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
280-483 |
1.05e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 280 VSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRwqGEIFIDGQPVSisncqqaiAHGIAmvpEDRKKDGIVP---VM 355
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRiVELER--GRILIDGCDIS--------KFGLM---DLRKVLGIIPqapVL 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVGK-NITLAALNQFTGA--MSSLDDAAEQHCIQQSIQRLKIKTSSpelAIGRLSGGNQQKAILARCLLLNPRILILDEP 432
Cdd:PLN03130 1325 FSGTvRFNLDPFNEHNDAdlWESLERAHLKDVIRRNSLGLDAEVSE---AGENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489011807 433 TRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPEVLGlSDRVLVMHEGRL 483
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIREEF-KSCTMLIIAHRLNTIID-CDRILVLDAGRV 1450
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
385-438 |
1.10e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 489011807 385 IQQSIQRLKIktsSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDI 438
Cdd:PRK11147 139 INEVLAQLGL---DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
258-490 |
1.13e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.57 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLTAWHPVNRhiKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGV-WPGrwQGEIFIDGQPVSISNCQQA-- 334
Cdd:PRK10908 1 MIRFEHVSKAYLGGR--QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPS--AGKIWFSGHDITRLKNREVpf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 335 IAHGIAMVPEDRKkdgIVPVMAVGKNITLAALnqFTGAmsSLDDAAEQhcIQQSIQRLKIKTSSPELAIgRLSGGNQQKA 414
Cdd:PRK10908 77 LRRQIGMIFQDHH---LLMDRTVYDNVAIPLI--IAGA--SGDDIRRR--VSAALDKVGLLDKAKNFPI-QLSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 415 ILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKANLVNQ 490
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
219-483 |
1.21e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.45 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 219 QHIGTRDASGMSEDDIITmmvgRELTALYPSEPHAHGEEI-LRVEHLTAWHPvNRHIKRVNDVSFSLRRGEILGIAGLVG 297
Cdd:PRK11160 302 QHLGQVIASARRINEITE----QKPEVTFPTTSTAAADQVsLTLNNVSFTYP-DQPQPVLKGLSLQIKAGEKVALLGRTG 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 298 AGRTEAVQCLFGVWPGRwQGEIFIDGQPVSiSNCQQAIAHGIAMVPEdRkkdgiVPVMA--VGKNITLAAlnqftgamSS 375
Cdd:PRK11160 377 CGKSTLLQLLTRAWDPQ-QGEILLNGQPIA-DYSEAALRQAISVVSQ-R-----VHLFSatLRDNLLLAA--------PN 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 376 LDDAAEQHCIQQ--------SIQRLkiktsspELAIG----RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYE 443
Cdd:PRK11160 441 ASDEALIEVLQQvgleklleDDKGL-------NAWLGeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQ 513
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489011807 444 IYKLINQlVQQGIAVIVISSELpevLGLS--DRVLVMHEGRL 483
Cdd:PRK11160 514 ILELLAE-HAQNKTVLMITHRL---TGLEqfDRICVMDNGQI 551
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-168 |
1.44e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.95 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAGETLqaNHIR-DTERKGIAIIHQELALVKHlT 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF--DVSEGDIRFHDIPL--TKLQlDSWRSRLAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 98 VLENIFLG------AEISRHGlldyetmtlrcqkLLAQV-----NLPISPDTRVGDLGL----GQQQLVEIAKALNKQVR 162
Cdd:PRK10789 405 VANNIALGrpdatqQEIEHVA-------------RLASVhddilRLPQGYDTEVGERGVmlsgGQKQRISIARALLLNAE 471
|
....*.
gi 489011807 163 LLILDE 168
Cdd:PRK10789 472 ILILDD 477
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-219 |
1.46e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTERKgIA 84
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT--PAHGHVWLDGEHIQHYASKEVARR-IG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVleniflgAEISRHGLLDYETMTLRCQK--------LLAQVNLPISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:PRK10253 85 LLAQNATTPGDITV-------QELVARGRYPHQPLFTRWRKedeeavtkAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 157 LNKQVRLLILDEPTASLTEQETATLLAIVRDL---QNHDIACIYisHKLNEVKAISDTICVIRDGQ 219
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELnreKGYTLAAVL--HDLNQACRYASHLIALREGK 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
277-483 |
1.75e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.25 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISncQQAIAHGIAMVPEdrkKDGIVPVMA 356
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT-SGTVLVGGKDIETN--LDAVRQSLGMCPQ---HNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 357 VGKNITLAAlnQFTGamSSLDDAaeQHCIQQSIQRLKIKTSSPELAiGRLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:TIGR01257 1020 VAEHILFYA--QLKG--RSWEEA--QLEMEAMLEDTGLHHKRNEEA-QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489011807 437 DIGAKYEIYKLINQLvQQGIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-219 |
2.21e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 51.32 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 22 NVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHgsYEGEIIFAGetlqanhirdterkGIAIIHQElALVKHLTVLEN 101
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK--LSGSVSVPG--------------SIAYVSQE-PWIQNGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 102 IFLGAEisrhglLD---YETmTLRCQKLLAQV-NLPISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPTASL 173
Cdd:cd03250 86 ILFGKP------FDeerYEK-VIKACALEPDLeILPDGDLTEIGEKGInlsgGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489011807 174 tEQETATLL---AIVRDLQNHDiACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:cd03250 159 -DAHVGRHIfenCILGLLLNNK-TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-182 |
2.75e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 26 RLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIifagetlQANHIRDTER-KGIAIIHQELALVKHLTVLENI-F 103
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-------DGKTATRGDRsRFMAYLGHLPGLKADLSTLENLhF 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 104 LGAEISRHGlldyETMTlrcQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLtEQETATLL 182
Cdd:PRK13543 106 LCGLHGRRA----KQMP---GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL-DLEGITLV 176
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
258-483 |
3.09e-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: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 258 ILRVEHLT-AWHPVNRHIKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLfgvwpgrwQGEIFIDGQPVS-ISNCQ-QA 334
Cdd:COG1135 1 MIELENLSkTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInlle-rptSGSVLVDGVDLTaLSERElRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 335 IAHGIAMVPE-----DRKKdgivpvmaVGKNITL----------------AALNQFTGamssLDDAAEQHciqqsiqrlk 393
Cdd:COG1135 80 ARRKIGMIFQhfnllSSRT--------VAENVALpleiagvpkaeirkrvAELLELVG----LSDKADAY---------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 394 iktssPElaigRLSGGNQQK-AIlARCLLLNPRILILDEPTRGIDIGAKYEIYKL---INQlvQQGIAVIVISSELPEVL 469
Cdd:COG1135 138 -----PS----QLSGGQKQRvGI-ARALANNPKVLLCDEATSALDPETTRSILDLlkdINR--ELGLTIVLITHEMDVVR 205
|
250
....*....|....
gi 489011807 470 GLSDRVLVMHEGRL 483
Cdd:COG1135 206 RICDRVAVLENGRI 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
256-484 |
3.23e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.32 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 256 EEILRVEHLTAWHPVNRH-IKRVNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQA 334
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHeLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS-SGEVSLVGQPLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 335 IAHGIAMVPEDRKKDGIVPVMAVGKNITLAALnqftgamssLDDAAEQHCIQQSIQRLKiktsspELAIGR--------L 406
Cdd:PRK10584 83 AKLRAKHVGFVFQSFMLIPTLNALENVELPAL---------LRGESSRQSRNGAKALLE------QLGLGKrldhlpaqL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 407 SGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLK 484
Cdd:PRK10584 148 SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-232 |
3.43e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVD---NVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYphGSYEGEIIFAgetlQANHIRDTE-- 79
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY--DPTEGDIIIN----DSHNLKDINlk 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 --RKGIAIIHQE---------------LALVKHLTVLENIF---------------------------LGAEISRHGLL- 114
Cdd:PTZ00265 457 wwRSKIGVVSQDpllfsnsiknnikysLYSLKDLEALSNYYnedgndsqenknkrnscrakcagdlndMSNTTDSNELIe 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 115 ---DYETMTLR-----CQKLLAQ---VNLPISPDTRVGD----LGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETA 179
Cdd:PTZ00265 537 mrkNYQTIKDSevvdvSKKVLIHdfvSALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489011807 180 TLLAIVRDLQ-NHDIACIYISHKLNEVKaISDTICVIRDGQHIGTRDASGMSED 232
Cdd:PTZ00265 617 LVQKTINNLKgNENRITIIIAHRLSTIR-YANTIFVLSNRERGSTVDVDIIGED 669
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-225 |
3.54e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVslrLNAGEVVSLCGENGSGKSTLMKVLCG-IYP-HGSYEGEIIFAGETLqaNHIRDTERK 81
Cdd:TIGR00956 64 KLKKFRDTKTFDILKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIASnTDGfHIGVEGVITYDGITP--EEIKKHYRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 82 GIAIIHQELALVKHLTVLENIFLGAEI----SRHGLLDYETMTLRCQKL-LAQVNLPISPDTRVGD-----LGLGQQQLV 151
Cdd:TIGR00956 139 DVVYNAETDVHFPHLTVGETLDFAARCktpqNRPDGVSREEYAKHIADVyMATYGLSHTRNTKVGNdfvrgVSGGERKRV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 152 EIAKALNKQVRLLILDEPTASLteqETATLLAIVRDLQN-----HDIACIYISHKLNEVKAISDTICVIRDGQHI--GTR 224
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGL---DSATALEFIRALKTsanilDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIyfGPA 295
|
.
gi 489011807 225 D 225
Cdd:TIGR00956 296 D 296
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
405-481 |
4.34e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.01 E-value: 4.34e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:PRK10851 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-482 |
4.58e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 9 NITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG--IYPHGSYEgeiIFAGETLQANHiRDTERKGIAII 86
Cdd:NF033858 6 GVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarKIQQGRVE---VLGGDMADARH-RRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 87 HQELA--LVKHLTVLENI-FLG-------AEisRHGlldyetmtlRCQKLLAQVNLPISPDTRVGDLGLGQQQLVEIAKA 156
Cdd:NF033858 82 PQGLGknLYPTLSVFENLdFFGrlfgqdaAE--RRR---------RIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 157 LNKQVRLLILDEPTAS---LTEQETATLLAIVRDlQNHD----IACIYIshklnEVKAISDTICVIRDGQHIGT------ 223
Cdd:NF033858 151 LIHDPDLLILDEPTTGvdpLSRRQFWELIDRIRA-ERPGmsvlVATAYM-----EEAERFDWLVAMDAGRVLATgtpael 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 224 --RDASGMSEDDIITMM-----VGRELTALYPSEPHAHGEEILRVEHLTawhpvnrhiKR------VNDVSFSLRRGEIL 290
Cdd:NF033858 225 laRTGADTLEAAFIALLpeekrRGHQPVVIPPRPADDDDEPAIEARGLT---------MRfgdftaVDHVSFRIRRGEIF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 291 GIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSisncqqaiAHGIAMvpedRKKdgiVPVMA----------VGKN 360
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPAS-EGEAWLFGQPVD--------AGDIAT----RRR---VGYMSqafslygeltVRQN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 361 ITL-AALNQFTGAmssldDAAEQhcIQQSIQRLKIKTSSPELAiGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIG 439
Cdd:NF033858 360 LELhARLFHLPAA-----EIAAR--VAEMLERFDLADVADALP-DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 489011807 440 AKYEIYKLINQLV-QQGIaVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:NF033858 432 ARDMFWRLLIELSrEDGV-TIFISTHFMNEAERCDRISLMHAGR 474
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
278-482 |
5.85e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.85 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 278 NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNcQQAIAHGIAMVPEDRKKdGIVPVMAV 357
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD-SGSILIDGKDVTKLP-EYKRAKYIGRVFQDPMM-GTAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 358 GKNITLAAL----------------NQFTGAMSSLDDAAEQhciqqsiqRLKIKtsspelaIGRLSGGNQQKAILARCLL 421
Cdd:COG1101 100 EENLALAYRrgkrrglrrgltkkrrELFRELLATLGLGLEN--------RLDTK-------VGLLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489011807 422 LNPRILILDEPTRGIDIGAKYEIYKLINQLVQ-QGIAVIVISSELPEVLGLSDRVLVMHEGR 482
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAALVLELTEKIVEeNNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
406-483 |
6.73e-07 |
|
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: 50.51 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGID--IGAKyeIYKLINQLVQ-QGIAVIVISSElPEVLGLSDRVLVMHEGR 482
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDaaTGEQ--IIDLLFELNReRGTTLVLVTHD-PALAARCDRVLRLRAGR 223
|
.
gi 489011807 483 L 483
Cdd:COG4181 224 L 224
|
|
| 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 489011807 405 RLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQL 451
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-170 |
7.57e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFaGETLQANHIrDTERKGIA 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDS--GTIKI-GETVKLAYV-DQSRDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 iihqelalvKHLTVLENIFLGAEISRHGllDYEtMTLRC------------QKllaqvnlpispdtRVGDLGLGQQQLVE 152
Cdd:PRK11819 401 ---------PNKTVWEEISGGLDIIKVG--NRE-IPSRAyvgrfnfkggdqQK-------------KVGVLSGGERNRLH 455
|
170
....*....|....*...
gi 489011807 153 IAKALNKQVRLLILDEPT 170
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPT 473
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-63 |
7.92e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 7.92e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 5 LEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEI 63
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDS--GTV 376
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
396-486 |
8.53e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 396 TSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRV 475
Cdd:NF000106 135 TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHEL 214
|
90
....*....|.
gi 489011807 476 LVMHEGRLKAN 486
Cdd:NF000106 215 TVIDRGRVIAD 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
404-483 |
9.11e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.23 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 404 GRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSElPEVLGLSDRVLVMHEGRL 483
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSP-AQAARVSDYVAFLYLGKL 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
249-460 |
9.88e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.17 E-value: 9.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 249 SEPHAHGEEILRVEHLTAWHPVNRHIKrvnDVSFSLRRGEILGIAGLVGAGRTEAVQC---LFGVWPG-RWQGEIFIDGQ 324
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfRVEGKVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 325 PVSISNCQQAiahgiamvpEDRKKDGIV-----PV-MAVGKNITLAA-LNQFTGAMSSLDDAAEQHCIQQSIQRLKIKTS 397
Cdd:PRK14243 78 NLYAPDVDPV---------EVRRRIGMVfqkpnPFpKSIYDNIAYGArINGYKGDMDELVERSLRQAALWDEVKDKLKQS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489011807 398 SpeLAigrLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIV 460
Cdd:PRK14243 149 G--LS---LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-219 |
1.37e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 23 VSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFAGETLQANHIRDTeRKGIAIIHQELALVKHlTVLENI 102
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE--LEKGRIMIDDCDVAKFGLTDL-RRVLSIIPQSPVLFSG-TVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 103 flgAEISRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDLG----LGQQQLVEIAKALNKQVRLLILDEPTASLTEQET 178
Cdd:PLN03232 1331 ---DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGenfsVGQRQLLSLARALLRRSKILVLDEATASVDVRTD 1407
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489011807 179 ATLLAIVRDlQNHDIACIYISHKLNEVKAiSDTICVIRDGQ 219
Cdd:PLN03232 1408 SLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-169 |
1.58e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.23 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTF-GAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLqaNHIRDTERkGI 83
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITS--GEIWIGGRVV--NELEPADR-DI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 84 AIIHQELALVKHLTVLENIFLG--------AEISRhglldyetmtlRCQKlLAQVnLPISP--DTRVGDLGLGQQQLVEI 153
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYGlkirgmpkAEIEE-----------RVAE-AARI-LELEPllDRKPRELSGGQRQRVAM 145
|
170
....*....|....*.
gi 489011807 154 AKALNKQVRLLILDEP 169
Cdd:PRK11650 146 GRAIVREPAVFLFDEP 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
406-500 |
1.58e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGRLKA 485
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTG 1438
|
90
....*....|....*
gi 489011807 486 NLVNQHLTQEQVMEA 500
Cdd:PTZ00265 1439 SFVQAHGTHEELLSV 1453
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
406-495 |
1.67e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVIS---SELPEVLG----LSDRVLVm 478
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLnrfDEIPDFVQfagvLADCTLA- 214
|
90
....*....|....*..
gi 489011807 479 HEGRlKANLVNQHLTQE 495
Cdd:PRK10938 215 ETGE-REEILQQALVAQ 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
280-468 |
1.76e-06 |
|
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: 48.51 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 280 VSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQA-----IAHgiamvpedrkKDGIVPV 354
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPD-SGEVRWNGTPLAEQRDEPHenilyLGH----------LPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 355 MAVGKNIT-LAALNQftGAMSSLDDAAEQHCIqqsiqrlkikTSSPELAIGRLSGGNQQKAILARCLLLNPRILILDEPT 433
Cdd:TIGR01189 88 LSALENLHfWAAIHG--GAQRTIEDALAAVGL----------TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 489011807 434 RGIDIGAKYEIYKLINQ-LVQQGIAVIVISSELPEV 468
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLV 191
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-77 |
1.88e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 1.88e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489011807 5 LEMKNITKTFGAVK-AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSyeGEIIFAGETLQANHIRD 77
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS--GEILLDGKPVTAEQPED 394
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-52 |
3.07e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 3.07e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489011807 9 NITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG 52
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGG 49
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-170 |
3.20e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 7 MKNITKTFGAVKAV-DNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIIFA-GETlqanhirdterkgIA 84
Cdd:PRK11819 9 MNRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK--EFEGEARPApGIK-------------VG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 85 IIHQELALVKHLTVLENIFLG-AEIsrHGLLD-----YETMTL-------------RCQKLLAQVN-------------- 131
Cdd:PRK11819 74 YLPQEPQLDPEKTVRENVEEGvAEV--KAALDrfneiYAAYAEpdadfdalaaeqgELQEIIDAADawdldsqleiamda 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489011807 132 --LPiSPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPT 170
Cdd:PRK11819 152 lrCP-PWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-234 |
3.61e-06 |
|
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: 49.23 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 18 KAVDNVSLRLNAGEVVsLCGENGSGKSTLMKVLCGIYPHGSYEG-------------------EIIFAG--ETLQANHIR 76
Cdd:COG3593 12 RSIKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSRKfdeedfylgddpdlpeieiELTFGSllSRLLRLLLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 77 DTERKGIAIIHQEL---------ALVKHLT-VLENIFLGAEISRHGLLDYETMTLRcqklLAQVNLPISPDTRVGDLGLG 146
Cdd:COG3593 91 EEDKEELEEALEELneelkealkALNELLSeYLKELLDGLDLELELSLDELEDLLK----SLSLRIEDGKELPLDRLGSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 147 QQQLVEIA-------KALNKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHK---LNEVKaISDTICVIR 216
Cdd:COG3593 167 FQRLILLAllsalaeLKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSphlLSEVP-LENIRRLRR 245
|
250
....*....|....*...
gi 489011807 217 DGQHIGTRDASGMSEDDI 234
Cdd:COG3593 246 DSGGTTSTKLIDLDDEDL 263
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
279-459 |
3.84e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 47.95 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNCQQAIA---HgiamvpedrkKDGIVPVM 355
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPA-AGTIKLDGGDIDDPDVAEACHylgH----------RNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 AVGKNITLAAlNQFTGAMSSLDDAAEqhCIQqsIQRLKiktsspELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRG 435
Cdd:PRK13539 89 TVAENLEFWA-AFLGGEELDIAAALE--AVG--LAPLA------HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*
gi 489011807 436 IDIGAKYEIYKLI-NQLVQQGIAVI 459
Cdd:PRK13539 158 LDAAAVALFAELIrAHLAQGGIVIA 182
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
401-478 |
4.62e-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: 46.93 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 401 LAIGR----LSGGNQQKAILARCLLLNPR--ILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSElPEVLGLSDR 474
Cdd:cd03238 79 LTLGQklstLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADW 157
|
....
gi 489011807 475 VLVM 478
Cdd:cd03238 158 IIDF 161
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-191 |
5.86e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 6 EMKNITKTFGaVKA-----VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGsyegeIIFAGETLQANHIRDTE- 79
Cdd:TIGR00956 761 HWRNLTYEVK-IKKekrviLNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTG-----VITGGDRLVNGRPLDSSf 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 80 RKGIAIIHQELALVKHLTVLENIFLGAEISR-HGLLDYETMTLrCQKLLAQVNLPISPDTRVGDLGLG----QQQLVEIA 154
Cdd:TIGR00956 835 QRSIGYVQQQDLHLPTSTVRESLRFSAYLRQpKSVSKSEKMEY-VEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIG 913
|
170 180 190
....*....|....*....|....*....|....*...
gi 489011807 155 KALNKQVRLLI-LDEPTASLTEQETATLLAIVRDLQNH 191
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH 951
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
278-481 |
9.70e-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: 46.47 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 278 NDVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGRWQGEIFIDGQPV------SISNCQQAIAH-GIAMVPEdrkkd 349
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGrKTAGVITGEILINGRPLdknfqrSTGYVEQQDVHsPNLTVRE----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 350 givpvmavgknitlaALnQFTGAMSSLddaaeqhciqqSIQRLKIKTSSPELAIgrlsggnqqkailarclllNPRILIL 429
Cdd:cd03232 99 ---------------AL-RFSALLRGL-----------SVEQRKRLTIGVELAA-------------------KPSILFL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489011807 430 DEPTRGIDIGAKYEIYKLINQLVQQGIAVIV-ISSELPEVLGLSDRVLVMHEG 481
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKLADSGQAILCtIHQPSASIFEKFDRLLLLKRG 185
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-228 |
1.01e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 17 VKAVDNVSLRLNAGEVVSLCGENGSGKSTLmkVLCGIYphgsyegeiifagETLQANHIRDTERKGiaiiHQELALVKHL 96
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY-------------ASGKARLISFLPKFS----RNKLIFIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 97 TVLENIFLGaeisrhglldYetmtlrcqkllaqvnlpISPDTRVGDLGLGQQQLVEIAKALNKQVR--LLILDEPTASLT 174
Cdd:cd03238 69 QFLIDVGLG----------Y-----------------LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489011807 175 EQETATLLAIVRDLQNHDIACIYISHKLnEVKAISDTICVI--RDGQHIGTRDASG 228
Cdd:cd03238 122 QQDINQLLEVIKGLIDLGNTVILIEHNL-DVLSSADWIIDFgpGSGKSGGKVVFSG 176
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-194 |
1.65e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 37 GENGSGKSTLMKVLCGIYPHGSyeGEIIFagetlQANHIRDTERKGIAIIHQELALVKHLTVLENIFLGAEISRHGLLDY 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSS--GNIYY-----KNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLY 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 117 ETMT-LRCQKLLaqvnlpispDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQEtatllaivRDLQNHDIA 194
Cdd:PRK13541 106 AAIHyFKLHDLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN--------RDLLNNLIV 167
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
277-464 |
2.32e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.33 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRwQGEIFIDGQPVSISNC---QQAIAHGiamvpedrKKDGIVP 353
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE-KGEILFERQSIKKDLCtyqKQLCFVG--------HRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 354 vmavgkNITLAALNQFTGAMSSLDDAAEQHCIQQSIQRLKiktsspELAIGRLSGGNQQKAILARCLLLNPRILILDEPT 433
Cdd:PRK13540 88 ------YLTLRENCLYDIHFSPGAVGITELCRLFSLEHLI------DYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|.
gi 489011807 434 RGIDIGAKYEIYKLINQLVQQGIAVIVISSE 464
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
279-481 |
2.41e-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: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFG-VWPGrwQGEIFIDGQpvsISNCQQAiahgiamvpedrkkDGIVPvMAV 357
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPS--EGKIKHSGR---ISFSPQT--------------SWIMP-GTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 358 GKNItLAALNQFTGAMSSLDDAAEqhcIQQSIQRLKIKTSSPELAIG-RLSGGNQQKAILARCLLLNPRILILDEPTRGI 436
Cdd:TIGR01271 504 KDNI-IFGLSYDEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489011807 437 DIGAKYEIYK--LINQLVQQgiAVIVISSELpEVLGLSDRVLVMHEG 481
Cdd:TIGR01271 580 DVVTEKEIFEscLCKLMSNK--TRILVTSKL-EHLKKADKILLLHEG 623
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-253 |
2.59e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.85 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 5 LEMKNITKTfGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHG--SYEGEIIFAGETLQANHIRdterkG 82
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrQTAGRVLLDGKPVAPCALR-----G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 83 IAIIhqelalvkhlTVLENiflgaeiSRHGLLDYETMTLRCQKLLAQVNLPISPDTRVGDL---GL-------------- 145
Cdd:PRK10418 79 RKIA----------TIMQN-------PRSAFNPLHTMHTHARETCLALGKPADDATLTAALeavGLenaarvlklypfem 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 146 --GQQQLVEIAKALNKQVRLLILDEPTASLTEQETATLLAIVRDL-QNHDIACIYISHKLNEVKAISDTICVIRDGQHIG 222
Cdd:PRK10418 142 sgGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
250 260 270
....*....|....*....|....*....|....
gi 489011807 223 TRDASGM---SEDDIITMMVGRELtALYPSEPHA 253
Cdd:PRK10418 222 QGDVETLfnaPKHAVTRSLVSAHL-ALYGMELAS 254
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
279-460 |
5.36e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.41 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 279 DVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPgRWQGEIFIDGQPvsISNCQQA-------IAHgiamvpedrkKDGI 351
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR-PDAGEVLWQGEP--IRRQRDEyhqdllyLGH----------QPGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 352 VPVMAVGKNIT-LAALNQFTGamsslDDAAEQHCIQQSIQRLKiktsspELAIGRLSGGNQQKAILARCLLLNPRILILD 430
Cdd:PRK13538 86 KTELTALENLRfYQRLHGPGD-----DEALWEALAQVGLAGFE------DVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|
gi 489011807 431 EPTRGIDIGAKYEIYKLINQLVQQGIAVIV 460
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQGGMVIL 184
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
348-479 |
6.00e-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: 43.71 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 348 KDGIVPVMaVGKNIT--LAALNQFTGAMSSLDDAAEQHCIQQSIQRLKIKtsspelaigrLSGGNQQKAILARCLLLNPR 425
Cdd:cd03222 23 KEGEVIGI-VGPNGTgkTTAVKILAGQLIPNGDNDEWDGITPVYKPQYID----------LSGGELQRVAIAAALLRNAT 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489011807 426 ILILDEPTRGIDIGAKYEIYKLINQLVQQGI-AVIVISSELPEVLGLSDRVLVMH 479
Cdd:cd03222 92 FYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
389-479 |
6.58e-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: 45.55 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 389 IQRLKIKTSSpELAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELpEV 468
Cdd:COG1245 197 AEKLGLENIL-DRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL-AI 274
|
90
....*....|..
gi 489011807 469 LG-LSDRVLVMH 479
Cdd:COG1245 275 LDyLADYVHILY 286
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
404-485 |
6.68e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 404 GRLSGGNQQKaiLARC--LLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ--GIAVIVISSELPEVLGLsDRVLVMH 479
Cdd:NF033858 135 GKLSGGMKQK--LGLCcaLIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMD 211
|
....*.
gi 489011807 480 EGRLKA 485
Cdd:NF033858 212 AGRVLA 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
407-483 |
1.41e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 1.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 407 SGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVIS--SELPEVLgLSDRVLVMHEGRL 483
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIThyQRLLDYI-KPDYVHVMQNGKI 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
283-477 |
1.68e-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: 43.17 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 283 SLRRGEILGIAGLVGAGRTEAVQCLFGVW-PGrwQGEIFIDGQPVSISNcQQAIAhgiamvpedrKKDGIVPVMAVGKNI 361
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLkPD--EGDIEIELDTVSYKP-QYIKA----------DYEGTVRDLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 362 TLAALNQF-TGAMSSLDdaaeqhcIQQSIQRLkiktsspelaIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGA 440
Cdd:cd03237 88 DFYTHPYFkTEIAKPLQ-------IEQILDRE----------VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 489011807 441 KYEIYKLINQLVQQGIA-VIVISSELPEVLGLSDRVLV 477
Cdd:cd03237 151 RLMASKVIRRFAENNEKtAFVVEHDIIMIDYLADRLIV 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
277-510 |
1.75e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 277 VNDVSFSLRRGEILGIAGLVGAGRTEAVQCLFGVWPGRWQGEIFIDGQpvsisncqqaiahgIAMVPEdrkkdgiVPVM- 355
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGS--------------VAYVPQ-------VSWIf 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 356 --AVGKNITLAALNQFTGAMSSLDDAAEQHciqqsiqRLKIKTSSPELAIGR----LSGGNQQKAILARCLLLNPRILIL 429
Cdd:PLN03232 692 naTVRENILFGSDFESERYWRAIDVTALQH-------DLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 430 DEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELpEVLGLSDRVLVMHEGRLK-----ANLVNQHLTQEQVMEAALRS 504
Cdd:PLN03232 765 DDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMIKeegtfAELSKSGSLFKKLMENAGKM 843
|
....*.
gi 489011807 505 ERHVEE 510
Cdd:PLN03232 844 DATQEV 849
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
402-499 |
2.12e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.05 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 402 AIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQL-VQQGIAVIVISSELPEVLGLSDRVLVMHE 480
Cdd:PRK10253 140 SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALRE 219
|
90
....*....|....*....
gi 489011807 481 GRLKANLVNQHLTQEQVME 499
Cdd:PRK10253 220 GKIVAQGAPKEIVTAELIE 238
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
8-102 |
2.25e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 8 KNITKTFgavKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPhgSYEGEIifagetlqanhirdtERKG-IAII 86
Cdd:PRK13546 31 KHKNKTF---FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS--PTVGKV---------------DRNGeVSVI 90
|
90
....*....|....*.
gi 489011807 87 HQELALVKHLTVLENI 102
Cdd:PRK13546 91 AISAGLSGQLTGIENI 106
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-173 |
3.14e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 22 NVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIfagetlqanhirdteRKGIAIIHQeLALVKHLTVLEN 101
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI---------------RGSVAYVPQ-VSWIFNATVREN 698
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 102 IFLGA--EISRHGLLDYETMTLRCQKLLAQVNLpispdTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPTASL 173
Cdd:PLN03232 699 ILFGSdfESERYWRAIDVTALQHDLDLLPGRDL-----TEIGERGVnisgGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
385-476 |
3.58e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 385 IQQSIQRLKIKTS----------SPELAIGRLSGGNQQKAILARCL--LLNPRILILDEPTRGIDIGAKYEIYKLINQLV 452
Cdd:PRK00635 446 IEEVLQGLKSRLSilidlglpylTPERALATLSGGEQERTALAKHLgaELIGITYILDEPSIGLHPQDTHKLINVIKKLR 525
|
90 100
....*....|....*....|....
gi 489011807 453 QQGIAVIVISSElPEVLGLSDRVL 476
Cdd:PRK00635 526 DQGNTVLLVEHD-EQMISLADRII 548
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-88 |
3.94e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGETLQANHIRDTERKGI 83
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
....*
gi 489011807 84 AIIHQ 88
Cdd:PRK09580 81 FMAFQ 85
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-173 |
4.08e-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: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 20 VDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGiyPHGSYEGEIIFAGEtlqanhirdterkgIAIIHQElALVKHLTVL 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLA--EMDKVEGHVHMKGS--------------VAYVPQQ-AWIQNDSLR 716
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 100 ENIFLGAEISRhgllDYETMTLRCQKLLAQVN-LPISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPTASL 173
Cdd:TIGR00957 717 ENILFGKALNE----KYYQQVLEACALLPDLEiLPSGDRTEIGEKGVnlsgGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
126-476 |
5.12e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 126 LLAQVNLP-ISPDTRVGDLGLGQQQLVEIAKALNKQVR--LLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKl 202
Cdd:PRK00635 459 ILIDLGLPyLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 203 NEVKAISDTICVIRDGQHI--------GTRDASGMSEDDIITMMVGRELTALYPsEPHAHGEEILRVEHLTawhpvnrhI 274
Cdd:PRK00635 538 EQMISLADRIIDIGPGAGIfggevlfnGSPREFLAKSDSLTAKYLRQELTIPIP-EKRTNSLGTLTLSKAT--------K 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 275 KRVNDVSFSLRRGEILGIAGLVGAGRTE-----AVQCLFGV-------------------------WPGRWQGEI----- 319
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSSlindtLVPAVEEFieqgfcsnlsiqwgaisrlvhitrdLPGRSQRSIpltyi 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 320 --FID------GQP---------------VSISNCQQAIAHGIAMVPED------------RKKDGIVPVMAVGKNItlA 364
Cdd:PRK00635 689 kaFDDlrelfaEQPrskrlgltkshfsfnTPLGACAECQGLGSITTTDNrtsipcpsclgkRFLPQVLEVRYKGKNI--A 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 365 ALNQFTgAMSSLDDAAEQHCIQQSIQRLkIKTSSPELAIGR----LSGGNQQKAILARCLLL---NPRILILDEPTRGID 437
Cdd:PRK00635 767 DILEMT-AYEAEKFFLDEPSIHEKIHAL-CSLGLDYLPLGRplssLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLH 844
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 489011807 438 igaKYEIYKLIN---QLVQQGIAVIVISSELpEVLGLSDRVL 476
Cdd:PRK00635 845 ---THDIKALIYvlqSLTHQGHTVVIIEHNM-HVVKVADYVL 882
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-52 |
5.28e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 5.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489011807 4 LLEMKNITKTFGAVKAVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCG 52
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG 360
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-219 |
9.38e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.67 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 37 GENGSGKSTLMK----VLCGIYPHGSYEG----EIIFAGETLQANHIRDTERKGIAI-IHQELAlvkhltVLEN-IFLGA 106
Cdd:cd03240 29 GQNGAGKTTIIEalkyALTGELPPNSKGGahdpKLIREGEVRAQVKLAFENANGKKYtITRSLA------ILENvIFCHQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 107 EISRHGLLDyetMTLRC---QKLLAqvNLPIspdtRVGdlglgqqqlveIAKALNKQVRLLILDEPTASLTEQE-TATLL 182
Cdd:cd03240 103 GESNWPLLD---MRGRCsggEKVLA--SLII----RLA-----------LAETFGSNCGILALDEPTTNLDEENiEESLA 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 489011807 183 AIVRDLQNHDI-ACIYISHKLNEVKAISDTICVIRDGQ 219
Cdd:cd03240 163 EIIEERKSQKNfQLIVITHDEELVDAADHIYRVEKDGR 200
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
16-57 |
9.88e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 40.90 E-value: 9.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489011807 16 AVKAVDnvSLRLNAGeVVSLCGENGSGKSTLMK---VLCGIYPHG 57
Cdd:COG3910 26 AVRNLE--GLEFHPP-VTFFVGENGSGKSTLLEaiaVAAGFNPEG 67
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
406-482 |
1.53e-03 |
|
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: 39.76 E-value: 1.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIG-AKYEIYKLINQLVQQGIAVIVISSELpEVLGLSDRVLVMHEGR 482
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-173 |
1.79e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 22 NVSLRLNAGEVVSLCGENGSGKSTLMKVLCgiyphGSYEgeiIFAGETLQAnhirdterKGIAIIHQElALVKHLTVLEN 101
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLL-----SQFE---ISEGRVWAE--------RSIAYVPQQ-AWIMNATVRGN 740
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 102 IFLGAEISRHGLLDyetmTLRCQKLLAQV-NLPISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPTASL 173
Cdd:PTZ00243 741 ILFFDEEDAARLAD----AVRVSQLEADLaQLGGGLETEIGEKGVnlsgGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
403-478 |
1.80e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 1.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489011807 403 IGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVqQGIAVIVISSELPeVLG-LSDRVLVM 478
Cdd:PRK13409 210 ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLA-VLDyLADNVHIA 284
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-177 |
1.90e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 40.23 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 22 NVSLRLNAGEVVSLCGENGSGKSTLMKVLCG-IYPHgsyEGEIIFAGEtlqanhirdterkgIAIIHQeLALVKHLTVLE 100
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPS---EGKIKHSGR--------------ISFSSQ-FSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 101 NIFLGAEISRHgllDYETMTLRCQKLLAQVNLPISPDTRVGDLGL----GQQQLVEIAKALNKQVRLLILDEPTASL--- 173
Cdd:cd03291 117 NIIFGVSYDEY---RYKSVVKACQLEEDITKFPEKDNTVLGEGGItlsgGQRARISLARAVYKDADLYLLDSPFGYLdvf 193
|
....
gi 489011807 174 TEQE 177
Cdd:cd03291 194 TEKE 197
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-53 |
3.09e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.26 E-value: 3.09e-03
10 20 30
....*....|....*....|....*....|....*
gi 489011807 19 AVDNVSLRLNAGEVVSLCGENGSGKSTLMKVLCGI 53
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGV 73
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
398-512 |
3.39e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 398 SPEL---AIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAkyeIYKLINQLVQQGIAVIVIS-------SELPE 467
Cdd:PLN03073 334 TPEMqvkATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVShareflnTVVTD 410
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489011807 468 VLGLSDRVLVMHEG------RLKANLVNQhltQEQVMEAALRSERHVEEHV 512
Cdd:PLN03073 411 ILHLHGQKLVTYKGdydtfeRTREEQLKN---QQKAFESNERSRSHMQAFI 458
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
406-481 |
3.43e-03 |
|
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: 39.24 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIgakyeiyKLINQLVQQGI---------AVIVISSELpEVLGLSDRVL 476
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDI-------HLSDHLMQEGIlkflqddkrTLVLVTHKL-QYLPHADWII 212
|
....*
gi 489011807 477 VMHEG 481
Cdd:cd03290 213 AMKDG 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
406-483 |
3.97e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.40 E-value: 3.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQ-GIAVIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
406-483 |
4.20e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.83 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGnQQKAILARCLLLNP-RILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVIS--SELPEVLGLSDRVLVMHEGR 482
Cdd:PLN03140 337 ISGG-QKKRVTTGEMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSllQPAPETFDLFDDIILLSEGQ 415
|
.
gi 489011807 483 L 483
Cdd:PLN03140 416 I 416
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
406-483 |
4.66e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 39.24 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGID----IGAKYEIYKLINQLvqqGIAVIVISSELPEVLGLSDRVLVMHEG 481
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
..
gi 489011807 482 RL 483
Cdd:PRK11000 211 RV 212
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-212 |
5.97e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.72 E-value: 5.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489011807 146 GQQQLVEIAKAL----NKQVRLLILDEPTASLTEQETATLLAIVRDLQNHDIACIYISHKlNEVKAISDTI 212
Cdd:cd03227 81 GEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL-PELAELADKL 150
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
406-510 |
6.27e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.34 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIY-KLINQLVQQGIAVIVISSE--LPEVlglsDRVLVMHEGR 482
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDELRGKTRVLVTNQLhfLSQV----DRIILVHEGM 816
|
90 100 110
....*....|....*....|....*....|...
gi 489011807 483 LKA-----NLVNQHLTQEQVMEAALRSERHVEE 510
Cdd:PLN03130 817 IKEegtyeELSNNGPLFQKLMENAGKMEEYVEE 849
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
381-462 |
6.79e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.52 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 381 EQHCIQQSIQRLKIKTSSPELAIGRLSGGNQQ-KAILARCL--LLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIA 457
Cdd:pfam13304 212 VDDRLRERGLILLENGGGGELPAFELSDGTKRlLALLAALLsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQ 291
|
....*
gi 489011807 458 VIVIS 462
Cdd:pfam13304 292 LILTT 296
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
406-496 |
6.98e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 38.30 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489011807 406 LSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAkyeiYKLINQLVQQGIA--VIVISSELPEVLGLSDRVLVMHEGRL 483
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT----YQVIRKTLKQAFAdcTVILSEHRIEAMLECQRFLVIEENKV 214
|
90
....*....|...
gi 489011807 484 KANLVNQHLTQEQ 496
Cdd:cd03289 215 RQYDSIQKLLNEK 227
|
|
| |
