|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-501 |
0e+00 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 1104.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAG 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIFLGREFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFES 160
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLIEMMVGR 240
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 241 KLEDQYPHLDNAPGEIRLKVDNLCGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHS 320
Cdd:PRK10762 241 KLEDQYPRLDKAPGEVRLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 321 PQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALGYFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGN 400
Cdd:PRK10762 321 PQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTRE 480
Cdd:PRK10762 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTRE 480
|
490 500
....*....|....*....|.
gi 2070354550 481 QATQEVLMAAAVGKLNRVNQE 501
Cdd:PRK10762 481 QATQEKLMAAAVGKLNRVNQE 501
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-493 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 809.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAG 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIFLGREFVnRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFES 160
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPR-RGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLIEMMVGR 240
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 241 KLEDQYPHLDNAPGEIRLKVDNLCGPG-VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTH 319
Cdd:COG1129 240 ELEDLFPKRAAAPGEVVLEVEGLSVGGvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 320 SPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALGYFSRaGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGG 399
Cdd:COG1129 320 SPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSR-GGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTR 479
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDR 478
|
490
....*....|....
gi 2070354550 480 EQATQEVLMAAAVG 493
Cdd:COG1129 479 EEATEEAIMAAATG 492
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-494 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 634.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY---TRDaGSLLWLGKETTFNGPKSSQ 77
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgTYE-GEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 78 EAGIGIIHQELNLIPQLTIAENIFLGREFVnRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLS 157
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEIT-PGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLIEMM 237
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 238 VGRKLEDQYPHLDNAPGEIRLKVDNLC-----GPG---VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMP-RTSGY 308
Cdd:PRK13549 240 VGRELTALYPREPHTIGEVILEVRNLTawdpvNPHikrVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 309 VTLDGHEVVTHSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALGYFSRaGGSLKHKDEQQAVGDFIRLFNVKTPS 388
Cdd:PRK13549 320 IFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTG-GSRIDDAAELKTILESIQRLKVKTAS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 389 MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVM 468
Cdd:PRK13549 399 PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
|
490 500
....*....|....*....|....*.
gi 2070354550 469 HEGHLSGEFTREQATQEVLMAAAVGK 494
Cdd:PRK13549 479 HEGKLKGDLINHNLTQEQVMEAALRS 504
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-491 |
0e+00 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 593.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAG 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIFLGReFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFES 160
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQ-LPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAERE-VATLTEDSLIEMMVG 239
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDdMAQVDRDQLVQAMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 240 RKLEDQYPHLDNAPGEIRLKVDNLCGPGV-NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVT 318
Cdd:PRK11288 240 REIGDIYGYRPRPLGEVRLRLDGLKGPGLrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 319 HSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALGYFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGLLSG 398
Cdd:PRK11288 320 RSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFT 478
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELA 479
|
490
....*....|...
gi 2070354550 479 REQATQEVLMAAA 491
Cdd:PRK11288 480 REQATERQALSLA 492
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-490 |
0e+00 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 549.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY---TRDaGSLLWLGKETTFNGPKSSQEAG 80
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYphgSYE-GEILFDGEVCRFKDIRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIFLGREfVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFES 160
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIFLGNE-RAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIA--EREVATLTEDSLIEMMV 238
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIEtlDCRADEVTEDRIIRGMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 239 GRKLEDQYPHLDNAPGEIRLKVDNLC-----GPG---VNDVSFVLRKGEILGISGLMGAGRTEL-MKVL---YGAmpRTS 306
Cdd:NF040905 239 GRDLEDRYPERTPKIGEVVFEVKNWTvyhplHPErkvVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFgrsYGR--NIS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 307 GYVTLDGHEVVTHSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALGYFSRaGGSLKHKDEQQAVGDFIRLFNVKT 386
Cdd:NF040905 317 GTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSR-RGVIDENEEIKVAEEYRKKMNIKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 387 PSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRII 466
Cdd:NF040905 396 PSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIY 475
|
490 500
....*....|....*....|....
gi 2070354550 467 VMHEGHLSGEFTREQATQEVLMAA 490
Cdd:NF040905 476 VMNEGRITGELPREEASQERIMRL 499
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-489 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 538.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAG 80
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIFLGREfVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFES 160
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLE-PTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLIEMMVGR 240
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 241 KLEDQYPHLDNAPGEIRLKVDNLC------GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGH 314
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVLEVENLSvrddrgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 315 EVVTHSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALG--YFSRaGGSLKHKDEQQAVGDFIRLFNVKTPSMEQA 392
Cdd:COG3845 321 DITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRrpPFSR-GGFLDRKAIRAFAEELIEEFDVRTPGPDTP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 393 IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
490 500
....*....|....*....|
gi 2070354550 473 LSGEFTREQATQEVL---MA 489
Cdd:COG3845 480 IVGEVPAAEATREEIgllMA 499
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-492 |
2.71e-171 |
|
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: 492.42 E-value: 2.71e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDA--GSLLWLGKETTFNGPKSSQEAGI 81
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GIIHQELNLIPQLTIAENIFLGREFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKL-VGELSIGDQQMVEIAKVLSFES 160
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLIEMMVGR 240
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 241 KLEDQYPHLDNAPGEIRLKVDNLCG--------PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMP-RTSGYVTL 311
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCwdvinphrKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 312 DGHEVVTHSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALGYFSRAGgSLKHKDEQQAVGDFIRLFNVKTPSMEQ 391
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKM-RIDAAAELQIIGSAIQRLKVKTASPFL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 392 AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
490 500
....*....|....*....|.
gi 2070354550 472 HLSGEFTREQATQEVLMAAAV 492
Cdd:TIGR02633 480 KLKGDFVNHALTQEQVLAAAL 500
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-492 |
3.92e-169 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 486.98 E-value: 3.92e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAG 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIFLGREFVNRF---GKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLS 157
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLTKKVcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLIEMM 237
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 238 VGRKLEDQY----PHLDNAPGEIRLKVDNLCG---PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVT 310
Cdd:PRK09700 242 VGRELQNRFnamkENVSNLAHETVFEVRNVTSrdrKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 311 LDGHEVVTHSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLT---ALGYFSRAGGSLKHKDEQQAVGDFIRLFNVKTP 387
Cdd:PRK09700 322 LNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrslKDGGYKGAMGLFHEVDEQRTAENQRELLALKCH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 388 SMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIV 467
Cdd:PRK09700 402 SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAV 481
|
490 500
....*....|....*....|....*.
gi 2070354550 468 MHEGHLSGEFT-REQATQEVLMAAAV 492
Cdd:PRK09700 482 FCEGRLTQILTnRDDMSEEEIMAWAL 507
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-491 |
4.47e-166 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 478.45 E-value: 4.47e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAGIGIIHQ 86
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 87 ELNLIPQLTIAENIFLGReFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMD 166
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGR-YPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 167 EPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLIEMMVGRKLEDQY 246
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 247 PHLDNAPGEIRLKVDNLCG---PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQD 323
Cdd:PRK10982 240 PDKENKPGEVILEVRNLTSlrqPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 324 GLANGIVYISEDRKRDGLVLGMSVKENMSLTALGYFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQK 403
Cdd:PRK10982 320 AINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 404 VAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQAT 483
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTT 479
|
....*...
gi 2070354550 484 QEVLMAAA 491
Cdd:PRK10982 480 QNEILRLA 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-493 |
5.71e-143 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 420.23 E-value: 5.71e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAG 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIFLGREFVNRfgkiDWKKMyaeaDQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFES 160
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGLPKRQA----SMQKM----KQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLIEMMV-- 238
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITpa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 239 --------GRKLEDQYP--HLDNAPGEIRLKVDNLCGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGY 308
Cdd:PRK15439 240 arekslsaSQKLWLELPgnRRQQAAGAPVLTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 309 VTLDGHEVVTHSPQDGLANGIVYISEDRKRDGLVLGMSVKENM-SLTalgyFSRAGGSLKHKDEQQAVGDFIRLFNVKTP 387
Cdd:PRK15439 320 IMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVcALT----HNRRGFWIKPARENAVLERYRRALNIKFN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 388 SMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIV 467
Cdd:PRK15439 396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLV 475
|
490 500
....*....|....*....|....*.
gi 2070354550 468 MHEGHLSGEFTREQATQEVLMAAAVG 493
Cdd:PRK15439 476 MHQGEISGALTGAAINVDTIMRLAFG 501
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
254-473 |
2.22e-87 |
|
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: 265.83 E-value: 2.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 254 GEIRLKVDNLCGPG-VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVYI 332
Cdd:cd03215 1 GEPVLEVRGLSVKGaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 SEDRKRDGLVLGMSVKENMSLTALgyfsraggslkhkdeqqavgdfirlfnvktpsmeqaiglLSGGNQQKVAIARGLMT 412
Cdd:cd03215 81 PEDRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-222 |
3.36e-76 |
|
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: 236.56 E-value: 3.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAGIGII 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQelnlipqltiaeniflgrefvnrfgkidwkkmyaeadqllaklnlrfksdklvgeLSIGDQQMVEIAKVLSFESKVII 164
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 165 MDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-473 |
1.51e-72 |
|
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: 238.65 E-value: 1.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY---TRDAGSLLWLGKETTfngPKS 75
Cdd:COG1123 1 MTPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGRDLL---ELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 76 SQEAG--IGIIHQE--LNLIPqLTIAENIflgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVE 151
Cdd:COG1123 78 EALRGrrIGMVFQDpmTQLNP-VTVGDQI----AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 152 IAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVAT-LT 229
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEiLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 230 EDSLIEMMVGRKLEDQYPHLDNAPGEIRLKVDNLC------GPG----VNDVSFVLRKGEILGISGLMGAGRTELMKVLY 299
Cdd:COG1123 233 APQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSkrypvrGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 300 GAMPRTSGYVTLDGHEVVTHSPQDglangivyISEDRKRDGLVL---------GMSVKENMS--LTALGYFSRAggslkh 368
Cdd:COG1123 313 GLLRPTSGSILFDGKDLTKLSRRS--------LRELRRRVQMVFqdpysslnpRMTVGDIIAepLRLHGLLSRA------ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 369 kDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLS 447
Cdd:COG1123 379 -ERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLT 457
|
490 500
....*....|....*....|....*.
gi 2070354550 448 IILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:COG1123 458 YLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-222 |
1.27e-53 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 180.33 E-value: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfnGPKSSQEAGIGII 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT--GLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 --HQELNLIPQLTIAENIFLGREFVNRFGKIDW------KKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVL 156
Cdd:cd03219 79 rtFQIPRLFPELTVLENVMVAAQARTGSGLLLArarreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-222 |
2.83e-50 |
|
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: 172.53 E-value: 2.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfnGPKSSQ--E 78
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT--GLPPHRiaR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 79 AGIGIIHQELNLIPQLTIAENIFLGREF---------VNRFGKI--DWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQ 147
Cdd:COG0411 79 LGIARTFQNPRLFPELTVLENVLVAAHArlgrgllaaLLRLPRArrEEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 148 QMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELK-SQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-233 |
2.58e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.39 E-value: 2.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEagIGII 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIflgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:COG1131 79 PQEPALYPDLTVRENL----RFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 165 MDEPTDALtDTETESLFR-VIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSL 233
Cdd:COG1131 155 LDEPTSGL-DPEARRELWeLLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
268-487 |
2.11e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.99 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdgLANGIVYISEDrkrDGLVLGMSV 347
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE--VRRRIGYVPQE---PALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENmsltaLGYFSRAGGsLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:COG1131 91 REN-----LRFFARLYG-LPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 428 VGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEVL 487
Cdd:COG1131 164 PEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-230 |
9.74e-43 |
|
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: 151.93 E-value: 9.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEagIGI 83
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ--IGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IHQELNLIPQLTIAENIflgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVI 163
Cdd:COG4555 79 LPDERGLYDRLTVRENI----RYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 164 IMDEPTDALtDTETESLFR-VIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTE 230
Cdd:COG4555 155 LLDEPTNGL-DVMARRLLReILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
266-485 |
1.72e-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: 151.16 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVTHSPQDGLANgIVYISEDRkrdGLVLGM 345
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG-EDVRKEPREARRQ-IGVLPDER---GLYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENmsltaLGYFSRAGGsLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
Cdd:COG4555 90 TVREN-----IRYFAELYG-LFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 426 VDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQE 485
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-224 |
2.19e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.19 E-value: 2.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfnGPKSS 76
Cdd:COG1136 1 MSPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS--SLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 77 QEAG-----IGIIHQELNLIPQLTIAENIflgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVE 151
Cdd:COG1136 79 ELARlrrrhIGFVFQFFNLLPELTALENV----ALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 152 IAKVLSFESKVIIMDEPTDALtDTET-ESLFRVIREL-KSQGRGIVYISHRMkEIFEICDDVTVFRDGQFIAERE 224
Cdd:COG1136 155 IARALVNRPKLILADEPTGNL-DSKTgEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVSDER 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
266-494 |
1.32e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 149.78 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGV---NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVYISEDRkrdGLV 342
Cdd:COG1129 15 GGVkalDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQEL---NLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LGMSVKENMsltALGYFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
Cdd:COG1129 92 PNLSVAENI---FLGREPRRGGLIDWRAMRRRARELLARLGLDIDP-DTPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 423 TRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEVLMAAAVGK 494
Cdd:COG1129 168 TASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGR 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
258-472 |
4.36e-39 |
|
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: 141.42 E-value: 4.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLCG-----PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVYI 332
Cdd:cd03224 1 LEVENLNAgygksQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 SEDRkrdGLVLGMSVKENMsltalgyfsRAGGSLKHKDEQQAVGDFI-RLFNVKTPSMEQAIGLLSGGNQQKVAIARGLM 411
Cdd:cd03224 81 PEGR---RIFPELTVEENL---------LLGAYARRRAKRKARLERVyELFPRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
258-473 |
7.37e-39 |
|
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: 139.07 E-value: 7.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC-----GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdgLANGIVYI 332
Cdd:cd03230 1 IEVRNLSkrygkKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE--VKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 SEDrkrDGLVLGMSVKENMSLtalgyfsraggslkhkdeqqavgdfirlfnvktpsmeqaigllSGGNQQKVAIARGLMT 412
Cdd:cd03230 79 PEE---PSLYENLTVRENLKL-------------------------------------------SGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-241 |
2.74e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 146.32 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 2 DALLQLKGIDKAfpgvKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAGI 81
Cdd:COG1129 254 EVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GII---HQELNLIPQLTIAENIFLGR-EFVNRFGKIDWKKMYAEADQLLAKLNLRFKS-DKLVGELSIGDQQMVEIAKVL 156
Cdd:COG1129 330 AYVpedRKGEGLVLDLSIRENITLASlDRLSRGGLLDRRRERALAEEYIKRLRIKTPSpEQPVGNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 157 SFESKVIIMDEPT---DALTDTEtesLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSL 233
Cdd:COG1129 410 ATDPKVLILDEPTrgiDVGAKAE---IYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEEAI 486
|
....*...
gi 2070354550 234 IEMMVGRK 241
Cdd:COG1129 487 MAAATGGA 494
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-219 |
7.28e-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: 136.37 E-value: 7.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEagIGII 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR--IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIflgrefvnrfgkidwkkmyaeadqllaklnlrfksdklvgELSIGDQQMVEIAKVLSFESKVII 164
Cdd:cd03230 79 PEEPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 165 MDEPTDALtDTETESLFR-VIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQF 219
Cdd:cd03230 119 LDEPTSGL-DPESRREFWeLLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
258-481 |
8.33e-38 |
|
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: 138.58 E-value: 8.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLCG-----PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVYI 332
Cdd:COG0410 4 LEVENLHAgyggiHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 SEDRkrdGLVLGMSVKENMsltALGYFSRAGGSLKHKDEQQAVGDFIRLfnvkTPSMEQAIGLLSGGNQQKVAIARGLMT 412
Cdd:COG0410 84 PEGR---RIFPSLTVEENL---LLGAYARRDRAEVRADLERVYELFPRL----KERRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 413 RPKVLILDEPTRG-----VDvgakkEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:COG0410 154 RPKLLLLDEPSLGlapliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-218 |
5.60e-37 |
|
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: 135.70 E-value: 5.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfnGPKSSQEAG 80
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS--KLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 -----IGIIHQELNLIPQLTIAENIflgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKV 155
Cdd:cd03255 79 frrrhIGFVFQSFNLLPDLTALENV----ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 156 LSFESKVIIMDEPTDALtDTET-ESLFRVIREL-KSQGRGIVYISHRMkEIFEICDDVTVFRDGQ 218
Cdd:cd03255 155 LANDPKIILADEPTGNL-DSETgKEVMELLRELnKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-221 |
1.35e-36 |
|
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: 134.33 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGpkssqEAGIGII 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAEN-IFLGREFvnrfgkiDWKKMYA--EADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESK 161
Cdd:cd03269 76 PEERGLYPKMKVIDQlVYLAQLK-------GLKKEEArrRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIA 221
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-169 |
1.61e-36 |
|
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: 132.00 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQeAGIGIIHQELNLIPQLTIAEN 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLR-KEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 100 IFLGREFVNRFGKIDWkkmyAEADQLLAKLNLRFKSDKLVG----ELSIGDQQMVEIAKVLSFESKVIIMDEPT 169
Cdd:pfam00005 80 LRLGLLLKGLSKREKD----ARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
268-471 |
5.48e-36 |
|
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: 133.33 E-value: 5.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVyisedRK--RDGLVLGM 345
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIG-----RTfqIPRLFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLTAL----GYFSRAGGSLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
Cdd:cd03219 91 TVLENVMVAAQartgSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2070354550 422 PTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-233 |
5.89e-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: 133.46 E-value: 5.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKS--SQEAGI 81
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GIIHQELNLIPQLTIAENIFLGR--------EFVNRFGKIDwkkmYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIA 153
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEE----KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDS 232
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
.
gi 2070354550 233 L 233
Cdd:cd03256 237 L 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-231 |
5.91e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 136.96 E-value: 5.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 2 DALLQLKGIDKAFP-----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSS 76
Cdd:COG1123 258 EPLLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 77 QEAG--IGIIHQ--ELNLIPQLTIAENIflgREFVNRFGKIDWKKMYAEADQLLAK--LNLRFKsDKLVGELSIGDQQMV 150
Cdd:COG1123 338 RELRrrVQMVFQdpYSSLNPRMTVGDII---AEPLRLHGLLSRAERRERVAELLERvgLPPDLA-DRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLT 229
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
..
gi 2070354550 230 ED 231
Cdd:COG1123 494 AN 495
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
268-471 |
6.06e-35 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 130.18 E-value: 6.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVtHSPQDGLAN-GIVYISedrkrDGLVLGMS 346
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEARRRlGFVSDS-----TGLYDRLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 347 VKENmsltaLGYFSRAGGsLKHKDEQQAVGDFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
Cdd:cd03266 95 AREN-----LEYFAGLYG-LKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2070354550 427 DVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:cd03266 168 DVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
266-494 |
8.19e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 136.31 E-value: 8.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGV---NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVYISEDRKrdgLV 342
Cdd:COG3845 16 GGVvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQHFM---LV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LGMSVKENMsltALGYFSRAGGSLKHKDEQQAVGDFIRLFNVKTPsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
Cdd:COG3845 93 PNLTVAENI---VLGLEPTKGGRLDRKAARARIRELSERYGLDVD-PDAKVEDLSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 423 TRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEVLMAAAVGK 494
Cdd:COG3845 169 TAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGR 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-491 |
1.08e-34 |
|
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: 136.35 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKS----TMMKVLTGIYTRDAGSLLWLGKETTFNG 72
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 73 PKSSQE---AGIGIIHQE----LNliPQLTI----AENIFLGRefvnrfgKIDWKKMYAEADQLLAKLNLRFKSDKLVG- 140
Cdd:COG4172 83 ERELRRirgNRIAMIFQEpmtsLN--PLHTIgkqiAEVLRLHR-------GLSGAAARARALELLERVGIPDPERRLDAy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 141 --ELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDG 217
Cdd:COG4172 154 phQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 218 QFIAEREVATL--------TedsliemmvgRKLEDQYPHLDNAP----GEIRLKVDNLC------------GPG----VN 269
Cdd:COG4172 234 EIVEQGPTAELfaapqhpyT----------RKLLAAEPRGDPRPvppdAPPLLEARDLKvwfpikrglfrrTVGhvkaVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPrTSGYVTLDGHEVVTHSPQDGLANgivyisedRKRDGLVL------ 343
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRPL--------RRRMQVVFqdpfgs 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 -------GMSVKENMSLTALGyfsraggsLKHKDEQQAVGDfirlfnvktpsMEQAIGL-----------LSGGNQQKVA 405
Cdd:COG4172 375 lsprmtvGQIIAEGLRVHGPG--------LSAAERRARVAE-----------ALEEVGLdpaarhrypheFSGGQRQRIA 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL--SGE----FT 478
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVveQGPteqvFD 515
|
570
....*....|....*
gi 2070354550 479 REQA--TQEvLMAAA 491
Cdd:COG4172 516 APQHpyTRA-LLAAA 529
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
268-475 |
4.59e-34 |
|
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: 127.65 E-value: 4.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEvvthspqdglangivyISEDRKRDGLV----- 342
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP----------------LEKERKRIGYVpqrrs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 ----LGMSVKENMSLTALGYfSRAGGSLKHKDEQ---QAVgDFIRLFNVKtpsmEQAIGLLSGGNQQKVAIARGLMTRPK 415
Cdd:cd03235 79 idrdFPISVRDVVLMGLYGH-KGLFRRLSKADKAkvdEAL-ERVGLSELA----DRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 416 VLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVM-HEGHLSG 475
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLnRTVVASG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-229 |
5.59e-34 |
|
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: 127.62 E-value: 5.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEagIG 82
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS--LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQELNLIPQLTIAENIflgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKV 162
Cdd:cd03263 79 YCPQFDALFDELTVREHL----RFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 163 IIMDEPTDALTDTETESLFRVIRELKsQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLT 229
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-231 |
3.14e-33 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 125.62 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngPKSSQE---AGI 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT---GLPPHErarAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GIIHQELNLIPQLTIAENIFLGrEFVNRFGKIDW--KKMYAEADQLLAKLNlrfksdKLVGELSIGDQQMVEIAKVLSFE 159
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLG-AYARRRAKRKArlERVYELFPRLKERRK------QLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTED 231
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-222 |
4.65e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 127.15 E-value: 4.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFngpksSQEAGIGII 84
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-----EDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENI-FLGRefvnRFGkIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVI 163
Cdd:COG4152 77 PEERGLYPKMKVGEQLvYLAR----LKG-LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
268-476 |
6.40e-33 |
|
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: 122.92 E-value: 6.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVYISEdrkrdglvlgmsv 347
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 kenmsltalgyfsraggslkhkdeqqavgdfirlfnvktpsmeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2070354550 428 VGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGE 476
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-222 |
7.88e-33 |
|
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: 124.40 E-value: 7.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGkettFNGPKSSQEA 79
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG----FDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 80 --GIGIIHQELNLIPQLTIAENIflgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLS 157
Cdd:cd03266 77 rrRLGFVSDSTGLYDRLTARENL----EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-218 |
1.22e-32 |
|
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: 123.73 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEaGIGIIHQ--ELNLIpQLT 95
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR-KVGLVFQnpDDQFF-GPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 96 IAENIFLGREfvNRfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
Cdd:cd03225 93 VEEEVAFGLE--NL--GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2070354550 176 ETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:cd03225 169 GRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-225 |
1.84e-32 |
|
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: 123.60 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngPKSSQEAG--I 81
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELRrkV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GIIHQElnliP--QL---TIAENIFLGREfvnRFGkIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVL 156
Cdd:COG1122 78 GLVFQN----PddQLfapTVEEDVAFGPE---NLG-LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE---REV 225
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADgtpREV 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
3.19e-32 |
|
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: 123.07 E-value: 3.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEA 79
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 80 --GIGIIHQELNLIPQLTIAENIFLGREfvnrFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLS 157
Cdd:cd03258 81 rrRIGMIFQHFNLLSSRTVFENVALPLE----IAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 158 FESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREV 225
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
258-490 |
3.96e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.28 E-value: 3.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC-----GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdglangIVYI 332
Cdd:COG1121 7 IELENLTvsyggRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 --SEDRKRDglvLGMSVKEnmsLTALGYFSRAG--GSLKHKDEQQA------VG--DFIRlfnvktpsmeQAIGLLSGGN 400
Cdd:COG1121 81 pqRAEVDWD---FPITVRD---VVLMGRYGRRGlfRRPSRADREAVdealerVGleDLAD----------RPIGELSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTRE 480
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEE 224
|
250
....*....|
gi 2070354550 481 QATQEVLMAA 490
Cdd:COG1121 225 VLTPENLSRA 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
4.04e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.28 E-value: 4.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKettfngPKSSQEAG 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK------PPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGiihqelnLIPQLTIAENIF--LGREFV--NRFGKIDW-----KKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVE 151
Cdd:COG1121 77 IG-------YVPQRAEVDWDFpiTVRDVVlmGRYGRRGLfrrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 152 IAKVLSFESKVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTE 230
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGV-DAATEeALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTP 228
|
...
gi 2070354550 231 DSL 233
Cdd:COG1121 229 ENL 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
254-471 |
5.33e-32 |
|
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: 123.23 E-value: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 254 GEIRLKVDNLC---GpG---VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLAN 327
Cdd:COG0411 1 SDPLLEVRGLTkrfG-GlvaVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 328 GIVY---ISEdrkrdgLVLGMSVKENMsltALGYFSRAGGSLKH---------KDEQQAVG------DFIRLfnvkTPSM 389
Cdd:COG0411 80 GIARtfqNPR------LFPELTVLENV---LVAAHARLGRGLLAallrlprarREEREAREraeellERVGL----ADRA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 390 EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVM 468
Cdd:COG0411 147 DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVL 226
|
...
gi 2070354550 469 HEG 471
Cdd:COG0411 227 DFG 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-452 |
1.35e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 127.49 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 7 LKGIDKAFPGVKALSGAALNVYPG-RVmALVGENGAGKSTMMKVLTGIYTRDAGSLlWLGKETTfngpkssqeagIGIIH 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGdRI-GLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGLR-----------IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 86 QELNLIPQLTIAENIFLG----REFVNRFGKI---------DWKKM---------------YAEADQLLAKLNL-RFKSD 136
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGdaelRALEAELEELeaklaepdeDLERLaelqeefealggweaEARAEEILSGLGFpEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 137 KLVGELSiGDQQM-VEIAKVLSFESKVIIMDEPTDALtDTET----ESLfrvireLKSQGRGIVYISH-RM------KEI 204
Cdd:COG0488 148 RPVSELS-GGWRRrVALARALLSEPDLLLLDEPTNHL-DLESiewlEEF------LKNYPGTVLVVSHdRYfldrvaTRI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 205 FEIcDD--VTVFRDG--QFIAERE----------------VATLTE---------------DSLIEMMvgRKLEDQYPHL 249
Cdd:COG0488 220 LEL-DRgkLTLYPGNysAYLEQRAerleqeaaayakqqkkIAKEEEfirrfrakarkakqaQSRIKAL--EKLEREEPPR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 250 DNAPGEIR-----------LKVDNLC-GPG----VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLdG 313
Cdd:COG0488 297 RDKTVEIRfppperlgkkvLELEGLSkSYGdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 314 HEVVthspqdglangIVYISEDrkRDGLVLGMSVKENMSLTALGyfsraggslkhKDEQQA---VGDFirLFnvkTPSM- 389
Cdd:COG0488 376 ETVK-----------IGYFDQH--QEELDPDKTVLDELRDGAPG-----------GTEQEVrgyLGRF--LF---SGDDa 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 390 EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkaDGlSIILVS 452
Cdd:COG0488 427 FKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVS 486
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
268-471 |
4.37e-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: 119.31 E-value: 4.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvthspQDGLANGIVYISEDRkrdGLVLGMSV 347
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-----DIAARNRIGYLPEER---GLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENmsltaLGYFSRAGGsLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:cd03269 88 IDQ-----LVYLAQLKG-LKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2070354550 428 VGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:cd03269 161 PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-225 |
4.69e-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: 4.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKettfngPKSSQEAG 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE------PVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIFLGREFVNrfgkIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFES 160
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQG----VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 161 KVIIMDEP---TDALTDTE-TESLFRVIRElksQGRGIVYISHRMKEIFEICDDVTVF--RDGQFIAEREV 225
Cdd:cd03293 151 DVLLLDEPfsaLDALTREQlQEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEV 218
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
5.77e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 120.22 E-value: 5.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGiYTR-DAGSLLWLGKETTfnGPKSSQ-- 77
Cdd:COG4674 7 HGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITG-KTRpDSGSVLFGGTDLT--GLDEHEia 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 78 EAGIGIIHQELNLIPQLTIAENIFLG--------REFVNRFGKIDWKKMyaeaDQLLAKLNLRFKSDKLVGELSIGDQQM 149
Cdd:COG4674 84 RLGIGRKFQKPTVFEELTVFENLELAlkgdrgvfASLFARLTAEERDRI----EEVLETIGLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 150 VEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELkSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSL-AGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAE 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-211 |
6.02e-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: 119.18 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKettfngPKSSQEAGIGiihqelnLIP 92
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK------PLEKERKRIG-------YVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 93 QLTIAENIF--LGREFV--NRFGKIDW-----KKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVI 163
Cdd:cd03235 75 QRRSIDRDFpiSVRDVVlmGLYGHKGLfrrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2070354550 164 IMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISHRMKEIFEICDDV 211
Cdd:cd03235 155 LLDEPFAGV-DPKTQeDIYELLRELRREGMTILVVTHDLGLVLEYFDRV 202
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
258-485 |
1.13e-30 |
|
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: 118.78 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC-----GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVYI 332
Cdd:TIGR03410 1 LEVSNLNvyygqSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 SEDRKRDGLvlgMSVKENMSLtalGYFSRAGGSLKHKDEQQAvgdfirLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMT 412
Cdd:TIGR03410 81 PQGREIFPR---LTVEENLLT---GLAALPRRSRKIPDEIYE------LFPVLKEMLGRRGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQE 485
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDED 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-249 |
1.66e-30 |
|
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: 118.99 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKE-TTFNGPKSSQEagIG 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlASLSRRELARR--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQELNLIPQLTIAENIFLGRE-FVNRFGKIDwKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESK 161
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGRYpHLGLFGRPS-AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 162 VIIMDEPTDALtD----TEtesLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE---REVatLTEDSL 233
Cdd:COG1120 158 LLLLDEPTSHL-DlahqLE---VLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQgppEEV--LTPELL 231
|
250 260
....*....|....*....|.
gi 2070354550 234 -----IEMMVGRKLEDQYPHL 249
Cdd:COG1120 232 eevygVEARVIEDPVTGRPLV 252
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
268-473 |
1.78e-30 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 117.99 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdgLANGIVYISEDrkrDGLVLGMSV 347
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLGYCPQF---DALFDELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENmsltaLGYFSRAGGsLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:cd03263 93 REH-----LRFYARLKG-LPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2070354550 428 VGAKKEIYQLINQFKAdGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03263 166 PASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-218 |
2.27e-30 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 117.62 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPkssQEAGIGII 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP---ERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIFLGRefvnRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGL----KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 165 MDEPTDALtDTET-ESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:cd03259 154 LDEPLSAL-DAKLrEELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-222 |
3.45e-30 |
|
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: 116.93 E-value: 3.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQeagIGII 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR---IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTiaeniflGREFVNRFGKIDWKKmYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:cd03268 78 IEAPGFYPNLT-------ARENLRLLARLLGIR-KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 165 MDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-259 |
3.87e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.50 E-value: 3.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGkeTTFNGPKSS-----QE 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDerlirQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 79 AGIgiIHQELNLIPQLTIAENIFLGREFVNRFGKIDWKKMyaeADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSF 158
Cdd:PRK09493 79 AGM--VFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQ---ARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMkeifeicddvtvfrdgQFiaEREVATltedSLIEMMV 238
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEI----------------GF--AEKVAS----RLIFIDK 211
|
250 260
....*....|....*....|...
gi 2070354550 239 GRKLEDQYPH--LDNAPGEiRLK 259
Cdd:PRK09493 212 GRIAEDGDPQvlIKNPPSQ-RLQ 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-243 |
4.13e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.83 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 2 DALLQLKGID-KAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAG 80
Cdd:COG3845 255 EVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELN---LIPQLTIAENIFLGREFVNRFGK---IDWKKMYAEADQLLAKLNLRFKS-DKLVGELSIGDQQMVEIA 153
Cdd:COG3845 335 VAYIPEDRLgrgLVPDMSVAENLILGRYRRPPFSRggfLDRKAIRAFAEELIEEFDVRTPGpDTPARSLSGGNQQKVILA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 154 KVLSFESKVIIMDEPT---DALTdteTESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTE 230
Cdd:COG3845 415 RELSRDPKLLIAAQPTrglDVGA---IEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATR 491
|
250
....*....|...
gi 2070354550 231 DSLIEMMVGRKLE 243
Cdd:COG3845 492 EEIGLLMAGVKEE 504
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
256-472 |
6.62e-30 |
|
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: 116.03 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 256 IRLKVDNLCGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLAN-GIVY--- 331
Cdd:cd03225 5 LSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLVFqnp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 332 ---ISEDRKRDGLVLGMsvkENMSLtalgyfsraggslKHKDEQQAVGDFIRLFNVKTPsMEQAIGLLSGGNQQKVAIAR 408
Cdd:cd03225 85 ddqFFGPTVEEEVAFGL---ENLGL-------------PEEEIEERVEEALELVGLEGL-RDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-218 |
1.76e-29 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 113.82 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKE-TTFNGPKSSQEAGIGI 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDlTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IHQELNLIPQLTIAENIFLGrefvnrfgkidwkkmyaeadqllaklnlrfksdklvgeLSIGDQQMVEIAKVLSFESKVI 163
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 164 IMDEPTDALtDTET-ESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:cd03229 123 LLDEPTSAL-DPITrREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
258-473 |
2.49e-29 |
|
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: 115.12 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC------GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGlangivy 331
Cdd:COG1122 1 IELENLSfsypggTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 332 isedRKRDGLVL--------GMSVKENM--SLTALGyfsraggsLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQ 401
Cdd:COG1122 74 ----RRKVGLVFqnpddqlfAPTVEEDVafGPENLG--------LPREEIRERVEEALELVGL-EHLADRPPHELSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-231 |
4.17e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 114.69 E-value: 4.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 2 DALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfnGPKSSQ--EA 79
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLPPHRiaRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 80 GIGIIHQELNLIPQLTIAENIFLGREFVNRFGKIDW--KKMYAeadqllakL--NLRFKSDKLVGELSIGDQQMVEIAKV 155
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRAdlERVYE--------LfpRLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 156 LSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTED 231
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-218 |
4.32e-29 |
|
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: 114.53 E-value: 4.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEA 79
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 80 G--IGIIHQE----LNliPQLTIAENIflgREFVNRFGKIDWKKMYAEA-DQLLAKLNL--RFKsDKLVGELSIGDQQMV 150
Cdd:cd03257 81 RkeIQMVFQDpmssLN--PRMTIGEQI---AEPLRIHGKLSKKEARKEAvLLLLVGVGLpeEVL-NRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 151 EIAKVLSFESKVIIMDEPTDAL-TDTETESLfRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALdVSVQAQIL-DLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
258-473 |
5.39e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.37 E-value: 5.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC-----GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivYi 332
Cdd:COG4619 1 LELEGLSfrvggKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE-------W- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 sedRKRDGLV------LGMSVKENMSLTAlgyfsraggSLKH-KDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVA 405
Cdd:COG4619 73 ---RRQVAYVpqepalWGGTVRDNLPFPF---------QLRErKFDRERALELLERLGLPPDILDKPVERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-199 |
6.74e-29 |
|
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: 113.34 E-value: 6.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEagIG 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQELNLIPQLTIAENIflgrEFVNRFGKIDWKKmyAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKV 162
Cdd:COG4133 79 YLGHADGLKPELTVRENL----RFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 2070354550 163 IIMDEPTDALtDTETESLF-RVIRELKSQGRGIVYISH 199
Cdd:COG4133 153 WLLDEPFTAL-DAAGVALLaELIAAHLARGGAVLLTTH 189
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
269-481 |
7.36e-29 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 113.75 E-value: 7.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLangivyisEDRKRDGLVL----- 343
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELY--------RLRRRMGMLFqsgal 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 --GMSVKENMsltalGYFSRAGGSLKHKDEQQAVGDFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
Cdd:cd03261 89 fdSLTVFENV-----AFPLREHTRLSEEEIREIVLEKLEAVGLR-GAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 422 PTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-222 |
7.44e-29 |
|
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: 113.06 E-value: 7.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGrVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEagIGII 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR--IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAEniFLgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:cd03264 78 PQEFGVYPNFTVRE--FL--DYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 165 MDEPTDALTDTETESLFRVIRELkSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-218 |
8.82e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 111.18 E-value: 8.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSsQEAGIGIIH 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 86 QelnlipqltiaeniflgrefvnrfgkidwkkmyaeadqllaklnlrfksdklvgeLSIGDQQMVEIAKVLSFESKVIIM 165
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 166 DEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-222 |
2.66e-28 |
|
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: 112.08 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsllwlgkETTFNGPKSSQEAG---- 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG-------RATVAGHDVVREPRevrr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 -IGIIHQELNLIPQLTIAENIFLgrefvnrFGKI---DWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVL 156
Cdd:cd03265 74 rIGIVFQDLSVDDELTGWENLYI-------HARLygvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 157 SFESKVIIMDEPTDALTDTETESLFRVIRELK-SQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
258-472 |
3.76e-28 |
|
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: 110.35 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLCG-----PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGlangivyi 332
Cdd:cd03229 1 LELKNVSKrygqkTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 sEDRKRDGLVL-------GMSVKENMSLtalgyfsraggslkhkdeqqavgdfirlfnvktpsmeqaigLLSGGNQQKVA 405
Cdd:cd03229 73 -PLRRRIGMVFqdfalfpHLTVLENIAL-----------------------------------------GLSGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-DGLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
268-473 |
8.15e-28 |
|
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: 110.66 E-value: 8.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivyISEDRKRD-------- 339
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE--------LAAFRRRHigfvfqsf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 340 GLVLGMSVKENMSLTALgyfsrAGGSLKHKDEQQAVgDFIRLFNVKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
Cdd:cd03255 92 NLLPDLTALENVELPLL-----LAGVPKKERRERAE-ELLERVGLGD-RLNHYPSELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 420 DEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEmPEVLGMSDRIIVMHEGHL 473
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
257-487 |
8.94e-28 |
|
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: 111.29 E-value: 8.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 257 RLKVDNLC-GPG----VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLANGIVY 331
Cdd:COG1120 1 MLEAENLSvGYGgrpvLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 332 ISEDRKRDGlvlGMSVKEnmsLTALGYFSRAG--GSLKHKDEQqAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARG 409
Cdd:COG1120 80 VPQEPPAPF---GLTVRE---LVALGRYPHLGlfGRPSAEDRE-AVEEALERTGL-EHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL--SGEfTREQATQEV 486
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIvaQGP-PEEVLTPEL 230
|
.
gi 2070354550 487 L 487
Cdd:COG1120 231 L 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
257-452 |
9.05e-28 |
|
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: 109.88 E-value: 9.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 257 RLKVDNL-CGPG----VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvtHSPQDGLANGIVY 331
Cdd:COG4133 2 MLEAENLsCRRGerllFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI--RDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 332 ISEdrkRDGLVLGMSVKENmsltaLGYFSRAGGSLKHKDEQQAVGDFIRLfnvkTPSMEQAIGLLSGGNQQKVAIARGLM 411
Cdd:COG4133 80 LGH---ADGLKPELTVREN-----LRFWAALYGLRADREAIDEALEAVGL----AGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2070354550 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVS 452
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTT 188
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-218 |
1.36e-27 |
|
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: 109.93 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQE-AGIGI 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IHQELNLIPQLTIAENIFLGREFVNrfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVI 163
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVK---GMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 164 IMDEPTDALtDTET--ESLfRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:cd03262 158 LFDEPTSAL-DPELvgEVL-DVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
265-472 |
1.51e-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: 107.72 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 265 GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLANGIVYISEdrkrdglvlg 344
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 msvkenmsltalgyfsraggslkhkdeqqavgdfirlfnvktpsmeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2070354550 425 GVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
256-473 |
1.62e-27 |
|
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: 109.90 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 256 IRLKVDNLCGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANG--IVYIS 333
Cdd:cd03257 9 VSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRkeIQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 334 EDrkrDGLVL--GMSVKEnmSLTALgyFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLM 411
Cdd:cd03257 89 QD---PMSSLnpRMTIGE--QIAEP--LRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
258-497 |
2.31e-27 |
|
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: 115.00 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC-------GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMP---RTSGYVTLDGHEVVTHSPQDgLAN 327
Cdd:COG1123 5 LEVRDLSvrypggdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEAL-RGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 328 GIVYISEDRKR--DGLVLGMSVKENMSLTALgyfSRAGGSLKHKDEQQAVGDFIRLfnvktpsmEQAIGLLSGGNQQKVA 405
Cdd:COG1123 84 RIGMVFQDPMTqlNPVTVGDQIAEALENLGL---SRAEARARVLELLEAVGLERRL--------DRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQ 484
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
250
....*....|...
gi 2070354550 485 EVLMAAAVGKLNR 497
Cdd:COG1123 233 APQALAAVPRLGA 245
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
258-493 |
2.83e-27 |
|
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: 109.89 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC---GPG------VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLANG 328
Cdd:COG1124 2 LEVRNLSvsyGQGgrrvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-TRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 329 IVYISED-------RKRdglvLGMSVKEnmSLTALGyfsraggslkHKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQ 401
Cdd:COG1124 81 VQMVFQDpyaslhpRHT----VDRILAE--PLRIHG----------LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTRE 480
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
250 260
....*....|....*....|.
gi 2070354550 481 Q--------ATQEvLMAAAVG 493
Cdd:COG1124 225 DllagpkhpYTRE-LLAASLA 244
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
268-481 |
5.57e-27 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 108.23 E-value: 5.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSpqDGLANGIVYISEDRKRDGlvlGMSV 347
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIVFQDLSVDD---ELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMSLTALGYfSRAGGSLKHKDEQqaVGDFIRLFNVKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:cd03265 91 WENLYIHARLY-GVPGAERRERIDE--LLDFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 428 VGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
258-473 |
1.46e-26 |
|
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: 106.83 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC-----GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVTHSPQdglangivyi 332
Cdd:cd03259 1 LELKGLSktygsVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG-RDVTGVPP---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 sedRKRD-GLVLG-------MSVKENmsltaLGYFSRAGGsLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKV 404
Cdd:cd03259 70 ---ERRNiGMVFQdyalfphLTVAEN-----IAFGLKLRG-VPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQ-FKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
258-481 |
2.71e-26 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 106.86 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLCG-----PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLAN-GIVY 331
Cdd:cd03218 1 LRAENLSKrygkrKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMHKRARlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 332 ISED----RKrdglvlgMSVKENMSLtALGYFSRAGGSLKHKDEQqavgdFIRLFNVKTPSMEQAIGLlSGGNQQKVAIA 407
Cdd:cd03218 80 LPQEasifRK-------LTVEENILA-VLEIRGLSKKEREEKLEE-----LLEEFHITHLRKSKASSL-SGGERRRVEIA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-218 |
3.74e-26 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 106.65 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngPKSSQEAGIGII 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT---DVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIFLGREFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 165 MDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
269-481 |
5.19e-26 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 106.22 E-value: 5.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivyISEDRKRDGLVL----- 343
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE--------LYELRRRIGMLFqggal 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 --GMSVKENmsltaLGYFSRAGGSLKHKDEQQAVGDFIRLFNvktpsMEQAIGL----LSGGNQQKVAIARGLMTRPKVL 417
Cdd:COG1127 94 fdSLTVFEN-----VAFPLREHTDLSEAEIRELVLEKLELVG-----LPGAADKmpseLSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 418 ILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEE 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
268-473 |
5.90e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 104.05 E-value: 5.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLANGIVYisedrkrdglvlgmsV 347
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE-LARKIAY---------------V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMSLTALGYFSRaggslkhkdeqqavgdfiRLFNVktpsmeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:cd03214 79 PQALELLGLAHLAD------------------RPFNE-----------LSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2070354550 428 VGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03214 130 IAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
231-490 |
7.98e-26 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 111.46 E-value: 7.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 231 DSLIEMMVGRKLEDQYPHLDNAPGEIRLkvDNLC-------GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMP 303
Cdd:COG2274 449 DDILDLPPEREEGRSKLSLPRLKGDIEL--ENVSfrypgdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 304 RTSGYVTLDGHEVVTHSPQDgLANGIVYISEdrkrDGLVLGMSVKENMSLTALGYfsraggslkhkDEQQAV-------- 375
Cdd:COG2274 527 PTSGRILIDGIDLRQIDPAS-LRRQIGVVLQ----DVFLFSGTIRENITLGDPDA-----------TDEEIIeaarlagl 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 376 GDFIRL----FNvkTPSMEQAIGlLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAdGLSIILV 451
Cdd:COG2274 591 HDFIEAlpmgYD--TVVGEGGSN-LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIII 666
|
250 260 270
....*....|....*....|....*....|....*....
gi 2070354550 452 SSEmPEVLGMSDRIIVMHEGHLsgeftREQATQEVLMAA 490
Cdd:COG2274 667 AHR-LSTIRLADRIIVLDKGRI-----VEDGTHEELLAR 699
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-222 |
9.38e-26 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 105.28 E-value: 9.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAG--IG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQELNLIPQLTIAENI-FLGREFVNRFgkidwKKMYAE-ADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFES 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVaFPLREHTRLS-----EEEIREiVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 161 KVIIMDEPT---DALTDTETESLfrvIRELK-SQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:cd03261 156 ELLLYDEPTaglDPIASGVIDDL---IRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-218 |
9.47e-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: 103.23 E-value: 9.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAgIG 82
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQElnliPQL---TIAENIflgrefvnrfgkidwkkmyaeadqllaklnlrfksdklvgeLSIGDQQMVEIAKVLSFE 159
Cdd:cd03228 80 YVPQD----PFLfsgTIRENI-----------------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 160 SKVIIMDEPTDALtDTETESL-FRVIRELkSQGRGIVYISHRMKEIfEICDDVTVFRDGQ 218
Cdd:cd03228 115 PPILILDEATSAL-DPETEALiLEALRAL-AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
268-423 |
1.16e-25 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 102.34 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLANGIVYISEDrkrDGLVLGMSV 347
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL-TDDERKSLRKEIGYVFQD---PQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 348 KENMSLTALGYFSRAGGSlkhKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
Cdd:pfam00005 77 RENLRLGLLLKGLSKREK---DARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-222 |
1.40e-25 |
|
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: 105.06 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQE-- 78
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 79 AGIGIIHQELNLIPQLTIAENI-FLGREFvnrfGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLS 157
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVaFPLREH----TDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 158 FESKVIIMDEPT---DALTdteTESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:COG1127 158 LDPEILLYDEPTaglDPIT---SAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-221 |
1.59e-25 |
|
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: 103.91 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSL-----LWLGKETTFNGPksSQEAGIGIIHQELNLIPQLTIAENIFLG 103
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtVLFDSRKKINLP--PQQRKIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 104 REFVNRfgkidwKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRV 183
Cdd:cd03297 100 LKRKRN------REDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2070354550 184 IRELKSQGRGIV-YISHRMKEIFEICDDVTVFRDGQFIA 221
Cdd:cd03297 174 LKQIKKNLNIPViFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
268-477 |
1.72e-25 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 103.84 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVyisedrKRDGLVLGMSV 347
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI------EAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMSLTALGYfsraggSLKHKDEQQAvgdfIRLFNVKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:cd03268 90 RENLRLLARLL------GIRKKRIDEV----LDVVGLKD-SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2070354550 428 VGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEF 477
Cdd:cd03268 159 PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
268-475 |
2.72e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.58 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvthSPQDglANGIVYISEDRkrdGLVLGMSV 347
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPED--RRRIGYLPEER---GLYPKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KEnmsltALGYFSRAGGsLKHKDEQQAVGDFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:COG4152 89 GE-----QLVYLARLKG-LSKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2070354550 428 VGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGH--LSG 475
Cdd:COG4152 162 PVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRkvLSG 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-276 |
2.93e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.72 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPkssQEAG 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP---EKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIflgrefvnRFG-KIdwKKMYAE-----ADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAK 154
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENV--------AFGlRM--RGVPKAeirarVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 155 VLSFESKVIIMDEPTDALtDTET-----ESLFRVIRELksqgrGI--VYISHRMKEIFEICDDVTVFRDGQFI------- 220
Cdd:COG3842 149 ALAPEPRVLLLDEPLSAL-DAKLreemrEELRRLQREL-----GItfIYVTHDQEEALALADRIAVMNDGRIEqvgtpee 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 221 -----AEREVAT-LTEDSLIEmmvGRKLEDQYPHLDNAPGEIRLKVDNLCGPGvNDVSFVLR 276
Cdd:COG3842 223 iyerpATRFVADfIGEANLLP---GTVLGDEGGGVRTGGRTLEVPADAGLAAG-GPVTVAIR 280
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-218 |
3.91e-25 |
|
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: 103.92 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGV-KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPkSSQEAGIGI 83
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-VELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IHQELNLIPQLTIAENIFLgrefVNRFGKIDWKKMYAEADQLLAKLNLRFKS--DKLVGELSIGDQQMVEIAKVLSFESK 161
Cdd:cd03295 80 VIQQIGLFPHMTVEENIAL----VPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 162 VIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGE 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-228 |
5.73e-25 |
|
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: 102.64 E-value: 5.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY-----TRDAGSLLWLGKE-TTFNGPKSSQE 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 79 AGIGIIHQELNLIPqLTIAENIFLGrefVNRFGKIDWKKMYAEADQLLAKLNL--RFKSDKLVGELSIGDQQMVEIAKVL 156
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYG---LRLHGIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATL 228
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-228 |
9.42e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.91 E-value: 9.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwLGkETTFNGPKS-SQEAG- 80
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIR-VG-DITIDTARSlSQQKGl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 -------IGIIHQELNLIPQLTIAENIFLGREFVNrfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIA 153
Cdd:PRK11264 80 irqlrqhVGFVFQNFNLFPHRTVLENIIEGPVIVK---GEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATL 228
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
268-471 |
1.19e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 104.42 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTE----LMKVLyGAMPRTSGYVTLDGHEVVThSPQDGL----ANGIVYISEDrkrd 339
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQtafaLMGLL-AANGRIGGSATFNGREILN-LPEKELnklrAEQISMIFQD---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 340 glvlgmsvkenmSLTALGYFSRAGGSL-------KHKDEQQAVGDFIRLFN-VKTPSMEQAIGL----LSGGNQQKVAIA 407
Cdd:PRK09473 106 ------------PMTSLNPYMRVGEQLmevlmlhKGMSKAEAFEESVRMLDaVKMPEARKRMKMypheFSGGMRQRVMIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK09473 174 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
252-490 |
1.63e-24 |
|
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: 106.77 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 252 APGEIRLKVDNLC------GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGL 325
Cdd:COG4988 331 AAGPPSIELEDVSfsypggRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL-SDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 326 ANGIVYISEDrkrdGLVLGMSVKENMSLtalgyfSRAGGSlkhkDEQ-----QAVG--DFIRLFN--VKTPSMEQAIGLl 396
Cdd:COG4988 410 RRQIAWVPQN----PYLFAGTIRENLRL------GRPDAS----DEEleaalEAAGldEFVAALPdgLDTPLGEGGRGL- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADglSIILVSSEMPEVLGMSDRIIVMHEGHLsge 476
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRI--- 549
|
250
....*....|....
gi 2070354550 477 ftREQATQEVLMAA 490
Cdd:COG4988 550 --VEQGTHEELLAK 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
266-472 |
1.64e-24 |
|
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: 99.76 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLANGIVYISEDrkrdGLVLGM 345
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES-LRKNIAYVPQD----PFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENmsltalgyfsraggslkhkdeqqavgdfirlfnvktpsmeqaigLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
Cdd:cd03228 91 TIREN--------------------------------------------ILSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2070354550 426 VDVGAKKEIYQLINQFkADGLSIILVSSEMpEVLGMSDRIIVMHEGH 472
Cdd:cd03228 127 LDPETEALILEALRAL-AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-234 |
2.06e-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: 101.47 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAGIGII 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIFLGREFvnrFGKIDWKKMyAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEI---RGLSKKERE-EKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 165 MDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLI 234
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-222 |
2.80e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.96 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEag 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIflgREFVNRFGkIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFES 160
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENL---LVFGRYFG-LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-217 |
3.48e-24 |
|
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: 100.77 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPkssQEAGIGII 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP---HKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIFLGRefvnRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGL----RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 165 MDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDG 217
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
266-473 |
3.57e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.51 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangIVYIsedRKRDGLVL-- 343
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE-----IPYL---RRRIGVVFqd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 -----GMSVKEN--MSLTALGYfsraggslKHKDEQQAVGDFIRLFnvktpsmeqaiGL----------LSGGNQQKVAI 406
Cdd:COG2884 88 frllpDRTVYENvaLPLRVTGK--------SRKEIRRRVREVLDLV-----------GLsdkakalpheLSGGEQQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 407 ARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-191 |
6.06e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 99.74 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETtfNGPKSSQEAG--- 80
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL--SRLKRREIPYlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 -IGIIHQELNLIPQLTIAENIflgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFE 159
Cdd:COG2884 80 rIGVVFQDFRLLPDRTVYENV----ALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190
....*....|....*....|....*....|...
gi 2070354550 160 SKVIIMDEPTDALtDTET-ESLFRVIRELKSQG 191
Cdd:COG2884 156 PELLLADEPTGNL-DPETsWEIMELLEEINRRG 187
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-213 |
6.75e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 102.05 E-value: 6.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY---TRDAGSLLWLGKETTFNGPKSS 76
Cdd:COG0444 1 LLEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 77 QE---AGIGIIHQE----LNliPQLTIAENIflgREFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLV---GELSIGD 146
Cdd:COG0444 81 RKirgREIQMIFQDpmtsLN--PVMTVGDQI---AEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDrypHELSGGM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 147 QQMVEIAKVLSFESKVIIMDEPTDALtDTETE-SLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTV 213
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTAL-DVTIQaQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAV 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-222 |
7.81e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.22 E-value: 7.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfnGPKSSQEAGIGII 84
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIFL-GREFvnrfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVI 163
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVfGRYF-----GMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-473 |
1.17e-23 |
|
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: 104.11 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI--YTRDAGSLLW---LGKETTFNGPKS---- 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvaLCEKCGYVERPSkvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 76 ----------SQEAG---------------IGIIHQE-LNLIPQLTIAENIFlgrEFVNRFGKIDWKKMYAEADqLLAKL 129
Cdd:TIGR03269 81 pcpvcggtlePEEVDfwnlsdklrrrirkrIAIMLQRtFALYGDDTVLDNVL---EALEEIGYEGKEAVGRAVD-LIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 130 NLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIREL-KSQGRGIVYISHRMKEIFEI 207
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTL-DPQTAKLVhNALEEAvKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 208 CDDVTVFRDGQFIA------------------EREVATLTEDSLIEMmvgRKLEDQYPHLDNapGEIRlkvdnlcgpGVN 269
Cdd:TIGR03269 236 SDKAIWLENGEIKEegtpdevvavfmegvsevEKECEVEVGEPIIKV---RNVSKRYISVDR--GVVK---------AVD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYV-TLDGHEVV--THSPQDGLANGIVYISEDRKRDGLVLGMS 346
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVdmTKPGPDGRGRAKRYIGILHQEYDLYPHRT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 347 VKENMSlTALGY-------FSRAGGSLKHK--DEQQAVGDFIRLfnvktPSMeqaiglLSGGNQQKVAIARGLMTRPKVL 417
Cdd:TIGR03269 382 VLDNLT-EAIGLelpdelaRMKAVITLKMVgfDEEKAEEILDKY-----PDE------LSEGERHRVALAQVLIKEPRIV 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 418 ILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
266-471 |
1.65e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 97.29 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPqDGLANGIVYISEDrkrDGLVLGm 345
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP-NELGDHVGYLPQD---DELFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENmsltalgyfsraggslkhkdeqqavgdfirlfnvktpsmeqaigLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
Cdd:cd03246 91 SIAEN--------------------------------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2070354550 426 VDVGAKKEIYQLINQFKADGLSIILVSSEmPEVLGMSDRIIVMHEG 471
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDG 171
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
268-473 |
1.93e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 98.80 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVYISEDRKrdgLVLGMSV 347
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMSLTalGYFSraggslKHKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:PRK11614 98 EENLAMG--GFFA------ERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2070354550 428 VGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
258-471 |
1.94e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLCGP-----GVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVYI 332
Cdd:PRK11300 6 LSVSGLMMRfggllAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 SEDRKrdgLVLGMSVKENMsLTALGYFSRAG---GSLK----HKDEQQAVG------DFIRLfnvkTPSMEQAIGLLSGG 399
Cdd:PRK11300 86 FQHVR---LFREMTVIENL-LVAQHQQLKTGlfsGLLKtpafRRAESEALDraatwlERVGL----LEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-471 |
2.57e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.86 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 21 SGAALNVYPGRVMALVGENGAGKS----TMMKVLTG---IYT----RDAGSLLWLGKETTFNGPKSSQeagIGIIHQE-- 87
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYPsgdiRFHGESLLHASEQTLRGVRGNK---IAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 88 LNLIPQLTIAENIFlgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVG---ELSIGDQQMVEIAKVLSFESKVII 164
Cdd:PRK15134 103 VSLNPLHTLEKQLY---EVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 165 MDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTedSLIEMMVGRKLE 243
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF--SAPTHPYTQKLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 244 DQYPHLD----NAPGEIRLKVDNL--CGPG--------------VNDVSFVLRKGEILGISGLMGAGRTE----LMKVLy 299
Cdd:PRK15134 258 NSEPSGDpvplPEPASPLLDVEQLqvAFPIrkgilkrtvdhnvvVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 300 gampRTSGYVTLDGH-----------------EVVTHSPQDGL---ANGIVYISEdrkrdglvlGMSVKENmSLTAlgyf 359
Cdd:PRK15134 337 ----NSQGEIWFDGQplhnlnrrqllpvrhriQVVFQDPNSSLnprLNVLQIIEE---------GLRVHQP-TLSA---- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 360 sraggslkHKDEQQAVGdfirlfnvktpSMEQaIGL-----------LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
Cdd:PRK15134 399 --------AQREQQVIA-----------VMEE-VGLdpetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2070354550 429 GAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK15134 459 TVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-206 |
3.21e-23 |
|
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: 97.48 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETtfNGPKSSQEA----GIGIIHQELNL 90
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV--SDLRGRAIPylrrKIGVVFQDFRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 91 IPQLTIAENIFLGREFVNRFGKiDWKKMYAEAdqlLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTD 170
Cdd:cd03292 90 LPDRNVYENVAFALEVTGVPPR-EIRKRVPAA---LELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 2070354550 171 ALTDTETESLFRVIRELKSQGRGIVYISHRmKEIFE 206
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATHA-KELVD 200
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
255-471 |
4.08e-23 |
|
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: 97.28 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 255 EIRLKVDNLCGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLANGIVYISE 334
Cdd:cd03245 7 NVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 335 DrkrDGLVLGmSVKENMSLtalgyfsragGSLKHKDEQ-------QAVGDFIRlfnvKTP-SMEQAIG----LLSGGNQQ 402
Cdd:cd03245 86 D---VTLFYG-TLRDNITL----------GAPLADDERilraaelAGVTDFVN----KHPnGLDLQIGergrGLSGGQRQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADglSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-222 |
4.84e-23 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 102.99 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwlgkettFNG-------PKS--SQeagIGIIHQ 86
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL-------IDGidlrqidPASlrRQ---IGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 87 ELNLIPQlTIAENIFLGREfvnrfgKIDWKKMY-----AEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAKVLS 157
Cdd:COG2274 557 DVFLFSG-TIRENITLGDP------DATDEEIIeaarlAGLHDFIEALPMGY--DTVVGEggsnLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 158 FESKVIIMDEPTDALtDTETESLF-RVIRELKsQGRGIVYISHRMkEIFEICDDVTVFRDGQFIAE 222
Cdd:COG2274 628 RNPRILILDEATSAL-DAETEAIIlENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRIVED 690
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-221 |
5.28e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.14 E-value: 5.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfnGPKSSQEAGIGI 83
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GLPGHQIARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IH--QELNLIPQLTIAENIFLGRE-------FVNRFGKIDWKKMYAE----ADQLLAKLNLRFKSDKLVGELSIGDQQMV 150
Cdd:PRK11300 83 VRtfQHVRLFREMTVIENLLVAQHqqlktglFSGLLKTPAFRRAESEaldrAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQFIA 221
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
252-490 |
6.21e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 102.15 E-value: 6.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 252 APGEIRLKVDNLC-------GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDG 324
Cdd:COG4987 328 APGGPSLELEDVSfrypgagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL-RDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 325 LANGIVYISEDrkrdGLVLGMSVKENMSLTalgyfsRAGGSlkhkDEQ-----QAVG--DFIRlfnvktpSMEQaiGL-- 395
Cdd:COG4987 407 LRRRIAVVPQR----PHLFDTTLRENLRLA------RPDAT----DEElwaalERVGlgDWLA-------ALPD--GLdt 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 396 --------LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkADGLSIILVSSEmPEVLGMSDRIIV 467
Cdd:COG4987 464 wlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHR-LAGLERMDRILV 541
|
250 260
....*....|....*....|...
gi 2070354550 468 MHEGHLsgeftREQATQEVLMAA 490
Cdd:COG4987 542 LEDGRI-----VEQGTHEELLAQ 559
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-221 |
8.64e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 97.27 E-value: 8.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAGIG 82
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQELNLIPQLTIAENIFLGREFVNRFGKidwKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKV 162
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDDLSA---EQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIA 221
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
268-476 |
8.82e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 96.65 E-value: 8.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLAN------GIVY-----ISEdr 336
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI-SSLSERELARlrrrhiGFVFqffnlLPE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 337 krdglvlgMSVKENMSLTALgyfsrAGGSLKHKDEQQA--------VGDFIRLFnvktPSMeqaiglLSGGNQQKVAIAR 408
Cdd:COG1136 101 --------LTALENVALPLL-----LAGVSRKERRERArellervgLGDRLDHR----PSQ------LSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEmPEVLGMSDRIIVMHEGHLSGE 476
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
258-489 |
1.00e-22 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 97.05 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC------GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivy 331
Cdd:COG3638 3 LELRNLSkrypggTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRA-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 332 ISEDRKRDG-------LVLGMSVKENMSLTALGYFS--RAGGSLKHKDEQQA-------VG--DFirlfnvktpsMEQAI 393
Cdd:COG3638 75 LRRLRRRIGmifqqfnLVPRLSVLTNVLAGRLGRTStwRSLLGLFPPEDRERalealerVGlaDK----------AYQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGR 224
|
250
....*....|....*..
gi 2070354550 473 LSGEFTREQATQEVLMA 489
Cdd:COG3638 225 VVFDGPPAELTDAVLRE 241
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
258-468 |
1.31e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 98.20 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC-----GPG----VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMP---RTSGYVTLDGHEVVTHSPQDGL 325
Cdd:COG0444 2 LEVRNLKvyfptRRGvvkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 326 A---NGIVYISED-------RKRdglvLGMSVKENMsltalgyfsRAGGSLKHKDEQQAVgdfIRLFN-VKTPSMEQAIG 394
Cdd:COG0444 82 KirgREIQMIFQDpmtslnpVMT----VGDQIAEPL---------RIHGGLSKAEARERA---IELLErVGLPDPERRLD 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 395 L----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVM 468
Cdd:COG0444 146 RypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
258-487 |
1.39e-22 |
|
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: 96.48 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNL------CGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivy 331
Cdd:cd03256 1 IEVENLsktypnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 332 ISEDRKRDG-------LVLGMSVKENMSLTALGYFS--RAGGSLKHKDEQQAVGDFIRLFNVKTpSMEQAIGLLSGGNQQ 402
Cdd:cd03256 73 LRQLRRQIGmifqqfnLIERLSVLENVLSGRLGRRStwRSLFGLFPKEEKQRALAALERVGLLD-KAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231
|
....*.
gi 2070354550 482 ATQEVL 487
Cdd:cd03256 232 LTDEVL 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
268-473 |
1.59e-22 |
|
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: 96.10 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKV---LYGAMP--RTSGYVTLDGHEVVthspqdglaNGIVYISEDRKRDGLV 342
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLlnrLNDLIPgaPDEGEVLLDGKDIY---------DLDVDVLELRRRVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LG------MSVKENMSLTAlgyfsRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPK 415
Cdd:cd03260 87 FQkpnpfpGSIYDNVAYGL-----RLHGIKLKEELDERVEEALRKAALWDEVKDRLHALgLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 416 VLILDEPTRGVDVGAKKEIYQLINQFKADgLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-220 |
1.64e-22 |
|
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: 100.65 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSL-LWLGKE---TTFNGPKSSQEAG--IGIIHQELNL 90
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwvdMTKPGPDGRGRAKryIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 91 IPQLTIAENIF--LGREFVNRFGKIdwKKMYA---------EADQLLaklnlrfksDKLVGELSIGDQQMVEIAKVLSFE 159
Cdd:TIGR03269 377 YPHRTVLDNLTeaIGLELPDELARM--KAVITlkmvgfdeeKAEEIL---------DKYPDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 160 SKVIIMDEPT---DALTDTE-TESLFRVIRELksqGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:TIGR03269 446 PRIVILDEPTgtmDPITKVDvTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-221 |
1.70e-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: 95.73 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwlgkettFNGPKSSQ----- 77
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL-------LDGTDIRQldpad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 78 -EAGIGIIHQELNLIPQlTIAENIFLGREFVNrfgkiDWKKM----YAEADQLLAKLNLRFksDKLVGE----LSIGDQQ 148
Cdd:cd03245 76 lRRNIGYVPQDVTLFYG-TLRDNITLGAPLAD-----DERILraaeLAGVTDFVNKHPNGL--DLQIGErgrgLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 149 MVEIAKVLSFESKVIIMDEPTDALtDTETEslFRVIRELKS--QGRGIVYISHRMKeIFEICDDVTVFRDGQFIA 221
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAM-DMNSE--ERLKERLRQllGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVA 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-230 |
1.85e-22 |
|
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: 100.60 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfNGPKSSQEAGIGI 83
Cdd:COG4988 337 IELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-DLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IHQElNLIPQLTIAENIFLGREfvnrfgKIDWKKMY-----AEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAK 154
Cdd:COG4988 416 VPQN-PYLFAGTIRENLRLGRP------DASDEELEaaleaAGLDEFVAALPDGL--DTPLGEggrgLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 155 VLSFESKVIIMDEPTDALtDTETES-LFRVIRELkSQGRGIVYISHRMKEIfEICDDVTVFRDGQFIAEREVATLTE 230
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHL-DAETEAeILQALRRL-AKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLA 560
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-199 |
1.99e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTF---NGPKSSQE--A 79
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFsktPSDKAIRElrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 80 GIGIIHQELNLIPQLTIAENIFlgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFE 159
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLI---EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2070354550 160 SKVIIMDEPTDALtDTE-TESLFRVIRELksQGRGI--VYISH 199
Cdd:PRK11124 160 PQVLLFDEPTAAL-DPEiTAQIVSIIREL--AETGItqVIVTH 199
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
270-490 |
2.31e-22 |
|
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: 95.63 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLAN-GIVYisedrkRDGLVLGMSVK 348
Cdd:cd03252 20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQvGVVL------QENVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 349 ENMSLTalgyfsRAGGSLKHKDEQQAVG---DFIRLFNVKTPSM--EQAIGLlSGGNQQKVAIARGLMTRPKVLILDEPT 423
Cdd:cd03252 94 DNIALA------DPGMSMERVIEAAKLAgahDFISELPEGYDTIvgEQGAGL-SGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 424 RGVDVGAKKEIYQLINQFkADGLSIILVSSEMPEVLGmSDRIIVMHEGHLSgeftrEQATQEVLMAA 490
Cdd:cd03252 167 SALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIV-----EQGSHDELLAE 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
266-473 |
3.58e-22 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 95.10 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLAnGIVYisedrKRDGLVLGM 345
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNV-GFVF-----QHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMsltALGYFSRAGGSLKHKDEQQA-VGDFIRL-----FNVKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLIL 419
Cdd:cd03296 90 TVFDNV---AFGLRVKPRSERPPEAEIRAkVHELLKLvqldwLADRYPAQ------LSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 420 DEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
267-473 |
3.77e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.44 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 267 GVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvthSPQDGLANgivyISEDRKRDGLVLGMS 346
Cdd:PRK13641 22 GLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI---TPETGNKN----LKKLRKKVSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 347 ---VKENMSLTALGYFSRAGGSLKHKDEQQAVgDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
Cdd:PRK13641 95 eaqLFENTVLKDVEFGPKNFGFSEDEAKEKAL-KWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2070354550 424 RGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-220 |
4.21e-22 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 94.25 E-value: 4.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETtfnGPKSSQEAgIGIIHQELNLipQL 94
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKS-IGYVMQDVDY--QL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 95 ---TIAENIflgrefvnRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDA 171
Cdd:cd03226 85 ftdSVREEL--------LLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2070354550 172 LTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
268-478 |
4.74e-22 |
|
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: 94.46 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdglangIVYISEDrkrDGLVLGMSV 347
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------RGYVFQQ---DALLPWLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENmslTALGYfsRAGGsLKHKDEQQAVGDFIRLFNV-----KTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
Cdd:cd03293 91 LDN---VALGL--ELQG-VPKAEARERAEELLELVGLsgfenAYPHQ------LSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 423 TRGVDVGAKKEIYQLI-NQFKADGLSIILVSSEMPEVLGMSDRIIVM--HEGHLSGEFT 478
Cdd:cd03293 159 FSALDALTREQLQEELlDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
268-471 |
6.00e-22 |
|
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: 94.45 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPqdglangivyiseDR----KRDGLVL 343
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-------------DRmvvfQNYSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 GMSVKENMSLTAlgyfSRAGGSLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
Cdd:TIGR01184 68 WLTVRENIALAV----DRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2070354550 424 RGVDVGAKKEIY-QLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:TIGR01184 143 GALDALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
268-473 |
6.08e-22 |
|
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: 93.80 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGeILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHspQDGLANGIVYISEDRkrdGLVLGMSV 347
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ--PQKLRRRIGYLPQEF---GVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KEnmsltALGYFSRAGGsLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:cd03264 90 RE-----FLDYIAWLKG-IPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2070354550 428 VGAKKEIYQLINQFKADglSIILVSSEMPE-VLGMSDRIIVMHEGHL 473
Cdd:cd03264 163 PEERIRFRNLLSELGED--RIVILSTHIVEdVESLCNQVAVLNKGKL 207
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-223 |
6.54e-22 |
|
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: 94.22 E-value: 6.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLG---KETTFNgpksSQEAGIGIIHQELNLI 91
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLD----SLRRAIGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 92 PQlTIAENIflgrefvnRFGKIDWKK--MY--AEADQLLAK-LNLRFKSDKLVGE----LSIGDQQMVEIAKVLSFESKV 162
Cdd:cd03253 88 ND-TIGYNI--------RYGRPDATDeeVIeaAKAAQIHDKiMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 163 IIMDEPTDALtDTETE-SLFRVIRELkSQGRGIVYISHRMKEIFEiCDDVTVFRDGQfIAER 223
Cdd:cd03253 159 LLLDEATSAL-DTHTErEIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGR-IVER 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-473 |
6.86e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.16 E-value: 6.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSL----LWLGK--------- 66
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkMLLRRrsrqviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 67 ETTFNGPKSSQEAGIGIIHQE--LNLIPQLTIAENIFLGREFVNRFGKidwKKMYAEADQLLAKLNLRfKSDKLVG---- 140
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASR---EEAMVEAKRMLDQVRIP-EAQTILSryph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 141 ELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQF 219
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 220 IAEREV-------------ATLTEDSLIEMMVGRKLEDQYP--HLDNA-------------PGEIRLKVDNLCGP----- 266
Cdd:PRK10261 248 VETGSVeqifhapqhpytrALLAAVPQLGAMKGLDYPRRFPliSLEHPakqeppieqdtvvDGEPILQVRNLVTRfplrs 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 267 -----------GVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQ--DGLANGIVYIS 333
Cdd:PRK10261 328 gllnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIF 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 334 EDRKRD---GLVLGMSVKENMsltalgyfsRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGL 410
Cdd:PRK10261 408 QDPYASldpRQTVGDSIMEPL---------RVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARAL 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
265-473 |
6.99e-22 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 94.23 E-value: 6.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 265 GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLANGIVYISEdrkrdGLVLG 344
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQNY-----ALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 MSVKENMsltALGYFSRaggSLKHKDEQQAVGDFIRLfnVKTPSMEQ-AIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
Cdd:cd03300 87 LTVFENI---AFGLRLK---KLPKAEIKERVAEALDL--VQLEGYANrKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 424 RGVDVGAKKEI-YQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03300 159 GALDLKLRKDMqLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-219 |
7.33e-22 |
|
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: 93.47 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKssqEAGIGII 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIFLGREfVNRFGKIDWKKMYAEADQLLAKLNLRfksDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLK-LRKVPKDEIDERVREVAELLQIEHLL---DRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 165 MDEP---TDALTDTETES-LFRVIRELksqGRGIVYISHRMKEIFEICDDVTVFRDGQF 219
Cdd:cd03301 154 MDEPlsnLDAKLRVQMRAeLKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
269-473 |
9.62e-22 |
|
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: 93.36 E-value: 9.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVTHSPQDglangivyISEDRKRDGLVL----- 343
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDG-LKLTDDKKN--------INELRQKVGMVFqqfnl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 --GMSVKENMSLtalgyfsrAGGSLKHKDEQQAVGDFIRLFN-VKTPSMEQA-IGLLSGGNQQKVAIARGLMTRPKVLIL 419
Cdd:cd03262 88 fpHLTVLENITL--------APIKVKGMSKAEAEERALELLEkVGLADKADAyPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 420 DEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
268-471 |
1.31e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.73 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSpqdglangiVYISEDRKRDGLV----- 342
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKK---------VKLSDIRKKVGLVfqype 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 ------------------LGMS-------VKENMSLTALGYfsraggsLKHKDeqqavgdfirlfnvKTPsMEqaiglLS 397
Cdd:PRK13637 94 yqlfeetiekdiafgpinLGLSeeeienrVKRAMNIVGLDY-------EDYKD--------------KSP-FE-----LS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 398 GGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-222 |
1.98e-21 |
|
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: 91.34 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLlwlgketTFNGpkssqeagigiih 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-------LLDG------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 86 QELNLIPQLTIAENI-FLGrefvnrfgkidwkkmyaeadQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:cd03214 61 KDLASLSPKELARKIaYVP--------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 165 MDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-242 |
3.71e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.67 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY-----TRDAGSLLWLGKETtFNGPKSSQ 77
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDI-FKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 78 EAGIGIIHQELNLIPQLTIAENIFLGREfVNRFGKiDWKKMYAEADQLLAKLNL----RFKSDKLVGELSIGDQQMVEIA 153
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLK-LNRLVK-SKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYISHRMKEIFEICDDVTVFRDGQFIAE---REVATLTE 230
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWgptREVFTNPR 237
|
250
....*....|..
gi 2070354550 231 DSLIEMMVGRKL 242
Cdd:PRK14247 238 HELTEKYVTGRL 249
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-221 |
4.01e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.13 E-value: 4.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAgIGIIHQEL-NLIPQLTIA 97
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK-IGIIFQNPdNQFIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 98 ENIFLGREfvNRfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTET 177
Cdd:PRK13632 103 DDIAFGLE--NK--KVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2070354550 178 ESLFRVIRELKSQG-RGIVYISHRMKEIFeICDDVTVFRDGQFIA 221
Cdd:PRK13632 179 REIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIA 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
266-473 |
4.03e-21 |
|
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: 92.01 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGheVVTHSPQDGLangivyisedRKRDGLVLG- 344
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKF----------LRRIGVVFGq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 -------MSVKENMSLTALGY---FSRAGGSLKHKDEQQAVGDFirlfnVKTPSMEqaiglLSGGNQQKVAIARGLMTRP 414
Cdd:cd03267 103 ktqlwwdLPVIDSFYLLAAIYdlpPARFKKRLDELSELLDLEEL-----LDTPVRQ-----LSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-221 |
4.42e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.72 E-value: 4.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVL-------TGIY--------TRDAGSL 61
Cdd:PRK10535 1 MTALLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYrvagqdvaTLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 62 LWLGKETtfngpkssqeagIGIIHQELNLIPQLTIAENIflgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGE 141
Cdd:PRK10535 81 AQLRREH------------FGFIFQRYHLLSHLTAAQNV----EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 142 LSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH------RMKEIFEIcddvtvfR 215
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHdpqvaaQAERVIEI-------R 217
|
....*.
gi 2070354550 216 DGQFIA 221
Cdd:PRK10535 218 DGEIVR 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
270-473 |
4.99e-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: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLrKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGheVVTHSPQDGLangivYISEDRKRDGLVLG----- 344
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDSRKKI-----NLPPQQRKIGLVFQqyalf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 --MSVKENMsltALGYFSRAGGSLKHKDEQQavgdfIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
Cdd:cd03297 88 phLNVRENL---AFGLKRKRNREDRISVDEL-----LDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 423 TRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
258-473 |
5.79e-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: 91.63 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLCGPGVN----DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglaNGIVYIS 333
Cdd:cd03299 1 LKVENLSKDWKEfklkNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK---RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 334 EDRkrdGLVLGMSVKENmsltaLGYFSRAGGSLKHKDEQQaVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTR 413
Cdd:cd03299 78 QNY---ALFPHMTVYKN-----IAYGLKKRKVDKKEIERK-VLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 414 PKVLILDEPTRGVDVGAK-KEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03299 148 PKILLLDEPFSALDVRTKeKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-218 |
5.80e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.38 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGS---LLWLG----KETTFNGP 73
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGrtvqREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 74 KSSQEAGIGIIHQELNLIPQLTIAENIFLGREFVNRFGK--IDW--KKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQM 149
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRtcFSWftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 150 VEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-226 |
7.25e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 93.71 E-value: 7.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 6 QLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEA-- 79
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 80 GIGIIHQELNLIPQLTIAENIFLGREFVNrfgkIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFE 159
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAG----TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 160 SKVIIMDEPTDALtDTET-----ESLFRVIRELksqGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVA 226
Cdd:PRK11153 159 PKVLLCDEATSAL-DPATtrsilELLKDINREL---GLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVS 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
268-494 |
1.10e-20 |
|
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: 94.89 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTS--GYVTLDGHEVVTHSPQDGLANGIVYISEDRKrdgLVLGM 345
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIVIIHQELT---LVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLtalgyfsraGGSLKHKDEQQAVGDFIR-----LFNVKTPSMEQA--IGLLSGGNQQKVAIARGLMTRPKVLI 418
Cdd:TIGR02633 94 SVAENIFL---------GNEITLPGGRMAYNAMYLraknlLRELQLDADNVTrpVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 419 LDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEVLMAAAVGK 494
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-222 |
1.26e-20 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 90.36 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfNGPKSSQEAGIGIIHQELNLIPQl 94
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 95 TIAENIFLGR-----EFVNRFGKIdwkkmyAEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAKVLSFESKVIIM 165
Cdd:cd03254 92 TIMENIRLGRpnatdEEVIEAAKE------AGAHDFIMKLPNGY--DTVLGEnggnLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 166 DEPTDALtDTETESLF-RVIRELKsQGRGIVYISHRMKEIFEiCDDVTVFRDGQFIAE 222
Cdd:cd03254 164 DEATSNI-DTETEKLIqEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEE 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.34e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.72 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngPKSSQE- 78
Cdd:PRK13647 1 MDNIIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKWv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 79 -AGIGIIHQELN-LIPQLTIAE-------NIFLGREFVNRfgkidwkkmyaEADQLLAKLNLRFKSDKLVGELSIGDQQM 149
Cdd:PRK13647 78 rSKVGLVFQDPDdQVFSSTVWDdvafgpvNMGLDKDEVER-----------RVEEALKAVRMWDFRDKPPYHLSYGQKKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 150 VEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLT 229
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
....*.
gi 2070354550 230 EDSLIE 235
Cdd:PRK13647 227 DEDIVE 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
257-492 |
1.64e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 94.43 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 257 RLKVDNLCG--PG-----VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLANGI 329
Cdd:COG4618 330 RLSVENLTVvpPGskrpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL-SQWDREELGRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 330 VYISEDrkrdglV--LGMSVKENMSltalgyfsRAGGSlkhKDEQ-----QAVG--DFIRLFN--VKTPsmeqaIG---- 394
Cdd:COG4618 409 GYLPQD------VelFDGTIAENIA--------RFGDA---DPEKvvaaaKLAGvhEMILRLPdgYDTR-----IGegga 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEmPEVLGMSDRIIVMHEGHLS 474
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHR-PSLLAAVDKLLVLRDGRVQ 545
|
250
....*....|....*...
gi 2070354550 475 GEFTREQATQEVLMAAAV 492
Cdd:COG4618 546 AFGPRDEVLARLARPAAA 563
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-222 |
1.94e-20 |
|
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: 89.47 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPkssQEAGIGIIHQELNLIPQLTIAENIFLGR 104
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 105 EFVNRFGKIDWKKMyaeaDQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVI 184
Cdd:cd03298 96 SPGLKLTAEDRQAI----EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 2070354550 185 RELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:cd03298 172 LDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
268-473 |
3.67e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 91.70 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVTHSPqdglANgivyisedrKRD-GLV---- 342
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG-RDVTGLP----PE---------KRNvGMVfqdy 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 -L--GMSVKENmsltaLGYfsraggSLKH----KDEQQA-VGDFIRLfnVKTPSMEQA-IGLLSGGNQQKVAIARGLMTR 413
Cdd:COG3842 87 aLfpHLTVAEN-----VAF------GLRMrgvpKAEIRArVAELLEL--VGLEGLADRyPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 414 PKVLILDEPTRGVDVGAKK----EIYQLINQFkadGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREemreELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-222 |
4.08e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.69 E-value: 4.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSsqeagigiIHQELNLIPQ------ 93
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--------LARRLALLPQhhltpe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 94 -LTIAENIFLGRE-FVNRFGKIDwKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDA 171
Cdd:PRK11231 90 gITVRELVAYGRSpWLSLWGRLS-AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 172 LTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
266-473 |
4.29e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 88.62 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLAN-----GIVYisEDRKrdg 340
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRGRAIPYlrrkiGVVF--QDFR--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 341 LVLGMSVKENMSltalgyFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGLlSGGNQQKVAIARGLMTRPKVLILD 420
Cdd:cd03292 89 LLPDRNVYENVA------FALEVTGVPPREIRKRVPAALELVGLSHKHRALPAEL-SGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 421 EPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-233 |
4.44e-20 |
|
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: 89.37 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 2 DALLQLKGIDKAFPGVKALSGAALNVYPG-RVmALVGENGAGKSTMMKVLTG-IYTRDAGSLLWLGKETtfnGPKSSQE- 78
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGeHW-AILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERR---GGEDVWEl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 79 -AGIGIIHQEL-NLIPQLTIAENIFL-GrefvnRFGKID-WKK----MYAEADQLLAKLNLRFKSDKLVGELSIGDQQMV 150
Cdd:COG1119 77 rKRIGLVSPALqLRFPRDETVLDVVLsG-----FFDSIGlYREptdeQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVA-TL 228
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEeVL 231
|
....*
gi 2070354550 229 TEDSL 233
Cdd:COG1119 232 TSENL 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-228 |
5.16e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.91 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEA- 79
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 80 -GIGIIHQELNLIPQLTIAENIflgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSF 158
Cdd:COG1135 82 rKIGMIFQHFNLLSSRTVAENV----ALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 159 ESKVIIMDEPTDALtDTE-TESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATL 228
Cdd:COG1135 158 NPKVLLCDEATSAL-DPEtTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
266-481 |
6.38e-20 |
|
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: 88.79 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivyISEDRKRDGLVL-- 343
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKE--------LRKARRRIGMIFqh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 -----GMSVKENMSLTalgyFSRAGGSLKHKDEQqaVGDFIRLfnvktpsmeqaIGL----------LSGGNQQKVAIAR 408
Cdd:cd03258 91 fnllsSRTVFENVALP----LEIAGVPKAEIEER--VLELLEL-----------VGLedkadaypaqLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
258-472 |
6.92e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.21 E-value: 6.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC---GP--GVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhevvthspQDGLANGIVYI 332
Cdd:PRK11701 7 LSVRGLTklyGPrkGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM--------RDGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 SEDRKR---------------DGLVLGMSVKENMS--LTALGyfSRAGGSLKhkdeqQAVGDFIRLFNVKTPSMEQAIGL 395
Cdd:PRK11701 79 SEAERRrllrtewgfvhqhprDGLRMQVSAGGNIGerLMAVG--ARHYGDIR-----ATAGDWLERVEIDAARIDDLPTT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-213 |
8.78e-20 |
|
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: 92.35 E-value: 8.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGV-KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwLGKETTFNGPKSSQEAGIGI 83
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA-VNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IHQELNLIPQlTIAENIFLGREFVNRfGKIDWKKMYAEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAKVLSFE 159
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDASD-AEIREALERAGLDEFVAALPQGL--DTPIGEggagLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 160 SKVIIMDEPTDALtDTETESLFR-VIRELkSQGRGIVYISHRmKEIFEICDDVTV 213
Cdd:TIGR02857 477 APLLLLDEPTAHL-DAETEAEVLeALRAL-AQGRTVLLVTHR-LALAALADRIVV 528
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
12-220 |
1.95e-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: 88.08 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 12 KAFPGVKALSgaaLNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngpKSSQEA-------GIGII 84
Cdd:cd03294 35 GQTVGVNDVS---LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA----AMSRKElrelrrkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIFLGREFVNrfgkIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQG----VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 165 MDEPTDAL-----TDTETEsLFRVIRELKsqgRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:cd03294 184 MDEAFSALdplirREMQDE-LLRLQAELQ---KTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
268-490 |
1.98e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 87.45 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGY-VTLDGHEVvthspqdglanGIVYISEDRKRDGLV---L 343
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERR-----------GGEDVWELRKRIGLVspaL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 GMSVKENMS-----LTalGYFSRAGGSLKHKDEQQA-VGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
Cdd:COG1119 88 QLRFPRDETvldvvLS--GFFDSIGLYREPTDEQRErARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 418 ILDEPTRGVDVGAKKEIYQLINQFKADG-LSIILVS---SEMPEVLgmsDRIIVMHEGHLSGEFTREQA-TQEVLMAA 490
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVThhvEEIPPGI---THVLLLKDGRVVAAGPKEEVlTSENLSEA 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-223 |
2.11e-19 |
|
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: 87.21 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKS--SQeagIGIIHQElnliP 92
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQ---IGLVSQE----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 93 QL---TIAENIFLGREFVNRFGKIDWKKMyAEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAKVLSFESKVIIM 165
Cdd:cd03249 87 VLfdgTIAENIRYGKPDATDEEVEEAAKK-ANIHDFIMSLPDGY--DTLVGErgsqLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 166 DEPTDALtDTETESLFRVIRELKSQGRGIVYISHRMKEIfEICDDVTVFRDGQfIAER 223
Cdd:cd03249 164 DEATSAL-DAESEKLVQEALDRAMKGRTTIVIAHRLSTI-RNADLIAVLQNGQ-VVEQ 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
270-481 |
5.64e-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: 88.25 E-value: 5.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVTHSPQDglangiVYISEDRKRDGLVLG----- 344
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-RTLFDSRKG------IFLPPEKRRIGYVFQearlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 --MSVKENmsltaLGY-FSRAGGSLKHKDEQQavgdFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
Cdd:TIGR02142 88 phLSVRGN-----LRYgMKRARPSERRISFER----VIELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 422 PTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-219 |
5.65e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 90.84 E-value: 5.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNgpkssqeagI 81
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN---------I 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GIIHQELNLIPQLTIAENIFLGREFVNRFGK---IDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSF 158
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHLYLYARlrgVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQF 219
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-229 |
6.09e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.58 E-value: 6.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFpGVKALSgAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngPKSSQEAGIGII 84
Cdd:COG3840 2 LRLDDLTYRY-GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT---ALPPAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIFLGREFVNRFGKIDWKKMyaeaDQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQV----EQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 165 MDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLT 229
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
265-468 |
6.39e-19 |
|
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: 89.65 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 265 GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLANGIVYISEdrkRDGLVLG 344
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL-ADADADSWRDQIAWVPQ---HPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 mSVKENMSLtALGYFSRAggSLKHKDEQQAVGDFIRLF--NVKTPSMEQAIGLlSGGNQQKVAIARGLMTRPKVLILDEP 422
Cdd:TIGR02857 411 -TIAENIRL-ARPDASDA--EIREALERAGLDEFVAALpqGLDTPIGEGGAGL-SGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2070354550 423 TRGVDVGAKKEIYQLINQFkADGLSIILVSSEmPEVLGMSDRIIVM 468
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRAL-AQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-233 |
6.95e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.75 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngPKSSQEAG--IG 82
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVE---ALSARAASrrVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQELNLIPQLTIAENIFLGRE-FVNRFGKIDWKKMYAeADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESK 161
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTpHRSRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE-REVATLTEDSL 233
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAgPPADVLTADTL 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
268-472 |
9.70e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.70 E-value: 9.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVTHSPQDglangivyisedrKRD-------- 339
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG-QDITHVPAE-------------NRHvntvfqsy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 340 GLVLGMSVKENMsltALGyfsraggsLK-----HKDEQQAVGDFIRLfnVKTPSM-EQAIGLLSGGNQQKVAIARGLMTR 413
Cdd:PRK09452 96 ALFPHMTVFENV---AFG--------LRmqktpAAEITPRVMEALRM--VQLEEFaQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 414 PKVLILDEPTRGVDVGAKK----EIYQLINQFkadGLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKqmqnELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
268-471 |
1.01e-18 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 84.62 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHevvthspqdglangIVYISEDRKRDGLVL---- 343
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK--------------PIKAKERRKSIGYVMqdvd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 ----GMSVKENMSLTALGYfsraggslkhKDEQQAVGDFIRLFNVKTPsMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
Cdd:cd03226 82 yqlfTDSVREELLLGLKEL----------DAGNEQAETVLKDLDLYAL-KERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 420 DEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEmPEVLGM-SDRIIVMHEG 471
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHD-YEFLAKvCDRVLLLANG 202
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
268-471 |
1.04e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.78 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVyisedRKRDGLVLGMSV 347
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV-----PQFDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMSLtalgyFSRAGGSLKHKDEQQAVG--DFIRLFNvktpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
Cdd:PRK13537 98 RENLLV-----FGRYFGLSAAAARALVPPllEFAKLEN----KADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2070354550 426 VDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-204 |
1.05e-18 |
|
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: 85.23 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPkSSQEAGIGIIHQElNLIPQLTIAE 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQE-NVLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 99 NIFLGREFVNRFGKIDWKKMyAEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAKVLSFESKVIIMDEPTDALtD 174
Cdd:cd03252 95 NIALADPGMSMERVIEAAKL-AGAHDFISELPEGY--DTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSAL-D 170
|
170 180 190
....*....|....*....|....*....|..
gi 2070354550 175 TETESLfrVIRELK--SQGRGIVYISHRMKEI 204
Cdd:cd03252 171 YESEHA--IMRNMHdiCAGRTVIIIAHRLSTV 200
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
268-487 |
1.40e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 87.12 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYG-AMPrTSGYVTLDGHEVVTH-SPQDglangivyisedrKRDGLVLG- 344
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETP-DSGRIVLNGRDLFTNlPPRE-------------RRVGFVFQh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 ------MSVKENMS--LTALGYFsraggslkhKDEQQA-VGDFIRLFnvktpsmeQAIGL-------LSGGNQQKVAIAR 408
Cdd:COG1118 84 yalfphMTVAENIAfgLRVRPPS---------KAEIRArVEELLELV--------QLEGLadrypsqLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLsgeftrEQ--ATQE 485
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRwLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI------EQvgTPDE 220
|
..
gi 2070354550 486 VL 487
Cdd:COG1118 221 VY 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
270-472 |
1.87e-18 |
|
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: 86.69 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVthspQDGlANGIvYISEDRKRDGLVLG----- 344
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVL----QDS-ARGI-FLPPHRRRIGYVFQearlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 --MSVKENmsltaLGY-FSRAGGSLKHKDEQQAVgdfiRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
Cdd:COG4148 90 phLSVRGN-----LLYgRKRAPRAERRISFDEVV----ELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 422 PTRGVDVGAKKEI--Y--QLINQFkadGLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:COG4148 160 PLAALDLARKAEIlpYleRLRDEL---DIPILYVSHSLDEVARLADHVVLLEQGR 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-217 |
1.88e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 86.68 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngPKSSQEAGIGII 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS---RLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIFLGREFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 165 MDEPTDALTDTETESLFRVIR----ELKSQGrgiVYISHRMKEIFEICDDVTVFRDG 217
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRqlheELKFTS---VFVTHDQEEAMEVADRVVVMSQG 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-228 |
2.38e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.16 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETT-FNGPKSSQEA 79
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 80 gIGIIHQELNLIPQLTIAENIFLGREFVNRfgkIDWKKMYAEADQLLAKLNLRfkSDKLVGELSIGDQQMVEIAKVLSFE 159
Cdd:PRK11614 82 -VAIVPEGRRVFSRMTVEENLAMGGFFAER---DQFQERIKWVYELFPRLHER--RIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATL 228
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-428 |
3.59e-18 |
|
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: 87.30 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 6 QLKGIDKAFPGVKA-LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIytrdagsllwlgkETTFNGPKSSQE-AGIGI 83
Cdd:TIGR03719 6 TMNRVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-------------DKDFNGEARPQPgIKVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IHQELNLIPQLTIAENIFLG----REFVNRFGKI---------DWKKMYAEADQLLAKLN-----------------LRF 133
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVEEGvaeiKDALDRFNEIsakyaepdaDFDKLAAEQAELQEIIDaadawdldsqleiamdaLRC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 134 KS-DKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTETES-LFRVIRELK----------------------- 188
Cdd:TIGR03719 153 PPwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHL-DAESVAwLERHLQEYPgtvvavthdryfldnvagwilel 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 189 SQGRGIVYISH----------RMKEifEICDDVTvfRDGQFIAERE-------------VATLTE-DSLIEMMVGRKLED 244
Cdd:TIGR03719 232 DRGRGIPWEGNysswleqkqkRLEQ--EEKEESA--RQKTLKRELEwvrqspkgrqaksKARLARyEELLSQEFQKRNET 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 245 QYPHLDNAP--GEIRLKVDNLC-GPG----VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLdGHEVV 317
Cdd:TIGR03719 308 AEIYIPPGPrlGDKVIEAENLTkAFGdkllIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 318 thspqdglangIVYIseDRKRDGLVLGMSVKENMS----LTALGYF---SRAggslkhkdeqqavgdFIRLFNVKTPSME 390
Cdd:TIGR03719 387 -----------LAYV--DQSRDALDPNKTVWEEISggldIIKLGKReipSRA---------------YVGRFNFKGSDQQ 438
|
490 500 510
....*....|....*....|....*....|....*...
gi 2070354550 391 QAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
Cdd:TIGR03719 439 KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-223 |
4.79e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.14 E-value: 4.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfNGPKSSQEAGIGIIHQElnliPQL 94
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR-DLTLESLRRQIGVVPQD----TFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 95 ---TIAENIflgrefvnRFGKID------WK--KMyAEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAKVLSFE 159
Cdd:COG1132 426 fsgTIRENI--------RYGRPDatdeevEEaaKA-AQAHEFIEALPDGY--DTVVGErgvnLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 160 SKVIIMDEPTDALtDTETESL-FRVIRELkSQGRGIVYISHRMKEIfEICDDVTVFRDGQfIAER 223
Cdd:COG1132 495 PPILILDEATSAL-DTETEALiQEALERL-MKGRTTIVIAHRLSTI-RNADRILVLDDGR-IVEQ 555
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
268-468 |
5.66e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.60 E-value: 5.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvthspqDGLANGIVYI-SEDRkrdgLVLGMS 346
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV------TGPGPDRGVVfQEPA----LLPWLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 347 VKENMSLtALgyfsRAGGSLKHKDEQQA------VG--DFIRLFnvktPSMeqaiglLSGGNQQKVAIARGLMTRPKVLI 418
Cdd:COG1116 97 VLDNVAL-GL----ELRGVPKAERRERArellelVGlaGFEDAY----PHQ------LSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 419 LDEPTRGVDVGAKKEIYQLINQ-FKADGLSIILVSSEMPEVLGMSDRIIVM 468
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRlWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-222 |
8.29e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.77 E-value: 8.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfNGP--KSSQeAG 80
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HLPmhKRAR-LG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIFLGREFVnrfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFES 160
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELR----KLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 161 KVIIMDEP---TDALTdteTESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:COG1137 156 KFILLDEPfagVDPIA---VADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAE 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-218 |
9.38e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.39 E-value: 9.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngPKSSQEAGIGII 84
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT---HRSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIFLGREFVNRfGKIDWKKMYAEAdqlLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLGV-PKEERKQRVKEA---LELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 165 MDEPTDALTDTETESLFRVIRELKSQgRGI--VYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQ-FNItsLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
268-471 |
1.23e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 81.93 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMP---RTSGYVTLDGHEVVTHSPQDGLAngivYISEDrkrDGLVLG 344
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKCVA----YVRQD---DILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 MSVKENMSLTALgyfsRAGGSLKHKDEQQAVGDFIRLFNVK-TPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
Cdd:cd03234 96 LTVRETLTYTAI----LRLPRKSSDAIRKKRVEDVLLRDLAlTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2070354550 424 RGVDVGAKKEIYQLINQFkADGLSIILVSSEMP--EVLGMSDRIIVMHEG 471
Cdd:cd03234 172 SGLDSFTALNLVSTLSQL-ARRNRIVILTIHQPrsDLFRLFDRILLLSSG 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
268-473 |
1.29e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLA-NGIVYISED----RKrdglv 342
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPMHKRArLGIGYLPQEasifRK----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 lgMSVKENMsLTALGYFSraggsLKHKDEQQAVGDFIRLFNV----KTPSMeqaigLLSGGNQQKVAIARGLMTRPKVLI 418
Cdd:COG1137 93 --LTVEDNI-LAVLELRK-----LSKKEREERLEELLEEFGIthlrKSKAY-----SLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 419 LDEPTRGVDVGAKKEIYQLINQFKADGLSIIL----VSsempEVLGMSDRIIVMHEGHL 473
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLKERGIGVLItdhnVR----ETLGICDRAYIISEGKV 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
270-482 |
1.29e-17 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 82.10 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLAN------GIVYISEDrkrdgLVL 343
Cdd:COG4181 30 GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL-FALDEDARARlrarhvGFVFQSFQ-----LLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 GMSVKENMSLTALgyfsRAGgslkHKD-EQQAVgdfirlfnvktpSMEQAIGL----------LSGGNQQKVAIARGLMT 412
Cdd:COG4181 104 TLTALENVMLPLE----LAG----RRDaRARAR------------ALLERVGLghrldhypaqLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEmPEVLGMSDRIIVMHEGHLSGEFTREQA 482
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHD-PALAARCDRVLRLRAGRLVEDTAATAA 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
266-468 |
1.45e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.74 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdglangivyisedRKRDGLVLGM 345
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-------------RSEVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKEnmsLTALGYFSRAGGSLKH-KDEQQAVGDfirlfnvktpSME---------QAIGLLSGGNQQKVAIARGLMTRPK 415
Cdd:NF040873 73 TVRD---LVAMGRWARRGLWRRLtRDDRAAVDD----------ALErvgladlagRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 416 VLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEmPEVLGMSDRIIVM 468
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-223 |
1.54e-17 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 81.89 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLG---KETTFNgpksSQEAGIGIIHQELNLIP 92
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLA----SLRRQIGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 93 QlTIAENIFLGREFVNRFGKIDWKKMyAEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAKVLSFESKVIIMDEP 168
Cdd:cd03251 90 D-TVAENIAYGRPGATREEVEEAARA-ANAHEFIMELPEGY--DTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 169 TDALtDTETESLF-RVIRELkSQGRGIVYISHRMKEIfEICDDVTVFRDGQfIAER 223
Cdd:cd03251 166 TSAL-DTESERLVqAALERL-MKNRTTFVIAHRLSTI-ENADRIVVLEDGK-IVER 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
266-493 |
1.76e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.44 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHE---------------VVTHSPQDGLANGIV 330
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdirnkagMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 331 yiSEDrkrdgLVLGmsvKENMSLTALGYFSRAGGSLKhkdeqqAVGdfirLFNVKtpsmEQAIGLLSGGNQQKVAIARGL 410
Cdd:PRK13633 104 --EED-----VAFG---PENLGIPPEEIRERVDESLK------KVG----MYEYR----RHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLgMSDRIIVMHEGHLSGEFTREQATQEVLMA 489
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAV-EADRIIVMDSGKVVMEGTPKEIFKEVEMM 238
|
....
gi 2070354550 490 AAVG 493
Cdd:PRK13633 239 KKIG 242
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-219 |
2.40e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 85.84 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSgaaLNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETtfngpkssqEAGIGIIHQELNLIPQ- 93
Cdd:TIGR01257 944 PAVDRLN---ITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---------ETNLDAVRQSLGMCPQh 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 94 ------LTIAENIFLGREFVNRfgkiDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDE 167
Cdd:TIGR01257 1012 nilfhhLTVAEHILFYAQLKGR----SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 168 PTDALTDTETESLFRVIRELKSqGRGIVYISHRMKEIFEICDDVTVFRDGQF 219
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
264-473 |
2.42e-17 |
|
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: 81.92 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 264 CGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivyISEDRKRD---- 339
Cdd:cd03294 36 QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKE--------LRELRRKKismv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 340 ----GLVLGMSVKENmslTALGyFSRAGgsLKHKDEQQAVGDFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPK 415
Cdd:cd03294 108 fqsfALLPHRTVLEN---VAFG-LEVQG--VPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 416 VLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
255-473 |
2.94e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.58 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 255 EIRLKVDNLC-------GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSpqdglan 327
Cdd:PRK13632 5 SVMIKVENVSfsypnseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 328 givyISEDRKRDGLVL--------GMSVKENMSLtalgyfsraggSLKHKDEQQAVGDFIRLFNVKTPSMEQAIG----L 395
Cdd:PRK13632 78 ----LKEIRKKIGIIFqnpdnqfiGATVEDDIAF-----------GLENKKVPPKKMKDIIDDLAKKVGMEDYLDkepqN 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGL-SIILVSSEMPEVLgMSDRIIVMHEGHL 473
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
266-472 |
3.50e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.57 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVyisedRKRDGLVLGM 345
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV-----PQFDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLtalgyFSRAGGsLKHKDEQQAVG---DFIRLFNvktpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
Cdd:PRK13536 130 TVRENLLV-----FGRYFG-MSTREIEAVIPsllEFARLES----KADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2070354550 423 TRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
249-490 |
3.61e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 84.45 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 249 LDNAPGEIRLkvDNLC------GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQ 322
Cdd:COG1132 333 LPPVRGEIEF--ENVSfsypgdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 323 DgLANGIVYISEDrkrdGLVLGMSVKENMSLtalgyfsragGSLKHKDEQ--QA-----VGDFIRlfnvktpSMEQaiGL 395
Cdd:COG1132 411 S-LRRQIGVVPQD----TFLFSGTIRENIRY----------GRPDATDEEveEAakaaqAHEFIE-------ALPD--GY 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 396 ----------LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIIL---VSSempevLGMS 462
Cdd:COG1132 467 dtvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIahrLST-----IRNA 541
|
250 260
....*....|....*....|....*...
gi 2070354550 463 DRIIVMHEGHLSgeftrEQATQEVLMAA 490
Cdd:COG1132 542 DRILVLDDGRIV-----EQGTHEELLAR 564
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
266-486 |
3.79e-17 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 80.81 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLANGIVYISEDRkrdGLVLGM 345
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE-LRRKIGYVIQQI---GLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLTAlgyfsraggSLKHKDEQQA---VGDFIRLFNVKTPS-MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
Cdd:cd03295 91 TVEENIALVP---------KLLKWPKEKIrerADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 422 PTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL-----SGEFTREQATQEV 486
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIvqvgtPDEILRSPANDFV 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
268-473 |
4.38e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.71 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVYISEDRKrdgLVLGMSV 347
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEAS---IFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENmsLTALGYFSRAGGSLKHKDEQQAVGDFIRLFNVKTpSMEQAiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:PRK10895 96 YDN--LMAVLQIRDDLSAEQREDRANELMEEFHIEHLRD-SMGQS---LSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2070354550 428 VGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK10895 170 PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-236 |
5.73e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.19 E-value: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAGIG 82
Cdd:PRK13644 1 MIRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQ--ELNLIPQlTIAENIFLGREFVNrFGKIDWKKMyaeADQLLAKLNL---RFKSDKlvgELSIGDQQMVEIAKVLS 157
Cdd:PRK13644 81 IVFQnpETQFVGR-TVEEDLAFGPENLC-LPPIEIRKR---VDRALAEIGLekyRHRSPK---TLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIfEICDDVTVFRDGQFIAEREVATLTED------ 231
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDvslqtl 231
|
250
....*....|
gi 2070354550 232 -----SLIEM 236
Cdd:PRK13644 232 gltppSLIEL 241
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
257-473 |
5.91e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 82.04 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 257 RLKVDNLC-----GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVTH-SPQD-GLA--- 326
Cdd:COG3839 3 SLELENVSksyggVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG-RDVTDlPPKDrNIAmvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 327 -NGIVYISedrkrdglvlgMSVKENMSLtalgyfsraggSLKH----KDE-QQAVGDFIRLFNVkTPSMEQAIGLLSGGN 400
Cdd:COG3839 82 qSYALYPH-----------MTVYENIAF-----------PLKLrkvpKAEiDRRVREAAELLGL-EDLLDRKPKQLSGGQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 401 QQKVAIARGLMTRPKVLILDEPTRGVDvgAK------KEIYQLINQFKAdglSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLD--AKlrvemrAEIKRLHRRLGT---TTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
266-481 |
6.49e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.83 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEvvthspqdgLANGIVYisEDRKRDGLV--- 342
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---------LSEETVW--DVRRQVGMVfqn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 -----LGMSVKENMSltalgyFSRAGGSLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
Cdd:PRK13635 90 pdnqfVGATVQDDVA------FGLENIGVPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 418 ILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLgMSDRIIVMHEGHLSGEFTREQ 481
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEE 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-221 |
6.96e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.82 E-value: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKettfngPKSSQEAGIGIIHQELNLI----PQLT 95
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK------PLDYSKRGLLALRQQVATVfqdpEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 96 IAENIFLGREFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2070354550 176 ETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIA 221
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
266-468 |
8.30e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 79.40 E-value: 8.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTL--DGHEV--VTHSPQDglangIVYIsedRKRdgl 341
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlAQASPRE-----ILAL---RRR--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 342 vlgmsvkenmsltALGYFS-------------------RAGGSLKHKDEQQAvGDFIRLFNVKTPSMEQAIGLLSGGNQQ 402
Cdd:COG4778 94 -------------TIGYVSqflrviprvsaldvvaeplLERGVDREEARARA-RELLARLNLPERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVM 468
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
265-486 |
9.47e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.56 E-value: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 265 GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGlangivyISEDRKRDGLVLG 344
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKD-------IKQIRKKVGLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 M---SVKENMSLTALGYFSRAGGSLKHKDEQQAVgDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
Cdd:PRK13649 93 FpesQLFEETVLKDVAFGPQNFGVSQEEAEALAR-EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 422 PTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEV 486
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDV 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
271-450 |
1.04e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.69 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 271 VSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvtHSPQDGLANGIVYISEdrkRDGLVLGMSVKEN 350
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL--DFQRDSIARGLLYLGH---APGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 351 MSltalgyFSRAggslKHKDEQ--QAVGDfirlfnVKTPSMEQAI-GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:cd03231 94 LR------FWHA----DHSDEQveEALAR------VGLNGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|...
gi 2070354550 428 VGAKKEIYQLINQFKADGLSIIL 450
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVL 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
268-493 |
1.04e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.82 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLAngivyisedrKRDGlVLgmsv 347
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-LA----------RRRA-VL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMSLT---------ALGyfsRAGGSLKHKDEQQAVGDfirlfnvktpSMEQAiGL----------LSGGNQQKVAIAR 408
Cdd:PRK13548 82 PQHSSLSfpftveevvAMG---RAPHGLSRAEDDALVAA----------ALAQV-DLahlagrdypqLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 409 GLM------TRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVssempevlgM---------SDRIIVMHEGH 472
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVV---------LhdlnlaaryADRIVLLHQGR 218
|
250 260
....*....|....*....|.
gi 2070354550 473 LSGEFTREQATQEVLMAAAVG 493
Cdd:PRK13548 219 LVADGTPAEVLTPETLRRVYG 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
268-473 |
1.09e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 79.11 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhevvTHSPQDGLANGIVYisedrkrdglvlGMSV 347
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVSSLLGLGGGFNP------------ELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KEN--MSLTALGyFSRaggslkhkDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
Cdd:cd03220 102 RENiyLNGRLLG-LSR--------KEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2070354550 426 VDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
266-471 |
1.10e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.81 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEvVTHSPQDGLANGIVYISEdrkrdGLVLGM 345
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPINMMFQSY-----ALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSltalgyFSRAGGSLKHKDEQQAVGDFIRL-----FNVKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILD 420
Cdd:PRK11607 107 TVEQNIA------FGLKQDKLPKAEIASRVNEMLGLvhmqeFAKRKPHQ------LSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 421 EPTRGVDVGAKKEI-YQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK11607 175 EPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-222 |
1.17e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.09 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKetTFNGPKSSQEAG-----IGIIHQELNLIPQL 94
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAElrnqkLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 95 TIAENIFLGRefvnRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTD 174
Cdd:PRK11629 103 TALENVAMPL----LIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 175 TETESLFRVIREL-KSQGRGIVYISH------RMKEIFEIcddvtvfRDGQFIAE 222
Cdd:PRK11629 179 RNADSIFQLLGELnRLQGTAFLVVTHdlqlakRMSRQLEM-------RDGRLTAE 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
270-473 |
1.24e-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: 79.05 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSpQDGLANGIVYISEDRkrdgLVLGMSVKE 349
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQEP----VLFARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 350 NMsltALGYFSRAGGSLKHKDEQQAVGDFIRLFNvKTPSME--QAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:cd03248 107 NI---AYGLQSCSFECVKEAAQKAHAHSFISELA-SGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2070354550 428 VGAKKEIYQLINQFKADglSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03248 183 AESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
268-470 |
1.98e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.00 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivyisedrkrdglvlgMSV 347
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK---------------------LYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMSLTaLGYFSRAGGSLKHKDEQQAvgdfirLFNVKTPSM-EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
Cdd:PRK09544 79 DTTLPLT-VNRFLRLRPGTKKEDILPA------LKRVQAGHLiDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2070354550 427 DVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHE 470
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
2.20e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 2 DALLQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFN--GPKSSQE 78
Cdd:PRK13636 3 DYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSrkGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 79 AgIGIIHQEL-NLIPQLTIAENIFLGRefVNRfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLS 157
Cdd:PRK13636 83 S-VGMVFQDPdNQLFSASVYQDVSFGA--VNL--KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 158 FESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
269-501 |
2.23e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.51 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLAnGIVYisedrKRDGLVLGMSVK 348
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKV-GFVF-----QHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 349 ENMS--LTALGYFSR-AGGSLKHKDEQqaVGDFIRLFNV--KTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPT 423
Cdd:PRK10851 93 DNIAfgLTVLPRRERpNAAAIKAKVTQ--LLEMVQLAHLadRYPAQ------LSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 424 RGVDVGAKKE----IYQLINQFKadgLSIILVSSEMPEVLGMSDRIIVMHEGHLS-----GEFTREQATQEVLmaAAVGK 494
Cdd:PRK10851 165 GALDAQVRKElrrwLRQLHEELK---FTSVFVTHDQEEAMEVADRVVVMSQGNIEqagtpDQVWREPATRFVL--EFMGE 239
|
....*..
gi 2070354550 495 LNRVNQE 501
Cdd:PRK10851 240 VNRLQGT 246
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
266-452 |
2.24e-16 |
|
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: 81.64 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVTHSPQDGLANGIVYISEDRKrdglVLGM 345
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG-VPVSSLDQDEVRRRVSVCAQDAH----LFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLtalgyfSRAGGS---LKHKDEQQAVGDFIRLF--NVKTPSMEQAIgLLSGGNQQKVAIARGLMTRPKVLILD 420
Cdd:TIGR02868 424 TVRENLRL------ARPDATdeeLWAALERVGLADWLRALpdGLDTVLGEGGA-RLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|..
gi 2070354550 421 EPTRGVDVGAKKEIYQLINQfKADGLSIILVS 452
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLA-ALSGRTVVLIT 527
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
270-486 |
2.40e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.39 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivYISEDRKRDGLVLGMSVKE 349
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQK-------EIKPVRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 350 NMSLTALG--YFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:PRK13643 97 LFEETVLKdvAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 428 VGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEV 486
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEV 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-222 |
2.99e-16 |
|
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: 78.14 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGkettfNGPKSSQE---AGIGIIH-QELNLIP 92
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRRKkflRRIGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 93 QLTIAENIFLGREFVNrfgkIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDAL 172
Cdd:cd03267 109 DLPVIDSFYLLAAIYD----LPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 173 TDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:cd03267 185 DVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
268-489 |
3.47e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.68 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLANGIVYISED-------RKRDG 340
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSQRIRMIFQDpstslnpRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 341 LVLGMSVKENMSLTAlgyfsraggslkhKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
Cdd:PRK15112 108 QILDFPLRLNTDLEP-------------EQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 421 EPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEghlsGEFTREQATQEVLMA 489
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQ----GEVVERGSTADVLAS 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-215 |
3.78e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 77.47 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFP-----GVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGP 73
Cdd:COG4778 1 MTTLLEVENLSKTFTlhlqgGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 74 KSSQ-------EAGIGIIHQELNLIPQLT----IAENIF-LGrefvnrfgkIDWKKMYAEADQLLAKLNLR--------- 132
Cdd:COG4778 81 QASPreilalrRRTIGYVSQFLRVIPRVSaldvVAEPLLeRG---------VDREEARARARELLARLNLPerlwdlppa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 133 -FksdklvgelSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICD-- 209
Cdd:COG4778 152 tF---------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADrv 222
|
....*..
gi 2070354550 210 -DVTVFR 215
Cdd:COG4778 223 vDVTPFS 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
268-472 |
4.09e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 79.37 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLA--NGIVYISEDrkrdglvlgm 345
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrSDIQMIFQD---------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 svkenmSLTALgyfsraggslkhkDEQQAVGDFI----RLFNVKTP---------SMEQAIGLL-----------SGGNQ 401
Cdd:PRK15079 107 ------PLASL-------------NPRMTIGEIIaeplRTYHPKLSrqevkdrvkAMMLKVGLLpnlinryphefSGGQC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
268-472 |
4.70e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 79.24 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdGLAN-----GIV----YISED-RK 337
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE-AQKLlrqkiQIVfqnpYGSLNpRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 338 RDGLVLGMSVKENMSLTAlgyfsraggslkhKDEQQAVGDFIRLFNVKT------PSMeqaiglLSGGNQQKVAIARGLM 411
Cdd:PRK11308 110 KVGQILEEPLLINTSLSA-------------AERREKALAMMAKVGLRPehydryPHM------FSGGQRQRIAIARALM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-218 |
4.73e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 79.35 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKssqEAGIG 82
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK---DRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQELNLIPQLTIAENIflgrEF---VNRFGKIDWKKMYAEA------DQLLaklnlrfksDKLVGELSIGDQQMVEIA 153
Cdd:COG3839 79 MVFQSYALYPHMTVYENI----AFplkLRKVPKAEIDRRVREAaellglEDLL---------DRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 154 KVLSFESKVIIMDEPT---DAL--TDTETEsLFRVIRELKSqgrGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:COG3839 146 RALVREPKVFLLDEPLsnlDAKlrVEMRAE-IKRLHRRLGT---TTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
266-471 |
8.23e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.46 E-value: 8.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLAN-GIVYISEDRKrdglVLG 344
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKiGMVFQNPDNQ----FVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 MSVKENMSltalgyFSRAGGSLKHKDEQQAVGDFIRL-----FNVKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLIL 419
Cdd:PRK13650 97 ATVEDDVA------FGLENKGIPHEEMKERVNEALELvgmqdFKEREPAR------LSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 420 DEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVlGMSDRIIVMHEG 471
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNG 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
268-478 |
8.36e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.90 E-value: 8.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGlangivYISEDRKRDGLVL---- 343
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI-THKTKDK------YIRPVRKRIGMVFqfpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 -------------------GMSVKENMS-----LTALGyFSRaggslkhkdeqqavgdfirlfNVktpsMEQAIGLLSGG 399
Cdd:PRK13646 96 sqlfedtvereiifgpknfKMNLDEVKNyahrlLMDLG-FSR---------------------DV----MSQSPFQMSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFT 478
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTS 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-467 |
8.54e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 8.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLlwlGKETT-------FNGP------KSSQEAGIGIIH--QELNLIPQ 93
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---EEEPSwdevlkrFRGTelqnyfKKLYNGEIKVVHkpQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 94 LtiaeniFLG--REFVNrfgKIDWKKMYaeaDQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDA 171
Cdd:PRK13409 175 V------FKGkvRELLK---KVDERGKL---DEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 172 LTDTETESLFRVIRELkSQGRGIVYISHRMKEIFEICDDVTV-----------------------------------FRD 216
Cdd:PRK13409 243 LDIRQRLNVARLIREL-AEGKYVLVVEHDLAVLDYLADNVHIaygepgaygvvskpkgvrvgineylkgylpeenmrIRP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 217 GQFiaEREVATLTEDSLIEMMVgrkledQYPHLDNAPGEIRLKVDnlcgPGvndvsfVLRKGEILGISGLMGAGRTELMK 296
Cdd:PRK13409 322 EPI--EFEERPPRDESERETLV------EYPDLTKKLGDFSLEVE----GG------EIYEGEVIGIVGPNGIGKTTFAK 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 297 VLYGAMPRTSGYVTLDghEVVTHSPQdglangivYISEDRKrdglvlgMSVKENMSLTAlgyfSRAGGS-LKHkdeqqav 375
Cdd:PRK13409 384 LLAGVLKPDEGEVDPE--LKISYKPQ--------YIKPDYD-------GTVEDLLRSIT----DDLGSSyYKS------- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 376 gDFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV----GAKKEIYQLINQFKAdglSIILV 451
Cdd:PRK13409 436 -EIIKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRIAEEREA---TALVV 510
|
490
....*....|....*.
gi 2070354550 452 SSEMPEVLGMSDRIIV 467
Cdd:PRK13409 511 DHDIYMIDYISDRLMV 526
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
269-472 |
8.57e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 76.57 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDglangivyISEDRKRDGLVL----- 343
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKD--------INKLRRKVGMVFqqfnl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 --GMSVKENMSLtALGYfsraggsLKHKDEQQAVgdfirlfnvktpsmEQA------IGL----------LSGGNQQKVA 405
Cdd:COG1126 89 fpHLTVLENVTL-APIK-------VKKMSKAEAE--------------ERAmellerVGLadkadaypaqLSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 406 IARGLMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKADGLSIILVSSEMP---EVlgmSDRIIVMHEGH 472
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGfarEV---ADRVVFMDGGR 213
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-220 |
8.71e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.74 E-value: 8.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwLGKETTFNGPKSSQEAG-----IGIIHQ--ELNL 90
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTI-VGDYAIPANLKKIKEVKrlrkeIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 91 IpQLTIAENIflgrefvnRFGKI----DWKKMYAEADQLLAKLNL-RFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIM 165
Cdd:PRK13645 104 F-QETIEKDI--------AFGPVnlgeNKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 166 DEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-239 |
8.98e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 2 DALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWlgKETTFNGPKSSQEA-G 80
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL--DAQPLESWSSKAFArK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAENIFLGRE----FVNRFGKIDWKKMyaeaDQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVL 156
Cdd:PRK10575 87 VAYLPQQLPAAEGMTVRELVAIGRYpwhgALGRFGAADREKV----EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 157 SFESKVIIMDEPTDALTDTETESLFRVIRELkSQGRGIVYIS--HRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLI 234
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRL-SQERGLTVIAvlHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETL 241
|
....*
gi 2070354550 235 EMMVG 239
Cdd:PRK10575 242 EQIYG 246
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-428 |
9.86e-16 |
|
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: 79.83 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 29 PGRVMALVGENGAGKSTMMKVLTG-------IYTRDA----------GSLLwlgkettFNGPKSSQEAGIGIIH--QELN 89
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGelkpnlgDYDEEPswdevlkrfrGTEL-------QDYFKKLANGEIKVAHkpQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 90 LIPQLtiaeniFLG--REFVNrfgKIDWKKMyaeADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDE 167
Cdd:COG1245 171 LIPKV------FKGtvRELLE---KVDERGK---LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 168 PTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTV---------------------------------- 213
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIlygepgvygvvskpksvrvginqyldgylpeenv 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 214 -FRDGQFiaEREVATLTEDSLIEMMVgrkledQYPHLDNAPGEIRLKVDnlcgPGVndvsfvLRKGEILGISGLMGAGRT 292
Cdd:COG1245 319 rIRDEPI--EFEVHAPRREKEEETLV------EYPDLTKSYGGFSLEVE----GGE------IREGEVLGIVGPNGIGKT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 293 ELMKVLYGAMPRTSGYVtlDGHEVVTHSPQdglangivYISEDrkRDGLV---LGMSVKENMsltalgyfsragGSLKHK 369
Cdd:COG1245 381 TFAKILAGVLKPDEGEV--DEDLKISYKPQ--------YISPD--YDGTVeefLRSANTDDF------------GSSYYK 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 370 DEqqavgdFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
Cdd:COG1245 437 TE------IIKPLGLE-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-172 |
1.32e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 77.85 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPG-----------VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETT 69
Cdd:COG4608 4 AEPLLEVRDLKKHFPVrgglfgrtvgvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 70 FNGPKSSQE--AGIGIIHQE----LNliPQLTIAEnIfLGREFVNrFGKIDWKKMYAEADQLLAKLNLR-FKSDKLVGEL 142
Cdd:COG4608 84 GLSGRELRPlrRRMQMVFQDpyasLN--PRMTVGD-I-IAEPLRI-HGLASKAERRERVAELLELVGLRpEHADRYPHEF 158
|
170 180 190
....*....|....*....|....*....|
gi 2070354550 143 SIGDQQMVEIAKVLSFESKVIIMDEPTDAL 172
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
268-473 |
1.32e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEvvthsPQdglangivyisEDR----KRDGLVL 343
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PF-----------KRRkefaRRIGVVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 G--------MSVKENMSLTALGYfsraggSLKHKDEQQAVGDFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPK 415
Cdd:COG4586 102 GqrsqlwwdLPAIDSFRLLKAIY------RIPDAEYKKRLDELVELLDLG-ELLDTPVRQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 416 VLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-220 |
1.44e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 74.89 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 12 KAFPGVKALSGAALnvyPGRVMALVGENGAGKSTMMKVLTG--IYTRDAGSLLwlgkettFNGPKSSQEAG---IGIIHQ 86
Cdd:cd03213 20 SGKQLLKNVSGKAK---PGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVL-------INGRPLDKRSFrkiIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 87 ELNLIPQLTIAENIflgrefvnrfgkidwkkMYAeadqllAKLnlrfKSdklvgeLSIGDQQMVEIAKVLSFESKVIIMD 166
Cdd:cd03213 90 DDILHPTLTVRETL-----------------MFA------AKL----RG------LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 167 EPTDALTDTETESLFRVIRELKSQGRGIVYISHRMK-EIFEICDDVTVFRDGQFI 220
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
264-471 |
1.76e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 74.89 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 264 CGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVL--YGAMPRTSGYVTLDGHEvvthSPQDGLANGIVYISEDrkrDGL 341
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRP----LDKRSFRKIIGYVPQD---DIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 342 VLGMSVKENMSLTALgyfsraggsLKHkdeqqavgdfirlfnvktpsmeqaiglLSGGNQQKVAIARGLMTRPKVLILDE 421
Cdd:cd03213 94 HPTLTVRETLMFAAK---------LRG---------------------------LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 422 PTRGVDVGAKKEIYQLINQFKADGLSIILV----SSEMpevLGMSDRIIVMHEG 471
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRLADTGRTIICSihqpSSEI---FELFDKLLLLSQG 188
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
268-458 |
1.80e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.52 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLANGIVYISEDRkrdgLVLGMSV 347
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI-YRQQVSYCAQTP----TLFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMsltALGYFSRAggslKHKDEQQAVGDFIRlFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:PRK10247 98 YDNL---IFPWQIRN----QQPDPAIFLDDLER-FALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190
....*....|....*....|....*....|..
gi 2070354550 428 VGAKKEIYQLINQFKAD-GLSIILVSSEMPEV 458
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREqNIAVLWVTHDKDEI 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-220 |
1.87e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.97 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIytRDAGSLLWLGKETTFNG-----PKS 75
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRM--NDLNPEVTITGSIVYNGhniysPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 76 SQ---EAGIGIIHQELNLIPqLTIAENIFLGRefvnRFGKIDWKKMYAEA-----------DQLLAKLNlrfksDKLVGe 141
Cdd:PRK14239 80 DTvdlRKEIGMVFQQPNPFP-MSIYENVVYGL----RLKGIKDKQVLDEAvekslkgasiwDEVKDRLH-----DSALG- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 142 LSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-221 |
1.98e-15 |
|
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: 78.64 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKA--LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwLGKETTFNGPKSSQEAGIG 82
Cdd:COG4618 331 LSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR-LDGADLSQWDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQELNLIPQlTIAENIflgrefvNRFGKIDWKKMY-----AEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIA 153
Cdd:COG4618 410 YLPQDVELFDG-TIAENI-------ARFGDADPEKVVaaaklAGVHEMILRLPDGY--DTRIGEggarLSGGQRQRIGLA 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 154 KVLSFESKVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISHRMKeIFEICDDVTVFRDGQFIA 221
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNL-DDEGEaALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQA 546
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-223 |
2.18e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.91 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLG---KETTFngpkSSQEA 79
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTL----ASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 80 GIGIIHQELNLIPQlTIAENIFLGR-EFVNRFGKIDWKKMyAEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAK 154
Cdd:PRK11176 418 QVALVSQNVHLFND-TIANNIAYARtEQYSREQIEEAARM-AYAMDFINKMDNGL--DTVIGEngvlLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 155 VLSFESKVIIMDEPTDALtDTETEslfRVIR----ELKsQGRGIVYISHRMKEIfEICDDVTVFRDGQfIAER 223
Cdd:PRK11176 494 ALLRDSPILILDEATSAL-DTESE---RAIQaaldELQ-KNRTSLVIAHRLSTI-EKADEILVVEDGE-IVER 559
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
266-490 |
2.30e-15 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 75.34 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLygamPR----TSGYVTLDGHEVVTHSPQDgLANGIVYISEDRkrdgL 341
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLI----PRfydvDSGRILIDGHDVRDYTLAS-LRRQIGLVSQDV----F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 342 VLGMSVKENMsltALGYFSRAGGSLKHKDEQQAVGDFIRlfnvKTPS-MEQAIG----LLSGGNQQKVAIARGLMTRPKV 416
Cdd:cd03251 87 LFNDTVAENI---AYGRPGATREEVEEAARAANAHEFIM----ELPEgYDTVIGergvKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 417 LILDEPTRGVDVGAKKEIYQLINQFKADGLSIIlVSSEMPEVLGmSDRIIVMHEGHLsgeftREQATQEVLMAA 490
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFV-IAHRLSTIEN-ADRIVVLEDGKI-----VERGTHEELLAQ 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
271-476 |
2.48e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.91 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 271 VSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEV--VTHSPQDGLANGIVYISEDRKrdgLVLGMSVK 348
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrLKNREVPFLRRQIGMIFQDHH---LLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 349 ENMSLTALgyfsRAGGSlkhkdeqqavGDFIRLfnvKTPSMEQAIGL----------LSGGNQQKVAIARGLMTRPKVLI 418
Cdd:PRK10908 98 DNVAIPLI----IAGAS----------GDDIRR---RVSAALDKVGLldkaknfpiqLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 419 LDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGE 476
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
266-489 |
2.79e-15 |
|
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: 75.34 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEV--VThspQDGLangivyisedRKRDGLVL 343
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVT---LDSL----------RRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 GMSVKENMSLtalgYFSRAGGSLKHKDEQQ-------AVGDFIRLFNVKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPK 415
Cdd:cd03253 82 QDTVLFNDTI----GYNIRYGRPDATDEEVieaakaaQIHDKIMRFPDGYDTIVGERGLkLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 416 VLILDEPTRGVDVGAKKEIYQLINQFkADGLSIILVSSEMPEVLGmSDRIIVMHEGHLSgeftrEQATQEVLMA 489
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV-----ERGTHEELLA 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-249 |
3.00e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 75.54 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKettfngPKSSQEAgigiihQELNLI----PQ-- 93
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR------PLAAWSP------WELARRravlPQhs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 94 -----LTIAENIFLGREFVNRFGKIDwkkmYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVL-------SFESK 161
Cdd:COG4559 85 slafpFTVEEVVALGRAPHGSSAAQD----RQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH-----RMkeifeICDDVTVFRDGQFIAE---REVatLTEDSL 233
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHdlnlaAQ-----YADRILLLHQGRLVAQgtpEEV--LTDELL 233
|
250 260
....*....|....*....|.
gi 2070354550 234 -----IEMMVGRKLEDQYPHL 249
Cdd:COG4559 234 ervygADLRVLAHPEGGCPQV 254
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-218 |
3.06e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.48 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwlgketTFNGPKSSQEAGIGII 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQELNLIPQLTIAENIFLGRefvnrfgKIDWKkmyAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL-------KGQWR---DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 165 MDEP---TDALTDTETESLfrvIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:PRK11247 157 LDEPlgaLDALTRIEMQDL---IESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-237 |
3.07e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.91 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSGAALNVYPGRVMALVGENGAGKS-TMMKVLTGIYTRD-AGSLLWLGKETTFNGPKSSQEAGIGII-----HQE 87
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNiSGTVFKDGKEVDVSTVSDAIDAGLAYVtedrkGYG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 88 LNLIPqlTIAENIFLGR-EFVNRFGKIDWKKMYAEADQLLAKLNLRFKS-DKLVGELSIGDQQMVEIAKVLSFESKVIIM 165
Cdd:NF040905 351 LNLID--DIKRNITLANlGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSvFQKVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 166 DEPT---DALTDTEtesLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLIEMM 237
Cdd:NF040905 429 DEPTrgiDVGAKYE---IYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-217 |
3.10e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.94 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 11 DKAFpgvkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAgIGIIHQElnl 90
Cdd:PRK13648 20 DASF----TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH-IGIVFQN--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 91 ipqltiAENIFLGR--EFVNRFG----KIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:PRK13648 92 ------PDNQFVGSivKYDVAFGlenhAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 165 MDEPTDALTDTETESLFRVIRELKSQGR-GIVYISHRMKEIFEiCDDVTVFRDG 217
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKG 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
268-471 |
3.22e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.56 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLAN-GIVYISEDRKrdglVLGMS 346
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHiGIVFQNPDNQ----FVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 347 VKENMSltalgyFSRAGGSLKHKDEQQAVGDFIRLFNV--KTPSMEQAiglLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
Cdd:PRK13648 101 VKYDVA------FGLENHAVPYDEMHRRVSEALKQVDMleRADYEPNA---LSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2070354550 425 GVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGmSDRIIVMHEG 471
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
271-452 |
3.74e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.93 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 271 VSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvtHSPQDGLANGIVYISEdrkRDGLVLGMSVKEN 350
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL--AEQRDEPHENILYLGH---LPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 351 MSltalgyFSRAggslKHKDEQQAVGDFIRLFNVKtpSMEQAI-GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVG 429
Cdd:TIGR01189 94 LH------FWAA----IHGGAQRTIEDALAAVGLT--GFEDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|...
gi 2070354550 430 AKKEIYQLINQFKADGLSIILVS 452
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTT 184
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
268-473 |
3.74e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 76.31 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQD--GLANGIVYISED-------RKR 338
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrPLRRRMQMVFQDpyaslnpRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 339 DGLVLGMSVKENMSLTALGYFSRAGGSLkhkdeqQAVG---DFIRLFnvktPSMeqaiglLSGGNQQKVAIARGLMTRPK 415
Cdd:COG4608 114 VGDIIAEPLRIHGLASKAERRERVAELL------ELVGlrpEHADRY----PHE------FSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 416 VLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKI 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-220 |
4.14e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPG-RVmALVGENGAGKSTMMKVLTGIYTRDAGSLLWlGKETTfngpkssqeagIG 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGdRI-GLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQEL-NLIPQLTIAENIFLGREfvnrfgkiDWKKMYAEadQLLAKLNlrFKSD---KLVGELSIGDQQMVEIAKVLSF 158
Cdd:COG0488 382 YFDQHQeELDPDKTVLDELRDGAP--------GGTEQEVR--GYLGRFL--FSGDdafKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 159 ESKVIIMDEPTDALtDTET-ESLFRVIRELKsqgrG-IVYISH-RMkeiF--EICDDVTVFRDGQFI 220
Cdd:COG0488 450 PPNVLLLDEPTNHL-DIETlEALEEALDDFP----GtVLLVSHdRY---FldRVATRILEFEDGGVR 508
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-203 |
4.26e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.12 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfnGPKSSQeagiGI 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IHQELNLIPQLTIAENIFLGREfvnrFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVI 163
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQ----LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2070354550 164 IMDEP---TDALT-DTETESLFRVIRElksQGRGIVYISHRMKE 203
Cdd:PRK11248 151 LLDEPfgaLDAFTrEQMQTLLLKLWQE---TGKQVLLITHDIEE 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
268-473 |
4.43e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 76.27 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivyISEDRKRdglvLGM-- 345
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE--------LRAARRK----IGMif 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 ---------SVKENMSLtalgyfsraggSLKH----KDEQQA-VGDFIRLfnvktpsmeqaIGL----------LSGGNQ 401
Cdd:COG1135 89 qhfnllssrTVAENVAL-----------PLEIagvpKAEIRKrVAELLEL-----------VGLsdkadaypsqLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQL---INQ-FkadGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLlkdINReL---GLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-213 |
4.67e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.28 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEA--GIGIIHQE----LNli 91
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsDIQMIFQDplasLN-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 92 PQLTIAENIF---------LGREFVnrfgKIDWKKMYAEADqLLAKLNLRFKSdklvgELSIGDQQMVEIAKVLSFESKV 162
Cdd:PRK15079 113 PRMTIGEIIAeplrtyhpkLSRQEV----KDRVKAMMLKVG-LLPNLINRYPH-----EFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 163 IIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTV 213
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLV 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
266-468 |
4.70e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 74.90 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvtHSPqdGLANGIVYisedrKRDGLVLGM 345
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--TGP--GADRGVVF-----QKDALLPWL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENmslTALGYfsRAGGSLKHKDEQQAvGDFIRLfnVKTPSMEQA-IGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
Cdd:COG4525 92 NVLDN---VAFGL--RLRGVPKAERRARA-EELLAL--VGLADFARRrIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2070354550 425 GVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVM 468
Cdd:COG4525 164 ALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
269-473 |
4.74e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 74.66 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVL-YGAMPRtSGYVTLDGHEV-VTHSPQDGLangivyISEDRKRDGLVLG-- 344
Cdd:COG4161 19 FDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPD-SGQLNIAGHQFdFSQKPSEKA------IRLLRQKVGMVFQqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 -----MSVKENMSLTALgyfsRAGGSLKHKDEQQAVGDFIRLfnvKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLI 418
Cdd:COG4161 92 nlwphLTVMENLIEAPC----KVLGLSKEQAREKAMKLLARL---RLTDKADRFPLhLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 419 LDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-218 |
4.80e-15 |
|
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: 74.43 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAgIGIIHQElnliPQL 94
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQE----PVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 95 ---TIAENIFLGREFVNrFGKIDWKKMYAEADQLLAKLNLRFKSDklVGE----LSIGDQQMVEIAKVLSFESKVIIMDE 167
Cdd:cd03248 100 farSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTE--VGEkgsqLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 168 PTDALtDTETESLFRVIRELKSQGRGIVYISHRMKEIfEICDDVTVFRDGQ 218
Cdd:cd03248 177 ATSAL-DAESEQQVQQALYDWPERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
247-471 |
5.03e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.59 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 247 PHLDNAPGEIRLKVDNLC---------GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDG---- 313
Cdd:PRK10261 2 PHSDELDARDVLAVENLNiafmqeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 314 ---HEVVTHSPQDGlangivyiSEDRKRDGLVLGMSVKENMslTALGYFSRAGGSLKHK-------DEQQAVGDFIRLFN 383
Cdd:PRK10261 82 rrsRQVIELSEQSA--------AQMRHVRGADMAMIFQEPM--TSLNPVFTVGEQIAESirlhqgaSREEAMVEAKRMLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 384 -VKTPSMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPE 457
Cdd:PRK10261 152 qVRIPEAQTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGV 231
|
250
....*....|....
gi 2070354550 458 VLGMSDRIIVMHEG 471
Cdd:PRK10261 232 VAEIADRVLVMYQG 245
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-231 |
5.14e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.84 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKettfngPKSSQE-----AGIGIIHQEln 89
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV------PLVQYDhhylhRQVALVGQE-- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 90 liPQL---TIAENIFLGREFVNRfGKIDWKKMYAEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAKVLSFESKV 162
Cdd:TIGR00958 564 --PVLfsgSVRENIAYGLTDTPD-EEIMAAAKAANAHDFIMEFPNGY--DTEVGEkgsqLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 163 IIMDEPTDALtDTETESLFRVIRelKSQGRGIVYISHRMKEIfEICDDVTVFRDGQFIAEREVATLTED 231
Cdd:TIGR00958 639 LILDEATSAL-DAECEQLLQESR--SRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
269-489 |
5.63e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 5.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLANgivYIS---EDRKRdGLVLGM 345
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKRAK---YIGrvfQDPMM-GTAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLTALGYFSRAGGSLKHKDEQQAVGDFIRLFNVKTPS-MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
Cdd:COG1101 98 TIEENLALAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLENrLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 425 GVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEGH----LSGEfTREQATQEVLMA 489
Cdd:COG1101 178 ALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRiildVSGE-EKKKLTVEDLLE 246
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-240 |
5.95e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.70 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 32 VMALVGENGAGKSTMMKVLT---GIY---TRDAGSLLWLGKET-TFNGPKSSQEagIGIIHQELNLIPQLTIAENIFLGr 104
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLNrliEIYdskIKVDGKVLYFGKDIfQIDAIKLRKE--VGMVFQQPNPFPHLSIYDNIAYP- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 105 efVNRFGKIDWKKMYAEADQLLAKLNL-RFKSDKL---VGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESL 180
Cdd:PRK14246 115 --LKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 181 FRVIRELKSQgRGIVYISHRMKEIFEICDDVTVFRDGQFI---AEREVATLTEDSLIE-MMVGR 240
Cdd:PRK14246 193 EKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVewgSSNEIFTSPKNELTEkYVIGR 255
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
258-473 |
6.40e-15 |
|
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: 78.13 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLCG-PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVThspqdglangivyiSEDR 336
Cdd:TIGR01257 935 VKIFEPSGrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET--------------NLDA 1000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 337 KRDGLvlGMSVKENMSLTALG------YFSRAGGslKHKDEQQavgdfirlfnVKTPSMEQAIGL----------LSGGN 400
Cdd:TIGR01257 1001 VRQSL--GMCPQHNILFHHLTvaehilFYAQLKG--RSWEEAQ----------LEMEAMLEDTGLhhkrneeaqdLSGGM 1066
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAdGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:TIGR01257 1067 QRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-220 |
7.35e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.03 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPkssQEAGIGI 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP---YQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IHQELNLIPQLTIAENIFLGRefvnRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVI 163
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGL----KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 164 IMDEPTDALTDTETESL-FRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
396-471 |
7.65e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.06 E-value: 7.65e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKG 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
266-484 |
7.81e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 77.64 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHevVTHSPQdglangIVYISEDRKRDGLVLGM 345
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQ------TSWIMPGTIKDNIIFGL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKEnmsltaLGYFSRAGGSLKHKDeqqavgdfIRLF--NVKTPSMEQAIgLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
Cdd:TIGR01271 512 SYDE------YRYTSVIKACQLEED--------IALFpeKDKTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 424 RGVDVGAKKEIYQ------LINQFKadglsiILVSSEMpEVLGMSDRIIVMHEGH--LSGEFTREQATQ 484
Cdd:TIGR01271 577 THLDVVTEKEIFEsclcklMSNKTR------ILVTSKL-EHLKKADKILLLHEGVcyFYGTFSELQAKR 638
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
268-473 |
8.43e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.27 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDG-----HEVVTHSPQDGLANGIVYISEDRKRDGLV 342
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdKKNNHELITNPYSKKIKNFKELRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LGM--------SVKENMSL--TALGyfsraggslKHKDE-QQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLM 411
Cdd:PRK13631 122 FQFpeyqlfkdTIEKDIMFgpVALG---------VKKSEaKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-218 |
1.01e-14 |
|
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: 71.86 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKA--LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKssqEAG-- 80
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN---ELGdh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQlTIAENIflgrefvnrfgkidwkkmyaeadqllaklnlrfksdklvgeLSIGDQQMVEIAKVLSFES 160
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI-----------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 161 KVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISHRMkEIFEICDDVTVFRDGQ 218
Cdd:cd03246 116 RILVLDEPNSHL-DVEGErALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-204 |
1.04e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.37 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAF-PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfnGPKSSQ----E 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIT--RLKNREvpflR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 79 AGIGIIHQELNLIPQLTIAENIFLGREFVNRFGKIDWKKMYAEADqllaKLNLRFKSDKLVGELSIGDQQMVEIAKVLSF 158
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALD----KVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2070354550 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEI 204
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
268-471 |
1.05e-14 |
|
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: 73.06 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivyisedrkRD-GLVL--- 343
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--------------RDiAMVFqny 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 ----GMSVKENMsltALGYFSRAGGSLKHKDEQQAVGDFIRLFNV--KTPSMeqaiglLSGGNQQKVAIARGLMTRPKVL 417
Cdd:cd03301 82 alypHMTVYDNI---AFGLKLRKVPKDEIDERVREVAELLQIEHLldRKPKQ------LSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 418 ILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-247 |
1.19e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.65 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKettfngPKSSQEAgig 82
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR------PLADWSP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 iihQELNLI----PQ---LTIAeniFLGREFVnRFGKIDWKKMYAEADQL----LAKLNLRFKSDKLVGELSIGDQQMVE 151
Cdd:PRK13548 72 ---AELARRravlPQhssLSFP---FTVEEVV-AMGRAPHGLSRAEDDALvaaaLAQVDLAHLAGRDYPQLSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 152 IAKVL------SFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISH------RMkeifeiCDDVTVFRDGQ 218
Cdd:PRK13548 145 LARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHdlnlaaRY------ADRIVLLHQGR 218
|
250 260 270
....*....|....*....|....*....|....*..
gi 2070354550 219 FIAE---REVatLTEDSL-----IEMMVGRKLEDQYP 247
Cdd:PRK13548 219 LVADgtpAEV--LTPETLrrvygADVLVQPHPETGAP 253
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-221 |
1.19e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngpKSSQEAGIGIIHQ--ELNLIPQ 93
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYVPQseEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 94 LTIAENIFLGrefvnRFGKIDWKKMYAEADQ-----LLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEP 168
Cdd:PRK15056 95 VLVEDVVMMG-----RYGHMGWLRRAKKRDRqivtaALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 169 TDALtDTETES-LFRVIRELKSQGRGIVYISHRMKEIFEICdDVTVFRDGQFIA 221
Cdd:PRK15056 170 FTGV-DVKTEArIISLLRELRDEGKTMLVSTHNLGSVTEFC-DYTVMVKGTVLA 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
269-489 |
1.72e-14 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 72.96 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVL---YGAmprTSGYVTLDGHEVVTHSPQDgLANGIVYISEDRkrdgLVLGM 345
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfYDP---TSGEILLDGVDIRDLNLRW-LRSQIGLVSQEP----VLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMsltALGYFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
Cdd:cd03249 92 TIAENI---RYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGsQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 425 GVDVGAKKEIYQLINQFKAdGLSIILVSSEMPEVLGmSDRIIVMHEGHLSgeftrEQATQEVLMA 489
Cdd:cd03249 169 ALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRN-ADLIAVLQNGQVV-----EQGTHDELMA 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-220 |
1.79e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.12 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLlWLGKetTFNGPKSSQEAG---------------- 80
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGD--IYIGDKKNNHELitnpyskkiknfkelr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 --IGIIHQ--ELNLIPQlTIAENIFlgrefvnrFGKIDWKKMYAEADQL----LAKLNLRFKS-DKLVGELSIGDQQMVE 151
Cdd:PRK13631 116 rrVSMVFQfpEYQLFKD-TIEKDIM--------FGPVALGVKKSEAKKLakfyLNKMGLDDSYlERSPFGLSGGQKRRVA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 152 IAKVLSFESKVIIMDEPTDALtDTETES-LFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGL-DPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
268-473 |
1.85e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 74.76 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVTHSPQDGLANGIVYISEdrkrdGLVLGMSV 347
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG-EDVTHRSIQQRDICMVFQSY-----ALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENmsltaLGYFSRAGGslKHKDE-QQAVGDFIRLfnVKTPSME-QAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
Cdd:PRK11432 96 GEN-----VGYGLKMLG--VPKEErKQRVKEALEL--VDLAGFEdRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 426 VDVGAKK----EIYQLINQFkadGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK11432 167 LDANLRRsmreKIRELQQQF---NITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-222 |
2.46e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.13 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLlwlgketTFNGPKSSQE 78
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI-------TVGGMVLSEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 79 ------AGIGIIHQelNLIPQL---TIAENIFLGREfvNRfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQM 149
Cdd:PRK13635 75 tvwdvrRQVGMVFQ--NPDNQFvgaTVQDDVAFGLE--NI--GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 150 VEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVY-ISHRMKEIFEiCDDVTVFRDGQFIAE 222
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-222 |
2.48e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 72.18 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKettfngPKSSQEAGIGiihqelnLIPQLTI 96
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSLLGLGGG-------FNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 97 AENI-----FLGREFVNRFGKIDWKKMYAEADQLLaklnlrfksDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTdA 171
Cdd:cd03220 102 RENIylngrLLGLSRKEIDEKIDEIIEFSELGDFI---------DLPVKTYSSGMKARLAFAIATALEPDILLIDEVL-A 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 172 LTDTET-ESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:cd03220 172 VGDAAFqEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
270-473 |
2.95e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.15 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPqDGLAN------GIVYisedrKRDGLVL 343
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDA-DALAQlrrehfGFIF-----QRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 GMSVKENMSLTALgyfsrAGGSLKHKDEQQAVGDFIRLfnvktpSMEQAI----GLLSGGNQQKVAIARGLMTRPKVLIL 419
Cdd:PRK10535 100 HLTAAQNVEVPAV-----YAGLERKQRLLRAQELLQRL------GLEDRVeyqpSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 420 DEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEmPEVLGMSDRIIVMHEGHL 473
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-220 |
2.96e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.24 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngpKSSQEAGIGIIHQELNLIPQLTIA 97
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT----STSKNKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 98 EnifLGREFVNR---FGKIDWKKMYAEADQL-LAKLNLRFKSDKLVG----ELSIGDQQMVEIAKVLSFESKVIIMDEPT 169
Cdd:PRK13649 97 Q---LFEETVLKdvaFGPQNFGVSQEEAEALaREKLALVGISESLFEknpfELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 170 DALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
268-498 |
3.17e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.96 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvtHSPQDGLAN-----GIVYISEDRKrdglV 342
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI--DYSRKGLMKlresvGMVFQDPDNQ----L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LGMSVKENMSLTALGYfsraggSLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
Cdd:PRK13636 96 FSASVYQDVSFGAVNL------KLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 423 TRGVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEGH--LSGEFTREQATQEVLMAAAVgKLNRV 498
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRviLQGNPKEVFAEKEMLRKVNL-RLPRI 246
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-223 |
3.37e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.73 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKE-TTFNGPKSSQ--EAGIGIIHQELNLIPQLTI 96
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlHQMDEEARAKlrAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 97 AENIFLGREFVnrfGKIDwKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTE 176
Cdd:PRK10584 106 LENVELPALLR---GESS-RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL-DRQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 177 T-----ESLFRVIRElksQGRGIVYISHRmKEIFEICDDVTVFRDGQFIAER 223
Cdd:PRK10584 181 TgdkiaDLLFSLNRE---HGTTLILVTHD-LQLAARCDRRLRLVNGQLQEEA 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-222 |
3.81e-14 |
|
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: 70.42 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKET-TFNGPKSSQeagI 81
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVsDLEKALSSL---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GIIHQELNLIpQLTIAENifLGREFvnrfgkidwkkmyaeadqllaklnlrfksdklvgelSIGDQQMVEIAKVLSFESK 161
Cdd:cd03247 78 SVLNQRPYLF-DTTLRNN--LGRRF------------------------------------SGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 162 VIIMDEPTDALtDTETE-SLFRVIRELkSQGRGIVYISHRMKEIfEICDDVTVFRDGQFIAE 222
Cdd:cd03247 119 IVLLDEPTVGL-DPITErQLLSLIFEV-LKDKTLIWITHHLTGI-EHMDKILFLENGKIIMQ 177
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
268-473 |
4.09e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhevvTHSPQDGLANGI---------VYISedrkr 338
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----RVSALLELGAGFhpeltgrenIYLN----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 339 dGLVLGMSVKEnmsltalgyfsraggsLKHK-DEQQA---VGDFIRLfNVKTPSmeqaigllSGgnqQKVAIARGLMT-- 412
Cdd:COG1134 113 -GRLLGLSRKE----------------IDEKfDEIVEfaeLGDFIDQ-PVKTYS--------SG---MRARLAFAVATav 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:COG1134 164 DPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
268-473 |
4.12e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.35 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMprtSGYVTLDGH-EVVTHSPQDG--LANGIvyiSEDRKRDG---- 340
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSAGSHiELLGRTVQREgrLARDI---RKSRANTGyifq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 341 ---LVLGMSVKENMSLTALG----------YFSRAggslkhkDEQQAVGDFIRLFNVKTPsmEQAIGLLSGGNQQKVAIA 407
Cdd:PRK09984 94 qfnLVNRLSVLENVLIGALGstpfwrtcfsWFTRE-------QKQRALQALTRVGMVHFA--HQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 408 RGLMTRPKVLILDEPTRGVDVGAKK---EIYQLINQfkADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARivmDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
256-473 |
4.56e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.97 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 256 IRLKVDNlCGPGVN----DVSFVLRKGEILGISGLMGAGRTELMKVL-YGAMPRtSGYVTLDGHEV-VTHSPQDGlangi 329
Cdd:PRK11124 3 IQLNGIN-CFYGAHqalfDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNHFdFSKTPSDK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 330 vYISEDRKRDGLVLG-------MSVKENMSLTALgyfsRAGGSLKHKDEQQAVGDFIRL----FNVKTPSMeqaiglLSG 398
Cdd:PRK11124 76 -AIRELRRNVGMVFQqynlwphLTVQQNLIEAPC----RVLGLSKDQALARAEKLLERLrlkpYADRFPLH------LSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
266-471 |
4.69e-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: 75.44 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdgLANGIVYISEDRKRDGLVLGm 345
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD--VHQNMGYCPQFDAIDDLLTG- 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 svKENMSLtalgyFSRAGGSLKHKDEQQAVgdfirlFNVKTPSM----EQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
Cdd:TIGR01257 2030 --REHLYL-----YARLRGVPAEEIEKVAN------WSIQSLGLslyaDRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2070354550 422 PTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-472 |
4.80e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.78 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLG------KETTFNGPKssqeagIGIIHQEL-- 88
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadaRHRRAVCPR------IAYMPQGLgk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 89 NLIPQLTIAENI-FLGREF----VNRFGKIDwkkmyaeadQLLAKLNL-RFKsDKLVGELSIGDQQMVEIAKVLSFESKV 162
Cdd:NF033858 88 NLYPTLSVFENLdFFGRLFgqdaAERRRRID---------ELLRATGLaPFA-DRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 163 IIMDEPTdaltdTETESLFR-----VIRELKSQGRG---IV---YishrMKEIfEICDDVTVFRDGQFIAerevaTLTED 231
Cdd:NF033858 158 LILDEPT-----TGVDPLSRrqfweLIDRIRAERPGmsvLVataY----MEEA-ERFDWLVAMDAGRVLA-----TGTPA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 232 SLIEMMVGRKLEDQY------------------PHLDNAPGEIRLKVDNLC---GP--GVNDVSFVLRKGEILGISGLMG 288
Cdd:NF033858 223 ELLARTGADTLEAAFiallpeekrrghqpvvipPRPADDDDEPAIEARGLTmrfGDftAVDHVSFRIRRGEIFGFLGSNG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 289 AGRTELMKVLYGAMPRTSGYVTLDGHEVVthspqdglANGIvyisEDRKRDGLvlgMS----------VKENMSLTALGY 358
Cdd:NF033858 303 CGKSTTMKMLTGLLPASEGEAWLFGQPVD--------AGDI----ATRRRVGY---MSqafslygeltVRQNLELHARLF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 359 fsraggSLKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ-L 437
Cdd:NF033858 368 ------HLPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRlL 440
|
490 500 510
....*....|....*....|....*....|....*
gi 2070354550 438 INQFKADGLSIILVSSEMPEVLgMSDRIIVMHEGH 472
Cdd:NF033858 441 IELSREDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
269-471 |
4.97e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPR---TSGYVTLDGHEVvtHSPQDGLANGivYISEDrkrDGLVLGM 345
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEMRAISA--YVQQD---DLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLTALgyfSRAGGSLKHKDEQQAVGDFIRLFNVKtPSMEQAIGL------LSGGNQQKVAIARGLMTRPKVLIL 419
Cdd:TIGR00955 115 TVREHLMFQAH---LRMPRRVTKKEKRERVDEVLQALGLR-KCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 420 DEPTRGVDVGAKKEIYQLINQFKADGLSIILV----SSempEVLGMSDRIIVMHEG 471
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSS---ELFELFDKIILMAEG 243
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
266-473 |
5.10e-14 |
|
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: 72.15 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPqdglangivyisEDRKRDGLVLGM 345
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR------------KQRRAFRRDVQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 -------SVKENMSLTA-LGYFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
Cdd:TIGR02769 93 vfqdspsAVNPRMTVRQiIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 418 ILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-445 |
5.95e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.90 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLtgiytrdAGSLLWLGKE--TTFNGP-KSSQEAGIGIIHQELN----- 89
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARAL-------AGELPLLSGErqSQFSHItRLSFEQLQKLVSDEWQrnntd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 90 -LIPQ-----LTIAENIFLGREFVNRFgkidwkKMYAEADQLLAKLNLRFKsdklvgELSIGDQQMVEIAKVLSFESKVI 163
Cdd:PRK10938 90 mLSPGeddtgRTTAEIIQDEVKDPARC------EQLAQQFGITALLDRRFK------YLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLI------EMM 237
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVaqlahsEQL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 238 VGRKLED-----QYPHL-DNAPgEIRLK---VDNLCGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRtsGY 308
Cdd:PRK10938 238 EGVQLPEpdepsARHALpANEP-RIVLNngvVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQ--GY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 309 ---VTLDGHevvthspQDGLANGIVYIsedRKRDGLV---LGMSVKENMSLTAL---GYFSRAGGSLKHKDEQQAVGD-F 378
Cdd:PRK10938 315 sndLTLFGR-------RRGSGETIWDI---KKHIGYVsssLHLDYRVSTSVRNVilsGFFDSIGIYQAVSDRQQKLAQqW 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 379 IRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADG 445
Cdd:PRK10938 385 LDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEG 451
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
6.12e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.03 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGpKSSQEA--G 80
Cdd:PRK13639 1 ILETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK-KSLLEVrkT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQelNLIPQL---TIAENIFLGRefVN-RFGKIDWKKMYAEAdqlLAKLNLRFKSDKLVGELSIGDQQMVEIAKVL 156
Cdd:PRK13639 80 VGIVFQ--NPDDQLfapTVEEDVAFGP--LNlGLSKEEVEKRVKEA---LKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
263-471 |
6.79e-14 |
|
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: 74.39 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 263 LCGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSpQDGLANGIVYISEDRkrdgLV 342
Cdd:TIGR01193 485 YGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID-RHTLRQFINYLPQEP----YI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LGMSVKENMSLTAlgyfsraggslKHKDEQQAVGDFIRLFNVKTPSMEQAIGL----------LSGGNQQKVAIARGLMT 412
Cdd:TIGR01193 560 FSGSILENLLLGA-----------KENVSQDEIWAACEIAEIKDDIENMPLGYqtelseegssISGGQKQRIALARALLT 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 413 RPKVLILDEPTRGVDVGAKKEIyqLINQFKADGLSIILVSSEMpEVLGMSDRIIVMHEG 471
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKI--VNNLLNLQDKTIIFVAHRL-SVAKQSDKIIVLDHG 684
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-202 |
8.14e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.54 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQ------------EAGIGIIH 85
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadknqlrllRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 86 QELNLIPQLTIAENIFLGREFVNRFGKIDWKKmyaEADQLLAKLNLRFKS-DKLVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:PRK10619 99 QHFNLWSHMTVLENVMEAPIQVLGLSKQEARE---RAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 2070354550 165 MDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMK 202
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-244 |
1.16e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGV---------KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKE-TTFNGp 73
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlAKLNR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 74 kssqeAGIGIIHQELNLI---------PQLTIAENIflgREFVNRFGKIDWKKMYAEADQLLAKLNLRFK-SDKLVGELS 143
Cdd:PRK10419 82 -----AQRKAFRRDIQMVfqdsisavnPRKTVREII---REPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 144 IGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
250 260
....*....|....*....|..
gi 2070354550 223 REVatlTEDSLIEMMVGRKLED 244
Cdd:PRK10419 234 QPV---GDKLTFSSPAGRVLQN 252
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-220 |
1.52e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.48 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIyTRD-----AGSLLWLGKETTFNGPKSSQE---AGIGIIHQEL 88
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDnwhvtADRFRWNGIDLLKLSPRERRKiigREIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 89 N--LIPQLTI----AENI---FLGREFVNRFGkidWKKMYAEAdqLLAKLNLrfKSDKLV-----GELSIGDQQMVEIAK 154
Cdd:COG4170 99 SscLDPSAKIgdqlIEAIpswTFKGKWWQRFK---WRKKRAIE--LLHRVGI--KDHKDImnsypHELTEGECQKVMIAM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 155 VLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
266-471 |
1.56e-13 |
|
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: 69.83 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLANGIVYISEDrkrdGLVLGM 345
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD-LRSRISIIPQD----PVLFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENmsLTALGYFSRAggSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDEPTR 424
Cdd:cd03244 93 TIRSN--LDPFGEYSDE--ELWQALERVGLKEFVESLPGGLDTVVEEGGEnLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2070354550 425 GVDVGAKKEIYQLI-NQFKadGLSIILVSSEMPEVLGmSDRIIVMHEG 471
Cdd:cd03244 169 SVDPETDALIQKTIrEAFK--DCTVLTIAHRLDTIID-SDRILVLDKG 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-220 |
1.60e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.07 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSGAALnvyPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAgIGIIHQELNLIPQl 94
Cdd:PRK13657 349 QGVEDVSFEAK---PGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN-IAVVFQDAGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 95 TIAENIFLGR-----EFVNRFGKIdwkkmyAEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAKVLSFESKVIIM 165
Cdd:PRK13657 424 SIEDNIRVGRpdatdEEMRAAAER------AQAHDFIERKPDGY--DTVVGErgrqLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 166 DEPTDALtDTETESlfRVIRELK--SQGRGIVYISHRMKEIFEiCDDVTVFRDGQFI 220
Cdd:PRK13657 496 DEATSAL-DVETEA--KVKAALDelMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
270-478 |
1.66e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSP--QDGLAN---GIVYisedrKRDGLVLG 344
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaaKAELRNqklGFIY-----QFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 MSVKENMSLTALgyfsraggsLKHKDEQQAvgdfirlfNVKTPSMEQAIGL----------LSGGNQQKVAIARGLMTRP 414
Cdd:PRK11629 102 FTALENVAMPLL---------IGKKKPAEI--------NSRALEMLAAVGLehranhrpseLSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 415 KVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFT 478
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-220 |
1.93e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFN-GPKSSQEagigiIHQELNLIPQL-- 94
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtGNKNLKK-----LRKKVSLVFQFpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 95 ------TIAENIFLGREfvnRFGKIDwKKMYAEADQLLAKLNLrfkSDKLVG----ELSIGDQQMVEIAKVLSFESKVII 164
Cdd:PRK13641 96 aqlfenTVLKDVEFGPK---NFGFSE-DEAKEKALKWLKKVGL---SEDLISkspfELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 165 MDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
269-474 |
1.96e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 69.74 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvthspQDGLANgivyISEDRKRDGLVLG---- 344
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-----NDPKVD----ERLIRQEAGMVFQqfyl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 ---MSVKENMSLTALgyfsRAGGSLKHKDEQQA------VGDFIRLFNVktPSMeqaiglLSGGNQQKVAIARGLMTRPK 415
Cdd:PRK09493 89 fphLTALENVMFGPL----RVRGASKEEAEKQArellakVGLAERAHHY--PSE------LSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 416 VLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLS 474
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-218 |
2.48e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.07 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDaGSLLWLGKETTFNGPKSSQEAGI-------GIIHQELNL 90
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEFFNQNIYERRVNLnrlrrqvSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 91 IPqLTIAENIFLGREFVNRFGKIDWKKMYAEADQlLAKL--NLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEP 168
Cdd:PRK14258 100 FP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALK-DADLwdEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 169 T---DALTDTETESLFRVIReLKSQgRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:PRK14258 178 CfglDPIASMKVESLIQSLR-LRSE-LTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-222 |
2.57e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 70.21 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSllwlGKETTFNGPKSSQEA------GIGIIHQEL-NLI 91
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP----NSKITVDGITLTAKTvwdireKVGIVFQNPdNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 92 PQLTIAENIFLGREfvNRfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDA 171
Cdd:PRK13640 98 VGATVGDDVAFGLE--NR--AVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 172 LTDTETESLFRVIREL-KSQGRGIVYISHRMKEIfEICDDVTVFRDGQFIAE 222
Cdd:PRK13640 174 LDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQ 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-226 |
2.63e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.22 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGaaLNVYPGR--VMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAgIGIIHQELN-LIPQ 93
Cdd:PRK13652 17 KEALNN--INFIAPRnsRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VGLVFQNPDdQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 94 LTIAENIFLGREFVNrfgkIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALT 173
Cdd:PRK13652 94 PTVEQDIAFGPINLG----LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 174 DTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVA 226
Cdd:PRK13652 170 PQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-222 |
2.89e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.34 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAG---------SLLWLGkeTTFNgpkssqeagigiihqe 87
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGrvevngrvsALLELG--AGFH---------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 88 lnliPQLTIAENIFLG-------REFVN-RFGKIDWkkmYAEadqLLAKLNLRFKSdklvgeLSIGdqqMV-----EIAk 154
Cdd:COG1134 101 ----PELTGRENIYLNgrllglsRKEIDeKFDEIVE---FAE---LGDFIDQPVKT------YSSG---MRarlafAVA- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 155 vLSFESKVIIMDEPTdALTDTE-TESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:COG1134 161 -TAVDPDILLVDEVL-AVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
258-485 |
2.91e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 69.73 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLCG-----PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVthSPqdGLANGIVYi 332
Cdd:PRK11248 2 LQISHLYAdyggkPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GP--GAERGVVF- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 sedrKRDGLVLGMSVKENMsltALGYfsRAGGSLKHKDEQQAvGDFIRLFNVKTPSmEQAIGLLSGGNQQKVAIARGLMT 412
Cdd:PRK11248 77 ----QNEGLLPWRNVQDNV---AFGL--QLAGVEKMQRLEIA-HQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEG------HLSGEFTREQATQE 485
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGpgrvveRLPLNFARRFVAGE 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
250-473 |
2.98e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.68 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 250 DNAPGEIRLKVDNLC---G--PGVNDVSFVLRKGEILGISGLMGAGRTELMKV------LY-GAmpRTSGYVTLDGHEVv 317
Cdd:COG1117 4 PASTLEPKIEVRNLNvyyGdkQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndLIpGA--RVEGEILLDGEDI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 318 tHSPQdglangiVYISEDRKRDGLV------LGMSVKENMsltALGYfsRAGGsLKHKDE---------QQA-----VGD 377
Cdd:COG1117 81 -YDPD-------VDVVELRRRVGMVfqkpnpFPKSIYDNV---AYGL--RLHG-IKSKSEldeiveeslRKAalwdeVKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 378 fiRLfnvKTPSMEqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADgLSIILVSSEMPE 457
Cdd:COG1117 147 --RL---KKSALG-----LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQ 215
|
250
....*....|....*.
gi 2070354550 458 VLGMSDRIIVMHEGHL 473
Cdd:COG1117 216 AARVSDYTAFFYLGEL 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
266-481 |
2.99e-13 |
|
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: 69.18 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEV--VTHSpqdGLANGIVYISEDRkrdgLVL 343
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrdISRK---SLRSMIGVVLQDT----FLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 GMSVKENMSLtalgyfsragGSLKHKDEQ-----QAVG--DFI-RLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPK 415
Cdd:cd03254 90 SGTIMENIRL----------GRPNATDEEvieaaKEAGahDFImKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 416 VLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILvsSEMPEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIII--AHRLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
268-491 |
4.10e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.45 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSpqdglangivyISEDRKRDGLVLGMSV 347
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN-----------IREVRKFVGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMSLTALG--YFSRAGGSLKHKDEQQAVGDFIRLFNVKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
Cdd:PRK13652 89 DQIFSPTVEQdiAFGPINLGLDEETVAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 426 VDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQA-TQEVLMAAA 491
Cdd:PRK13652 168 LDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLARV 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
304-493 |
4.59e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.98 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 304 RTSGYVTLDGHEVVTHSPQDgLANGIVYISEDRkrdgLVLGMSVKENMSltalgyFSRAGGSL---KHKDEQQAVGDFIR 380
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKD-LRNLFSIVSQEP----MLFNMSIYENIK------FGKEDATRedvKRACKFAAIDEFIE 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 381 LFNVKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVL 459
Cdd:PTZ00265 1343 SLPNKYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
170 180 190
....*....|....*....|....*....|....
gi 2070354550 460 GMSDRIIVMHEGHLSGEFTREQATQEVLMAAAVG 493
Cdd:PTZ00265 1423 KRSDKIVVFNNPDRTGSFVQAHGTHEELLSVQDG 1456
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
268-490 |
4.87e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 69.35 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLAN-GIVYISEDRKrdglVLGMS 346
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKiGMVFQNPDNQ----FVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 347 VKENMSLTALGYFSRAGGSLKHKDEQQAVGDFIRlFNVKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLD-FKTREPAR------LSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 427 DVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVlGMSDRIIVMHeghlSGEFTREQATQEVLMAA 490
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEA-ASSDRILVMK----AGEIIKEAAPSELFATS 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
231-490 |
5.33e-13 |
|
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: 71.29 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 231 DSLIEMMVGRKledqypHLDNAPGEIRLKVDNLCGPG-----VNDVSFVLRKGEILGISGLMGAGRTELMKVLygamPR- 304
Cdd:TIGR02203 312 DSPPEKDTGTR------AIERARGDVEFRNVTFRYPGrdrpaLDSISLVIEPGETVALVGRSGSGKSTLVNLI----PRf 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 305 ---TSGYVTLDGHEVVTHSPQDgLANGIVYISEDrkrdgLVL-GMSVKENMSLTALGYFSRAggslkhKDEQQAVGDFIR 380
Cdd:TIGR02203 382 yepDSGQILLDGHDLADYTLAS-LRRQVALVSQD-----VVLfNDTIANNIAYGRTEQADRA------EIERALAAAYAQ 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 381 LFNVKTP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaDGLSIILVSSEM 455
Cdd:TIGR02203 450 DFVDKLPlGLDTPIGengvLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRL 528
|
250 260 270
....*....|....*....|....*....|....*
gi 2070354550 456 PEVLGmSDRIIVMHEGHLSgeftrEQATQEVLMAA 490
Cdd:TIGR02203 529 STIEK-ADRIVVMDDGRIV-----ERGTHNELLAR 557
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-239 |
5.49e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLlWLGKETTFNGPKSSQEAGIGIIHQELNLIPQLTIAENIFLGR 104
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 105 eFVNRFGKIDWKKMYAEA-DQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRV 183
Cdd:PRK10253 107 -YPHQPLFTRWRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 184 IREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDSLIEMMVG 239
Cdd:PRK10253 186 LSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
263-473 |
7.65e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.64 E-value: 7.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 263 LCGPgvndVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTsGYVTLDGHEVVTHSPQDGLANgIVYISEDRKrdgLV 342
Cdd:PRK11174 365 LAGP----LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKH-LSWVGQNPQ---LP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LGmSVKENMsltALGYFSRAGGSLKHKDEQQAVGDFI-RLFN-VKTPSMEQAIGLlSGGNQQKVAIARGLMTRPKVLILD 420
Cdd:PRK11174 436 HG-TLRDNV---LLGNPDASDEQLQQALENAWVSEFLpLLPQgLDTPIGDQAAGL-SVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 421 EPTRGVDVGAKKEIYQLINQfKADGLSIILVSSEMPEVLGMsDRIIVMHEGHL 473
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
266-473 |
8.82e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.67 E-value: 8.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYG-----AMPRTSgyVTLDGHEVVTHSPQDGLAN-GIVYISEDRKRD 339
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpdDNPNSK--ITVDGITLTAKTVWDIREKvGIVFQNPDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 340 GLVLGMSVkenmsltALGYFSRAGGSLKHKD------EQQAVGDFIRlfnvKTPSMeqaiglLSGGNQQKVAIARGLMTR 413
Cdd:PRK13640 99 GATVGDDV-------AFGLENRAVPRPEMIKivrdvlADVGMLDYID----SEPAN------LSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVlGMSDRIIVMHEGHL 473
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
269-478 |
9.09e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 68.57 E-value: 9.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvtHSPQDGLAN-----GIVYISEDRKrdglVL 343
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI--KYDKKSLLEvrktvGIVFQNPDDQ----LF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 GMSVKENMSLTALGY-FSRAGGSLKHKDEQQAVGdfIRLFNVKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
Cdd:PRK13639 93 APTVEEDVAFGPLNLgLSKEEVEKRVKEALKAVG--MEGFENKPPHH------LSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 423 TRGVD-VGAKKeIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFT 478
Cdd:PRK13639 165 TSGLDpMGASQ-IMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-233 |
9.22e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.19 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKE--TTfngpKSSQEAG-IG 82
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvaTT----PSRELAKrLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQELNLIPQLTIAENIFLGReFV---NRFGKIDWKKMyaeaDQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFE 159
Cdd:COG4604 79 ILRQENHINSRLTVRELVAFGR-FPyskGRLTAEDREII----DEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 160 SKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHrmkEI-FEIC--DDVTVFRDGQFIAEREVA-TLTEDSL 233
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH---DInFASCyaDHIVAMKDGRVVAQGTPEeIITPEVL 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
272-472 |
9.62e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 67.86 E-value: 9.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 272 SFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSP---------QDGlaNgivyisedrkrdgLV 342
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaerpvsmlfQEN--N-------------LF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LGMSVKENMsltALGYfsRAGGSLKhKDEQQAVGDFIRlfNVKTPSMEQAI-GLLSGGNQQKVAIARGLMTRPKVLILDE 421
Cdd:COG3840 84 PHLTVAQNI---GLGL--RPGLKLT-AEQRAQVEQALE--RVGLAGLLDRLpGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 422 PTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
268-473 |
9.93e-13 |
|
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: 66.57 E-value: 9.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvtHSPQDGLANGIVYISEDrkrdglvlgmsv 347
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLISVLNQR------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 kenmsltalgyfsraggslkhkdeqqavgdfIRLFNVktpSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
Cdd:cd03247 84 -------------------------------PYLFDT---TLRNNLGRrFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2070354550 427 DVGAKKEIYQLINQFkADGLSIILVSSEMPEVLGMsDRIIVMHEGHL 473
Cdd:cd03247 130 DPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-199 |
1.02e-12 |
|
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: 67.13 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPkSSQEAGIGIIHQElNLIPQLTIAEN 99
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAP-GIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 100 IflgrEFVNRFGKIDwkkmyaEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETES 179
Cdd:cd03231 94 L----RFWHADHSDE------QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 2070354550 180 LFRVIRELKSQGRGIVYISH 199
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
268-473 |
1.06e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.15 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHevvthspqdglangIVYISED---------RKR 338
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK--------------VLYFGKDifqidaiklRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 339 DGLVLG-------MSVKENMSltalgYFSRAGGSLKHKDEQQAVGDFIR---LFNVKTPSMEQAIGLLSGGNQQKVAIAR 408
Cdd:PRK14246 92 VGMVFQqpnpfphLSIYDNIA-----YPLKSHGIKEKREIKKIVEECLRkvgLWKEVYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADgLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-172 |
1.07e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAG 80
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 I--------GIIHQ--ELNLIPQLTIAENI-----FLGrefVNRFGKIDwkkmyAEADQLLAKLNL-RFKSDKLVGELSI 144
Cdd:PRK11701 83 RrrllrtewGFVHQhpRDGLRMQVSAGGNIgerlmAVG---ARHYGDIR-----ATAGDWLERVEIdAARIDDLPTTFSG 154
|
170 180
....*....|....*....|....*...
gi 2070354550 145 GDQQMVEIAKVLSFESKVIIMDEPTDAL 172
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGL 182
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-212 |
1.10e-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: 67.30 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGiytRDAGSLLWLGkETTFNG----PKSSQEAgIGIIHQELNLIP 92
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG---RVEGGGTTSG-QILFNGqprkPDQFQKC-VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 93 QLTIAENIFLGREFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDAL 172
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2070354550 173 TDTETESLFRVIRELKSQGRGIVYISHRMK-EIFEICDDVT 212
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRsDLFRLFDRIL 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-222 |
1.40e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.40 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 7 LKGIDkafpgvkalsgaaLNVYPGRVMALVGENGAGKSTMMKVLTGI--YTRDAGSLLWLGKETTfngPKSSQE---AGI 81
Cdd:COG0396 16 LKGVN-------------LTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIL---ELSPDErarAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GIIHQ---ElnlIPQLTIAEniFLgREFVN--RFGKIDWKKMYAEADQLLAKLNLrfKSDKL-----VGeLSIGDQQMVE 151
Cdd:COG0396 80 FLAFQypvE---IPGVSVSN--FL-RTALNarRGEELSAREFLKLLKEKMKELGL--DEDFLdryvnEG-FSGGEKKRNE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 152 IAKVLSFESKVIIMDEP-----TDALtdtetESLFRVIRELKSQGRGIVYISH--RMKEIFEIcDDVTVFRDGQFIAE 222
Cdd:COG0396 151 ILQMLLLEPKLAILDETdsgldIDAL-----RIVAEGVNKLRSPDRGILIITHyqRILDYIKP-DFVHVLVDGRIVKS 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
396-498 |
1.42e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.78 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGH-- 472
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIeSLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKig 213
|
90 100
....*....|....*....|....*....
gi 2070354550 473 --LSGEFTREQATQEVLMAAAVGK-LNRV 498
Cdd:PRK11247 214 ldLTVDLPRPRRRGSARLAELEAEvLQRV 242
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-213 |
1.48e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.45 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFP---G-------VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTF 70
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvkrGlfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 71 NGPKSSQEA--GIGIIHQ----ELNliPQLTIAE--------NIFLGRefvnrfgkidwKKMYAEADQLLAKLNLRFK-S 135
Cdd:PRK11308 82 ADPEAQKLLrqKIQIVFQnpygSLN--PRKKVGQileeplliNTSLSA-----------AERREKALAMMAKVGLRPEhY 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 136 DKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTV 213
Cdd:PRK11308 149 DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMV 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-236 |
1.52e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.81 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAgIGIIHQEL-NLIPQLT 95
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK-IGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 96 IAENIFLGREfvNRfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
Cdd:PRK13642 99 VEDDVAFGME--NQ--GIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 176 ETESLFRVIRELKSQGR-GIVYISHRMKEIFEiCDDVTVFRDGQFIAEREVATL--TEDSLIEM 236
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELfaTSEDMVEI 237
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
254-484 |
1.58e-12 |
|
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: 67.96 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 254 GEIRLKVDNLC---GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHevVTHSPQdglangIV 330
Cdd:cd03291 36 DDNNLFFSNLClvgAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQ------FS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 331 YISEDRKRDGLVLGMSVKEnmsltalgyfSRAGGSLKHKDEQQAVGDFIRLFNvkTPSMEQAIgLLSGGNQQKVAIARGL 410
Cdd:cd03291 108 WIMPGTIKENIIFGVSYDE----------YRYKSVVKACQLEEDITKFPEKDN--TVLGEGGI-TLSGGQRARISLARAV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 411 MTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKADGlSIILVSSEMpEVLGMSDRIIVMHEG--HLSGEFTREQATQ 484
Cdd:cd03291 175 YKDADLYLLDSPFGYLDVFTEKEIFEsCVCKLMANK-TRILVTSKM-EHLKKADKILILHEGssYFYGTFSELQSLR 249
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-222 |
1.62e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.81 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 13 AFPGVKALSGAALNvYPGR-VMALVGENGAGKSTMMKVLTGIYT-----RDAGSLLwLGKETTFNGPKSSQ-EAGIGIIH 85
Cdd:PRK14271 30 GFAGKTVLDQVSMG-FPARaVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVL-LGGRSIFNYRDVLEfRRRVGMLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 86 QELNLIPqLTIAENIFLGrefVNRFGKIDWKKMYAEADQLLAKLNL-RFKSDKLVG---ELSIGDQQMVEIAKVLSFESK 161
Cdd:PRK14271 108 QRPNPFP-MSIMDNVLAG---VRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 162 VIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
277-471 |
2.05e-12 |
|
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: 66.36 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 277 KGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVyisedrKRDGLVLGMSVKENMSLtal 356
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF------QENNLFAHLTVEQNVGL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 357 gyfSRAGGSLKHKDEQQAVGDFIRLFNVKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ 436
Cdd:cd03298 94 ---GLSPGLKLTAEDRQAIEVALARVGLAG-LEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2070354550 437 LINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:cd03298 170 LVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-219 |
2.35e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.44 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 2 DALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQeagI 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH---V 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GIIHQELNLIPQLTIAENIFLGREfVNRFGKIDWKKMYAEAdqlLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESK 161
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLR-MQKTPAAEITPRVMEA---LRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 162 VIIMDEPTDALtDTETESLFRVirELKSQGR--GI--VYISHRMKEIFEICDDVTVFRDGQF 219
Cdd:PRK09452 165 VLLLDESLSAL-DYKLRKQMQN--ELKALQRklGItfVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
2.88e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLlwlgkettfngpKSSQEAG 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 IGIIHQELNLIPQLTIAeniflgrefVNRFGKIdwKKMYAEADQL--LAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSF 158
Cdd:PRK09544 69 IGYVPQKLYLDTTLPLT---------VNRFLRL--RPGTKKEDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDV 211
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
266-473 |
3.38e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.52 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivyISEDRKRDG----- 340
Cdd:PRK11153 19 HALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE--------LRKARRQIGmifqh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 341 --LVLGMSVKENMSLtALgyfsRAGGslKHKDE-QQAVGDFIRLfnvktpsmeqaIGL----------LSGGNQQKVAIA 407
Cdd:PRK11153 91 fnLLSSRTVFDNVAL-PL----ELAG--TPKAEiKARVTELLEL-----------VGLsdkadrypaqLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-218 |
3.59e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAAlnvYPGRVMALVGENGAGKSTMMKVLTGiytRDAGSLLWLGkETTFNG---PKSSQEAGIGIIHQELNLIPQL 94
Cdd:TIGR00955 42 KNVSGVA---KPGELLAVMGSSGAGKTTLMNALAF---RSPKGVKGSG-SVLLNGmpiDAKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 95 TIAENIFLGREFvnRFGKIDWKKMYAEA-DQLLAKLNLRFKSDKLVGE------LSIGDQQMVEIAKVLSFESKVIIMDE 167
Cdd:TIGR00955 115 TVREHLMFQAHL--RMPRRVTKKEKRERvDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 168 PTDALTDTETESLFRVIRELKSQGRGIVYISHR-MKEIFEICDDVTVFRDGQ 218
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGR 244
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
245-472 |
3.75e-12 |
|
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: 65.36 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 245 QYPHLDNAPGEIRLKVDNLcgPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMP---RTSGYVTLDGHEV-VTHS 320
Cdd:cd03233 2 STLSWRNISFTTGKGRSKI--PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYkEFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 321 PQDGlanGIVYISEDrkrDGLVLGMSVKENMsltalgYFS-RAGGSlkhkdeqqavgDFIRLFnvktpsmeqaigllSGG 399
Cdd:cd03233 80 KYPG---EIIYVSEE---DVHFPTLTVRETL------DFAlRCKGN-----------EFVRGI--------------SGG 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLS-IILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:cd03233 123 ERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMaDVLKTTtFVSLYQASDEIYDLFDKVLVLYEGR 197
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
29-198 |
3.82e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.28 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPkSSQEAGIGiiHQElNLIPQLTIAENIFLGREFvn 108
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV-AEACHYLG--HRN-AMKPALTVAENLEFWAAF-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 109 rFGKIDWKKMYA-EADQLLAKLNLRFksdklvGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRE 186
Cdd:PRK13539 101 -LGGEELDIAAAlEAVGLAPLAHLPF------GYLSAGQKRRVALARLLVSNRPIWILDEPTAAL-DAAAVALFaELIRA 172
|
170
....*....|..
gi 2070354550 187 LKSQGrGIVYIS 198
Cdd:PRK13539 173 HLAQG-GIVIAA 183
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-172 |
5.06e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.76 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPksSQEAgIGIIHQELNLIPQLTIAENIFLGR 104
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP--SRRP-VSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 105 EFVNRFGKIDWKKMYAEADQ--LLAKLnlrfksDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDAL 172
Cdd:PRK10771 97 NPGLKLNAAQREKLHAIARQmgIEDLL------ARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
266-489 |
7.77e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.54 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSpQDGLANGI------VYISEDRKRD 339
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS-EAALRQAIsvvsqrVHLFSATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 340 GLVLGmsvKENMSltalgyfsraggslkhkDEQ-----QAVGdfirLFNVktpsMEQAIGL----------LSGGNQQKV 404
Cdd:PRK11160 433 NLLLA---APNAS-----------------DEAlievlQQVG----LEKL----LEDDKGLnawlgeggrqLSGGEQRRL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkADGLSIILVSSEMPEVLGMsDRIIVMHEGHLsgeftREQATQ 484
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQF-DRICVMDNGQI-----IEQGTH 557
|
....*
gi 2070354550 485 EVLMA 489
Cdd:PRK11160 558 QELLA 562
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
266-474 |
7.79e-12 |
|
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: 68.05 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHevVTHSPQDGlangivYISEDRKRDGLVLGM 345
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQA------WIQNDSLRENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLTALgyfsrAGGSLKHKDEQQAVGDfirlfnvKTPSMEQAIGlLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
Cdd:TIGR00957 724 ALNEKYYQQVL-----EACALLPDLEILPSGD-------RTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 426 VDVGAKKEIYQliNQFKADGL----SIILVS---SEMPEVlgmsDRIIVMHEGHLS 474
Cdd:TIGR00957 791 VDAHVGKHIFE--HVIGPEGVlknkTRILVThgiSYLPQV----DVIIVMSGGKIS 840
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
260-487 |
9.09e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 260 VDNLCGPgvndVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPrTSGYVTLDGHEVVTHSPQDgLANGIVYISEDRKRd 339
Cdd:PRK03695 8 VSTRLGP----LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAE-LARHRAYLSQQQTP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 340 glVLGMSVKEnmsltalgYFSRAGGSLKHKDE-QQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIA-------RGLM 411
Cdd:PRK03695 81 --PFAMPVFQ--------YLTLHQPDKTRTEAvASALNEVAEALGL-DDKLGRSVNQLSGGEWQRVRLAavvlqvwPDIN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL--SGEfTREQATQEVL 487
Cdd:PRK03695 150 PAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLlaSGR-RDEVLTPENL 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-220 |
1.01e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAG----------------- 80
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVleklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 81 ------IGIIHQ--ELNLIPQlTIAENIFlgrefvnrFGKIDWKKMYAEADQLLAKLnlrfksDKLVG-----------E 141
Cdd:PRK13651 101 keirrrVGVVFQfaEYQLFEQ-TIEKDII--------FGPVSMGVSKEEAKKRAAKY------IELVGldesylqrspfE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 142 LSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
268-449 |
1.11e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.40 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEV-----------VTHSPQDGlangivyisedr 336
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaraasrrVASVPQDT------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 337 krdGLVLGMSVKE--NMSLTA-LGYFSRAGgslkhKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTR 413
Cdd:PRK09536 87 ---SLSFEFDVRQvvEMGRTPhRSRFDTWT-----ETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 2070354550 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSII 449
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAV 193
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-218 |
1.20e-11 |
|
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: 62.47 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETtfngpkssqeagIGII 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK------------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQelnlipqltiaeniflgrefvnrfgkidwkkmyaeadqllaklnlrfksdklvgeLSiGDQQM-VEIAKVLSFESKVI 163
Cdd:cd03221 69 EQ-------------------------------------------------------LS-GGEKMrLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 164 IMDEPTDALtDTET-ESLfrvIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:cd03221 93 LLDEPTNHL-DLESiEAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
280-472 |
1.26e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.05 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 280 ILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHspqdglANGIvYISEDRKRDGLVLG-------MSVKENms 352
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDA------EKGI-CLPPEKRRIGYVFQdarlfphYKVRGN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 353 ltaLGYfsraggSLKHKDEQQaVGDFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKK 432
Cdd:PRK11144 97 ---LRY------GMAKSMVAQ-FDKIVALLGIE-PLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2070354550 433 EI--Y--QLINQFKadgLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:PRK11144 166 ELlpYleRLAREIN---IPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
396-463 |
1.29e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.06 E-value: 1.29e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADG-LSIILVSSEMPEVLGMSD 463
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSD 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-220 |
1.30e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngpkssqEAGIGIIHQELNLIPQ 93
Cdd:PLN03232 1246 PGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--------KFGLTDLRRVLSIIPQ 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 94 LTIaenIFLGrefVNRFgKIDWKKMYAEAD--QLLAKLNLR-------FKSDKLVGE----LSIGDQQMVEIAKVLSFES 160
Cdd:PLN03232 1318 SPV---LFSG---TVRF-NIDPFSEHNDADlwEALERAHIKdvidrnpFGLDAEVSEggenFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 161 KVIIMDEPTdALTDTETESLF-RVIRElKSQGRGIVYISHRMKEIFEiCDDVTVFRDGQFI 220
Cdd:PLN03232 1391 KILVLDEAT-ASVDVRTDSLIqRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-200 |
1.49e-11 |
|
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: 66.62 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwLGKETTFNGPKSSQEAGIGI 83
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT-LDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IHQELNLIPQlTIAENIFLGREFVNRfgkidwkkmyAEADQLLAKLNL----RFKSDKL---VGE----LSIGDQQMVEI 152
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRLARPDATD----------EELWAALERVGLadwlRALPDGLdtvLGEggarLSGGERQRLAL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2070354550 153 AKVLSFESKVIIMDEPTDALtDTETESlfRVIRELKS--QGRGIVYISHR 200
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHL-DAETAD--ELLEDLLAalSGRTVVLITHH 529
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
266-471 |
1.51e-11 |
|
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: 63.64 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHevVTHSPQDG-LANGIVyisedrkRDGLVLG 344
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQEPwIQNGTI-------RENILFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 MSVKENMSLTALgyfsRAGG------SLKHKDEQQaVGdfirlfnvktpsmEQAIGLlSGGNQQKVAIARGLMTRPKVLI 418
Cdd:cd03250 90 KPFDEERYEKVI----KACAlepdleILPDGDLTE-IG-------------EKGINL-SGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 419 LDEPTRGVDVGAKKEIYQ-LINQFKADGLSIILVSSEMpEVLGMSDRIIVMHEG 471
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
268-488 |
1.53e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.41 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLyGAM----PR--TSGYVTLDGHEVvtHSPQDGLAngivyisEDRKRDGL 341
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMndlnPEvtITGSIVYNGHNI--YSPRTDTV-------DLRKEIGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 342 VLG------MSVKENMSltalgYFSRAGGSlkhKDEQ---QAVGDFIRLFN----VKTPSMEQAIGLlSGGNQQKVAIAR 408
Cdd:PRK14239 91 VFQqpnpfpMSIYENVV-----YGLRLKGI---KDKQvldEAVEKSLKGASiwdeVKDRLHDSALGL-SGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADgLSIILVSSEMPEVLGMSDRIIVMheghLSGEFTREQATQEVLM 488
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFF----LDGDLIEYNDTKQMFM 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-221 |
1.57e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.14 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwLGKETTFNGPKSSQ----EAGIGIIHQ--ELNLI 91
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT-VGDIVVSSTSKQKEikpvRKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 92 PQLTIAENIFLGREFvnRFGKIDWKKMYAEADQLLAkLNLRFkSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDA 171
Cdd:PRK13643 99 EETVLKDVAFGPQNF--GIPKEKAEKIAAEKLEMVG-LADEF-WEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2070354550 172 LTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIA 221
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
396-476 |
1.62e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.61 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSG 475
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
.
gi 2070354550 476 E 476
Cdd:PRK10619 233 E 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-172 |
1.79e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.34 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAF-PG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfNGPKSSQEA 79
Cdd:COG1101 2 LELKNLSKTFnPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-KLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 80 GIGIIHQE--LNLIPQLTIAENIFL----GREFVNRFGKIdwKKMYAEADQLLAKLNLRFKsDKL---VGELSIGDQQ-- 148
Cdd:COG1101 81 YIGRVFQDpmMGTAPSMTIEENLALayrrGKRRGLRRGLT--KKRRELFRELLATLGLGLE-NRLdtkVGLLSGGQRQal 157
|
170 180
....*....|....*....|....*..
gi 2070354550 149 ---MVEIAKvlsfeSKVIIMDEPTDAL 172
Cdd:COG1101 158 sllMATLTK-----PKLLLLDEHTAAL 179
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-222 |
1.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.80 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwLGKETTFNGPKSSQ----EAGIGIIHQ--ELNLI 91
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVT-VDDITITHKTKDKYirpvRKRIGMVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 92 PQLTIAENIFLGREFvnrfgKIDWKKMYAEADQLLakLNLRFKSDKLVG---ELSIGDQQMVEIAKVLSFESKVIIMDEP 168
Cdd:PRK13646 100 EDTVEREIIFGPKNF-----KMNLDEVKNYAHRLL--MDLGFSRDVMSQspfQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 169 TDALTDTETESLFRVIRELK-SQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE 222
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-222 |
1.83e-11 |
|
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: 63.31 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI--YTRDAGSLLWLGKETTFNGPKSSQEAGIGIIHQELNLIPQ 93
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 94 LTIAEniFLgrEFVNrfgkidwkkmyaeadqllaklnlrfksdklVGeLSIGDQQMVEIAKVLSFESKVIIMDEPTDALT 173
Cdd:cd03217 92 VKNAD--FL--RYVN------------------------------EG-FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 174 DTETESLFRVIRELKSQGRGIVYISHRmKEIFE--ICDDVTVFRDGQFIAE 222
Cdd:cd03217 137 IDALRLVAEVINKLREEGKSVLIITHY-QRLLDyiKPDRVHVLYDGRIVKS 186
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-234 |
2.00e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.21 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIyTRDAGS------------LLWLGKET-----------TFNGP 73
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRvtadrmrfddidLLRLSPRErrklvghnvsmIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 74 KSSQEAGIGIIHQELNLIPQLTiaeniFLGReFVNRFGkidWKKMyaEADQLLAKLNLRFKSDKLVG---ELSIGDQQMV 150
Cdd:PRK15093 99 QSCLDPSERVGRQLMQNIPGWT-----YKGR-WWQRFG---WRKR--RAIELLHRVGIKDHKDAMRSfpyELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQfiaerEVATLT 229
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQ-----TVETAP 242
|
....*
gi 2070354550 230 EDSLI 234
Cdd:PRK15093 243 SKELV 247
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
265-477 |
2.04e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.14 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 265 GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdGLAN--GIVYisedrkRDGLV 342
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA-SLRRniAVVF------QDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LGMSVKENMSLtalgyfSRAGGS---LKHKDEQQAVGDFI--RLFNVKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVL 417
Cdd:PRK13657 421 FNRSIEDNIRV------GRPDATdeeMRAAAERAQAHDFIerKPDGYDTVVGERG-RQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 418 ILDEPTRGVDVGAKKEIYQLINQFK--------ADGLSIIlvssempevlGMSDRIIVMHEGHL--SGEF 477
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELMkgrttfiiAHRLSTV----------RNADRILVFDNGRVveSGSF 553
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-220 |
2.39e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.72 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKEttfngP-KSSQE--AGIGIIH-QELNLIP 92
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PfKRRKEfaRRIGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 93 QLTIAENIFLGREfVNRFGKIDWKKMYAEADQLlakLNLRFKSDKLVGELSIGdQQM-VEIAKVLSFESKVIIMDEPT-- 169
Cdd:COG4586 110 DLPAIDSFRLLKA-IYRIPDAEYKKRLDELVEL---LDLGELLDTPVRQLSLG-QRMrCELAAALLHRPKILFLDEPTig 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 170 -DALTDtetESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:COG4586 185 lDVVSK---EAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
266-486 |
2.98e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.85 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLAN--GIVYISEDRKrdglVL 343
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlvGIVFQNPETQ----FV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 GMSVKE-------NMSLTALGYFSRAGGSLKHKDEQQavgdfirlFNVKTPSMeqaiglLSGGNQQKVAIARGLMTRPKV 416
Cdd:PRK13644 92 GRTVEEdlafgpeNLCLPPIEIRKRVDRALAEIGLEK--------YRHRSPKT------LSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 417 LILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEvLGMSDRIIVMHEGHLSGEFTREQATQEV 486
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
257-473 |
3.20e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.57 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 257 RLKVDNLC----GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMP----RTSGYVTLDGHEVvthSPQDGLANG 328
Cdd:PRK10418 4 QIELRNIAlqaaQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPV---APCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 329 IVYISED-RKRDGLVLGMSVKENMSLTALGyfsraggslKHKDEQQAVGdfiRLFNVKTPSMEQAIGL----LSGGNQQK 403
Cdd:PRK10418 81 IATIMQNpRSAFNPLHTMHTHARETCLALG---------KPADDATLTA---ALEAVGLENAARVLKLypfeMSGGMLQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 404 VAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
268-452 |
3.48e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 61.79 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVtldghevvtHSPQDglaNGIVYISEdrkrdglvlgmsv 347
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEG---EDLLFLPQ------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 kenmsltaLGYFSRagGSLKhkdEQqavgdfirlfnVKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:cd03223 72 --------RPYLPL--GTLR---EQ-----------LIYPWDDV----LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*
gi 2070354550 428 VGAKKEIYQLINQfkadgLSIILVS 452
Cdd:cd03223 124 EESEDRLYQLLKE-----LGITVIS 143
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
268-490 |
3.50e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.51 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEI--------------LGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdGLANGIVYIS 333
Cdd:PRK10790 343 IDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-VLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 334 ED------RKRDGLVLGMSVKENMSLTALgyfsraggslkhkdEQQAVGDFIRLF--NVKTPSMEQAiGLLSGGNQQKVA 405
Cdd:PRK10790 422 QDpvvladTFLANVTLGRDISEEQVWQAL--------------ETVQLAELARSLpdGLYTPLGEQG-NNLSVGQKQLLA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK--------ADGLSIILvssempevlgMSDRIIVMHEGHlsgef 477
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRehttlvviAHRLSTIV----------EADTILVLHRGQ----- 551
|
250
....*....|...
gi 2070354550 478 TREQATQEVLMAA 490
Cdd:PRK10790 552 AVEQGTHQQLLAA 564
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
271-500 |
3.64e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.60 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 271 VSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLANGIVYISEDRkrDGLVLGMSVKE- 349
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NAENEKWVRSKVGLVFQDP--DDQVFSSTVWDd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 350 ------NMSLTALGYFSRAGGSLKhkdeqqAVGdfIRLFNVKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPT 423
Cdd:PRK13647 101 vafgpvNMGLDKDEVERRVEEALK------AVR--MWDFRDKPPYH------LSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 424 RGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEVLMAAAVGKLNRVNQ 500
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGLRLPLVAQ 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
267-471 |
3.99e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.87 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 267 GVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMprtsgyVTLDGHEVVTHSPQDGLANGIVYISEDRKRDGLVLGMS 346
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI------ISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 347 VKENMSLTALGYFSRAGGSLKHKDEQ--QAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
Cdd:PRK13645 100 EYQLFQETIEKDIAFGPVNLGENKQEayKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2070354550 425 GVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK13645 180 GLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEG 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-220 |
4.24e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 62.43 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngpkssqEAGIGIIHQELNLIPQLTIa 97
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS--------TIPLEDLRSSLTIIPQDPT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 98 enIFLG--REFVNRFGKIDWKKMYAEadqllaklnLRFKSDKLvgELSIGDQQMVEIAKVLSFESKVIIMDEPTdALTDT 175
Cdd:cd03369 93 --LFSGtiRSNLDPFDEYSDEEIYGA---------LRVSEGGL--NLSQGQRQLLCLARALLKRPRVLVLDEAT-ASIDY 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2070354550 176 ETESLF-RVIRELkSQGRGIVYISHRMKEIFEiCDDVTVFRDGQFI 220
Cdd:cd03369 159 ATDALIqKTIREE-FTNSTILTIAHRLRTIID-YDKILVMDAGEVK 202
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
268-473 |
4.51e-11 |
|
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: 62.16 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGaMPR---TSGYVTLDGHEVVTHSPqdglangivyisEDRKRDGLVLG 344
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKyevTEGEILFKGEDITDLPP------------EERARLGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 MSVKENMSltalgyfsraggSLKhkdeqqaVGDFIRLFNVKtpsmeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
Cdd:cd03217 83 FQYPPEIP------------GVK-------NADFLRYVNEG----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 425 GVDVGAKKEIYQLINQFKADGLSIILVsSEMPEVLGM--SDRIIVMHEGHL 473
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLII-THYQRLLDYikPDRVHVLYDGRI 183
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-471 |
4.60e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.19 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGS--------LLWLGKETtfngPKSSQEAGIGII---HQEL 88
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgnwqLAWVNQET----PALPQPALEYVIdgdREYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 89 NLIPQLTIAENIFLGREFVNRFGKID----WkKMYAEADQLLAKLNlrFKSDKL---VGELSIGDQQMVEIAKVLSFESK 161
Cdd:PRK10636 93 QLEAQLHDANERNDGHAIATIHGKLDaidaW-TIRSRAASLLHGLG--FSNEQLerpVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 162 VIIMDEPTDALtdtETESLFRVIRELKSQGRGIVYISH---------------RMKEIFEICDDVTVF------RDGQFI 220
Cdd:PRK10636 170 LLLLDEPTNHL---DLDAVIWLEKWLKSYQGTLILISHdrdfldpivdkiihiEQQSLFEYTGNYSSFevqratRLAQQQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 221 A-----EREVATLTE---------------DSLIEMMvgRKLEDQYP-HLDN-------APGEIR---LKVDNL-CGPG- 267
Cdd:PRK10636 247 AmyesqQERVAHLQSyidrfrakatkakqaQSRIKML--ERMELIAPaHVDNpfhfsfrAPESLPnplLKMEKVsAGYGd 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 ---VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVtldghevvthspqdGLANGIvyisedrkrdglvlg 344
Cdd:PRK10636 325 riiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------------GLAKGI--------------- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 msvkenmsltALGYFS-------RAGGS-LKH------KDEQQAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGL 410
Cdd:PRK10636 376 ----------KLGYFAqhqleflRADESpLQHlarlapQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIV 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFkaDGlSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLLRSTTDDLYLVHDG 503
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
270-456 |
4.62e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEvvthSPQDGLANGIVYISEdrkRDGLVLGMSVKE 349
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----IDDPDVAEACHYLGH---RNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 350 NMSltalgyFSRA--GGSLKHKDEQQAVGDFIRLFNVKtpsmeqaIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:PRK13539 93 NLE------FWAAflGGEELDIAAALEAVGLAPLAHLP-------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*....
gi 2070354550 428 VGAKKEIYQLINQFKADGlSIILVSSEMP 456
Cdd:PRK13539 160 AAAVALFAELIRAHLAQG-GIVIAATHIP 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
268-481 |
4.95e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.58 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGY-----VTLDGHEVVTHSPqdglangivyISEDRKRDGLV 342
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRD----------VLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LG------MSVKENMsLTALgyfsRAGGSLKHKDEQ---QAVGDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTR 413
Cdd:PRK14271 107 FQrpnpfpMSIMDNV-LAGV----RAHKLVPRKEFRgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 414 PKVLILDEPTRGVDVGAKKEIYQLINQFkADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
280-487 |
5.96e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 62.62 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 280 ILGISGLMGAGRTELMKV------LYGAmPRTSGYVTLDGHEVVTHSpqdglangivyISEDRKRDGLVL-------GMS 346
Cdd:PRK14247 31 ITALMGPSGSGKSTLLRVfnrlieLYPE-ARVSGEVYLDGQDIFKMD-----------VIELRRRVQMVFqipnpipNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 347 VKENMsltALGY-FSRAGGSLKHKDE--QQAVgDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
Cdd:PRK14247 99 IFENV---ALGLkLNRLVKSKKELQErvRWAL-EKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 424 RGVDVGAKKEIYQLINQFKADgLSIILVSSEMPEVLGMSDRIIVMHEGHLsgefTREQATQEVL 487
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQI----VEWGPTREVF 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
273-474 |
6.20e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 273 FVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLAN--GIV--YISEDRKRDGLVL----G 344
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNveGTVydFVAEGIEEQAEYLkryhD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 MS--VKENMSLTALGYFSRAGGSLKHKDEQQavgdfirlFNVKTPSMEQAIGL--------LSGGNQQKVAIARGLMTRP 414
Cdd:PRK11147 104 IShlVETDPSEKNLNELAKLQEQLDHHNLWQ--------LENRINEVLAQLGLdpdaalssLSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAdglSIILVSSEMPEVLGMSDRIIVMHEGHLS 474
Cdd:PRK11147 176 DVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-222 |
6.64e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwLGKETTFNGPKSsqEAGIG 82
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLF-IGEKRMNDVPPA--ERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 IIHQELNLIPQLTIAENIFLGRefvnRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKV 162
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGL----KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 163 IIMDEPTDALtDTETESLFRV-IREL-KSQGRGIVYISHRMKEIFEICDDVTVFrDGQFIAE 222
Cdd:PRK11000 155 FLLDEPLSNL-DAALRVQMRIeISRLhKRLGRTMIYVTHDQVEAMTLADKIVVL-DAGRVAQ 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
253-473 |
8.87e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 61.27 E-value: 8.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 253 PGEIRLKVDNLC-------GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGL 325
Cdd:cd03369 2 PEHGEIEVENLSvryapdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-STIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 326 ANGIVYISEDRkrdgLVLGMSVKENmsLTALGYFSraggslkhkDEQqavgdfirLFNVKTPSMEqaiGL-LSGGNQQKV 404
Cdd:cd03369 81 RSSLTIIPQDP----TLFSGTIRSN--LDPFDEYS---------DEE--------IYGALRVSEG---GLnLSQGQRQLL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADglSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTN--STILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
396-471 |
9.41e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.07 E-value: 9.41e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
266-489 |
9.84e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 64.36 E-value: 9.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVV--THspqdglangiVYIsedRKRDGLV- 342
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqyDH----------HYL---HRQVALVg 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 -----LGMSVKENmsltaLGYfsraGGSLKHKDEQQAVG------DFIRLFnvkTPSMEQAIG----LLSGGNQQKVAIA 407
Cdd:TIGR00958 562 qepvlFSGSVREN-----IAY----GLTDTPDEEIMAAAkaanahDFIMEF---PNGYDTEVGekgsQLSGGQKQRIAIA 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQfkaDGLSIILVSSEMPEVlGMSDRIIVMHEGHLsgeftREQATQEVL 487
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTV-ERADQILVLKKGSV-----VEMGTHKQL 700
|
..
gi 2070354550 488 MA 489
Cdd:TIGR00958 701 ME 702
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-288 |
1.03e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.22 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMmKVLTGIYTRDAGSLLWlgKETTFNGPKSSQEAGIGIi 84
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPW--RF*TWCANRRALRRTIG*- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQelnliPQLTIAENIFLGRE---FVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESK 161
Cdd:NF000106 90 HR-----PVR*GRRESFSGREnlyMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVatlteDSLIEMMVGRK 241
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV-----DELKTKVGGRT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 242 LEDQYPH---LDNAPGEI-RLKVDNLCGP------GVNDVSFVLRKgEILGISGLMG 288
Cdd:NF000106 240 LQIRPAHaaeLDRMVGAIaQAGLDGIAGAtadhedGVVNVPIVSDE-QLSAVVGMLG 295
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-220 |
1.07e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.51 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 23 AALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEA---GIGIIHQELNLIPQLTIAEN 99
Cdd:PRK10070 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkKIAMVFQSFALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 100 IFLGREFVNrfgkIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTD-TETE 178
Cdd:PRK10070 127 TAFGMELAG----INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2070354550 179 SLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
258-470 |
1.14e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 61.34 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLC-----GPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMP---RTSGYVTLDGHEVVTHSPQdglANGI 329
Cdd:COG4136 2 LSLENLTitlggRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPAE---QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 330 VYISEDrkrDGLVLGMSVKENMsltALGYFSRAGGSLKHKDEQQAvgdfirLFNVKTPSMEQA-IGLLSGGNQQKVAIAR 408
Cdd:COG4136 79 GILFQD---DLLFPHLSVGENL---AFALPPTIGRAQRRARVEQA------LEEAGLAGFADRdPATLSGGQRARVALLR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKADGLSIILVSSEMPEVLGMSdRIIVMHE 470
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
249-489 |
1.20e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.88 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 249 LDNAPGEIRLKVDNLCGPG-----VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHE-------- 315
Cdd:PRK11176 335 IERAKGDIEFRNVTFTYPGkevpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDlrdytlas 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 316 ------VVT---HSPQDGLANGIVYISEDRkrdglvlgmsvkenmsltalgyFSRAggSLKHKDEQQAVGDFIRlfnvkt 386
Cdd:PRK11176 415 lrnqvaLVSqnvHLFNDTIANNIAYARTEQ----------------------YSRE--QIEEAARMAYAMDFIN------ 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 387 pSMEQ----AIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSiiLVSSEMPEV 458
Cdd:PRK11176 465 -KMDNgldtVIGengvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS--LVIAHRLST 541
|
250 260 270
....*....|....*....|....*....|.
gi 2070354550 459 LGMSDRIIVMHEGHLsgeftREQATQEVLMA 489
Cdd:PRK11176 542 IEKADEILVVEDGEI-----VERGTHAELLA 567
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-428 |
1.24e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 6 QLKGIDKAFPGVKA-LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIytrdagsllwlgkETTFNG-PKSSQEAGIGI 83
Cdd:PRK11819 8 TMNRVSKVVPPKKQiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-------------DKEFEGeARPAPGIKVGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 84 IHQELNLIPQLTIAENIFLG----REFVNRFGKI---------DWKKMYAEADQLLAKLN-----------------LRF 133
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVEEGvaevKAALDRFNEIyaayaepdaDFDALAAEQGELQEIIDaadawdldsqleiamdaLRC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 134 KS-DKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTETES----------------------LFRV---IREL 187
Cdd:PRK11819 155 PPwDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHL-DAESVAwleqflhdypgtvvavthdryfLDNVagwILEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 188 kSQGRGIVY---------------------ISHRMKEIfeicddvtvfrdgqfiaEREV---------------ATLTEd 231
Cdd:PRK11819 234 -DRGRGIPWegnysswleqkakrlaqeekqEAARQKAL-----------------KRELewvrqspkarqakskARLAR- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 232 slIEMMVG----RKLEDQYPHLDNAP--GEIRLKVDNLC-GPG----VNDVSFVLRKGEILGISGLMGAGRTELMKVLYG 300
Cdd:PRK11819 295 --YEELLSeeyqKRNETNEIFIPPGPrlGDKVIEAENLSkSFGdrllIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 301 AMPRTSGYVTLdGHEVVthspqdglangIVYIseDRKRDGLVLGMSVKENMS----LTALGYF---SRAggslkhkdeqq 373
Cdd:PRK11819 373 QEQPDSGTIKI-GETVK-----------LAYV--DQSRDALDPNKTVWEEISggldIIKVGNReipSRA----------- 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2070354550 374 avgdFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
Cdd:PRK11819 428 ----YVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
396-481 |
1.40e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 62.62 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI---NQFKadGLSIILVSSEMPEVLGMSDRIIVMHEGH 472
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLarlNQLQ--GTSILLISHDLESISQWADTITVLYCGQ 236
|
90
....*....|.
gi 2070354550 473 L--SGefTREQ 481
Cdd:COG4170 237 TveSG--PTEQ 245
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
256-454 |
1.66e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 256 IRLKVDNLCGPGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEV----VTHSPQdglangIVY 331
Cdd:PRK13540 5 IELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlCTYQKQ------LCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 332 ISEdrkRDGLVLGMSVKENMsltalgYFSraggsLKHKDEQQAVGDFIRLFNVKTpSMEQAIGLLSGGNQQKVAIARGLM 411
Cdd:PRK13540 79 VGH---RSGINPYLTLRENC------LYD-----IHFSPGAVGITELCRLFSLEH-LIDYPCGLLSSGQKRQVALLRLWM 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2070354550 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSE 454
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-200 |
1.91e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKetTFNGPKSSQEAGIGIIHQELNLIPQLTIAEN 99
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ--SIKKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 100 IFLgrefvnrfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETES 179
Cdd:PRK13540 95 CLY---------DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|.
gi 2070354550 180 LFRVIRELKSQGRGIVYISHR 200
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
270-450 |
2.04e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSP---QD----GLANGIvyisedrKRDglv 342
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyhQDllylGHQPGI-------KTE--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 lgMSVKENmsltaLGYFSRAGGSLKHKDEQQAVgdfirlfnvktpsmeQAIGL----------LSGGNQQKVAIARGLMT 412
Cdd:PRK13538 89 --LTALEN-----LRFYQRLHGPGDDEALWEAL---------------AQVGLagfedvpvrqLSAGQQRRVALARLWLT 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 2070354550 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIIL 450
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVIL 184
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-220 |
2.24e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.60 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQ-EAGIGIIHQ--ELNLIPQl 94
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDiRKKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 95 TIAENIFLGREFVNrFGKIDWKKMYAEADQLLaKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTD 174
Cdd:PRK13637 100 TIEKDIAFGPINLG-LSEEEIENRVKRAMNIV-GLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2070354550 175 TETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:PRK13637 178 KGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-223 |
2.33e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.81 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKettfngPKSSQ-----EAGIGIIHQELNLIPQl 94
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR------PLSSLshsvlRQGVAMVQQDPVVLAD- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 95 TIAENIFLGREfvnrfgkIDWKKMYA--EADQlLAKLnLRFKSDKL---VGE----LSIGDQQMVEIAKVLSFESKVIIM 165
Cdd:PRK10790 430 TFLANVTLGRD-------ISEEQVWQalETVQ-LAEL-ARSLPDGLytpLGEqgnnLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 166 DEPT---DALTDTETESLFRVIRELKSqgrgIVYISHRMKEIFEiCDDVTVFRDGQfIAER 223
Cdd:PRK10790 501 DEATaniDSGTEQAIQQALAAVREHTT----LVVIAHRLSTIVE-ADTILVLHRGQ-AVEQ 555
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
268-473 |
2.36e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.64 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYV-----------TLDGHEVVTHSP--QDGLANGIVYISE 334
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTKEKEKVLEKLviQKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 335 DRKRDGLVLGM--------SVKENMSLTALGYfsragGSLKHKDEQQAVgDFIRLFNVKTPSMEQAIGLLSGGNQQKVAI 406
Cdd:PRK13651 103 IRRRVGVVFQFaeyqlfeqTIEKDIIFGPVSM-----GVSKEEAKKRAA-KYIELVGLDESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 407 ARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-223 |
2.77e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 62.53 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwlgkettFNG------PKSSQEAGIGIIHQElnliPQ 93
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIL-------IDGqdirdvTQASLRAAIGIVPQD----TV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 94 L---TIAENIflgrefvnRFGKIDwkkmyAEADQL-----LAKLnLRF------KSDKLVGE----LSIGDQQMVEIAKV 155
Cdd:COG5265 443 LfndTIAYNI--------AYGRPD-----ASEEEVeaaarAAQI-HDFieslpdGYDTRVGErglkLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 156 LSFESKVIIMDEPTDALtDTETESlfRVIRELK--SQGRGIVYISHRMKEIFEiCDDVTVFRDGQfIAER 223
Cdd:COG5265 509 LLKNPPILIFDEATSAL-DSRTER--AIQAALRevARGRTTLVIAHRLSTIVD-ADEILVLEAGR-IVER 573
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
258-488 |
2.88e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.80 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNL-CGPG----VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLANGIVYI 332
Cdd:PRK11231 3 LRTENLtVGYGtkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 333 SEdrkrdglVL----GMSVKEnmsLTALG---YFSrAGGSLKHKDEQQAvgdfirlfnvkTPSMEQ---------AIGLL 396
Cdd:PRK11231 82 PQ-------HHltpeGITVRE---LVAYGrspWLS-LWGRLSAEDNARV-----------NQAMEQtrinhladrRLTDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGE 476
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
250
....*....|..
gi 2070354550 477 FTREQATQEVLM 488
Cdd:PRK11231 220 GTPEEVMTPGLL 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
278-492 |
3.15e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 278 GEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdGLANGIVYISEDRKRdglVLGMSVKEnmsLTALG 357
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQQLPA---AEGMTVRE---LVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 358 YFSRAG--GSLKHKDEQQaVGDFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIY 435
Cdd:PRK10575 110 RYPWHGalGRFGAADREK-VEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 436 QLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHLSGeftreQATQEVLMAAAV 492
Cdd:PRK10575 188 ALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIA-----QGTPAELMRGET 240
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-222 |
3.64e-10 |
|
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: 59.81 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAgIGIIHQElnliPQL---T 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR-ISIIPQD----PVLfsgT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 96 IAENIflgrefvNRFGKID----WK-----KMYAEADQLLAKLNLRFKSDKLVgeLSIGDQQMVEIAKVLSFESKVIIMD 166
Cdd:cd03244 94 IRSNL-------DPFGEYSdeelWQalervGLKEFVESLPGGLDTVVEEGGEN--LSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 167 EPTDALtDTETESL-FRVIRElKSQGRGIVYISHRMKEIFEiCDDVTVFRDGQfIAE 222
Cdd:cd03244 165 EATASV-DPETDALiQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGR-VVE 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
395-452 |
3.68e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.13 E-value: 3.68e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADglsIILVS 452
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG---TTVIS 539
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-211 |
3.85e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.73 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 2 DALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQeagi 81
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 giihQELNLIPQL------TIAENIFLGREFvnRFGKIDWKKMYAEADQLLAKLNLRfksDKLVGELSIGDQQMVEIAKV 155
Cdd:PRK10247 81 ----QQVSYCAQTptlfgdTVYDNLIFPWQI--RNQQPDPAIFLDDLERFALPDTIL---TKNIAELSGGEKQRISLIRN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 156 LSFESKVIIMDEPTDALTDTETESLFRVI-RELKSQGRGIVYISHRMKEIFEiCDDV 211
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIhRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
269-452 |
3.94e-10 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 57.84 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVthspqdglangivyisedrkrdglvlgmsvk 348
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKI------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 349 enmsltalGYFsraggslkhkdeqqavgdfirlfnvktpsmEQaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
Cdd:cd03221 66 --------GYF------------------------------EQ----LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180
....*....|....*....|....
gi 2070354550 429 GAKKEIYQLINQFKAdglSIILVS 452
Cdd:cd03221 104 ESIEALEEALKEYPG---TVILVS 124
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
267-473 |
4.21e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.59 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 267 GVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDglangivYISEDRKRDGLVL-GM 345
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAE-------LREVRRKKIAMVFqSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLTALGYFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
Cdd:PRK10070 116 ALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2070354550 426 VDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-214 |
6.86e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.80 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYT-----RDAGSLLWLGKEttFNGPK---SSQEAGIGIIHQELNL 90
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKN--LYAPDvdpVEVRRRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 91 IPQlTIAENIFLGREFVNRFGKID-----WKKMYAEADQLLAKLNLRFKSdklvgeLSIGDQQMVEIAKVLSFESKVIIM 165
Cdd:PRK14243 103 FPK-SIYDNIAYGARINGYKGDMDelverSLRQAALWDEVKDKLKQSGLS------LSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2070354550 166 DEPTDALTDTETESLFRVIRELKSQgRGIVYISHRMKEIFEICDDVTVF 214
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFF 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
270-481 |
8.54e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.39 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVThspqdgLANGIVYisEDRKRdglvLGMSVKE 349
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPA------MSRSRLY--TVRKR----MSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 350 NMSLTALGYFSRAGGSLKhkDEQQAVGDFIRlfnvKTPSME-QAIGL----------LSGGNQQKVAIARGLMTRPKVLI 418
Cdd:PRK11831 93 GALFTDMNVFDNVAYPLR--EHTQLPAPLLH----STVMMKlEAVGLrgaaklmpseLSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 419 LDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-218 |
8.60e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.75 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQEAgIGIIHQEL-NLIPQLTIAE 98
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-IGMVFQNPdNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 99 NIFLGREfvNRfgKIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
Cdd:PRK13650 102 DVAFGLE--NK--GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2070354550 179 SLFRVIRELKSQ-GRGIVYISHRMKEIfEICDDVTVFRDGQ 218
Cdd:PRK13650 178 ELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
266-490 |
9.74e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 60.99 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGL--ANGIVyisedrKRDGLVL 343
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQASLraAIGIV------PQDTVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 GMSVKENmsltaLGYfSRAGGSlkhKDEQQAV------GDFIRlfnvktpSMEQAI-------GL-LSGGNQQKVAIARG 409
Cdd:COG5265 445 NDTIAYN-----IAY-GRPDAS---EEEVEAAaraaqiHDFIE-------SLPDGYdtrvgerGLkLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIIL-------VSsempevlgmSDRIIVMHEGHLSgeftrEQA 482
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIahrlstiVD---------ADEILVLEAGRIV-----ERG 574
|
....*...
gi 2070354550 483 TQEVLMAA 490
Cdd:COG5265 575 THAELLAQ 582
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-220 |
1.05e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 2 DALLQLKGIDKAFP-----------GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGK--ET 68
Cdd:PRK10261 311 EPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 69 TFNGPKSSQEAGIGIIHQE--LNLIPQLTIAENIFlgrEFVNRFGKIDWKKMYAEADQLLAKLNLRFKSD-KLVGELSIG 145
Cdd:PRK10261 391 LSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSIM---EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGG 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 146 DQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-177 |
1.19e-09 |
|
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: 60.72 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 2 DALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwLGkETTfngpkssqeaGI 81
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IG-ETV----------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GIIHQEL-NLIPQLTIAENIFLG-------------REFVNRFGkidwkkmYAEADQllaklnlrfksDKLVGELSIGDQ 147
Cdd:TIGR03719 388 AYVDQSRdALDPNKTVWEEISGGldiiklgkreipsRAYVGRFN-------FKGSDQ-----------QKKVGQLSGGER 449
|
170 180 190
....*....|....*....|....*....|
gi 2070354550 148 QMVEIAKVLSFESKVIIMDEPTDALtDTET 177
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDL-DVET 478
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-225 |
1.25e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.33 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKET--TFNGPKSSQEAGIgIIHQELNLIPQLTI 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENLWDIRNKAGM-VFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 97 AENIFLGREFVNrfgkIDWKKMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTE 176
Cdd:PRK13633 104 EEDVAFGPENLG----IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 177 TESLFRVIREL-KSQGRGIVYISHRMKEIFEiCDDVTVFRDGQFIAE---REV 225
Cdd:PRK13633 180 RREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEgtpKEI 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-220 |
1.27e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.04 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 12 KAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI---YTRDAGSLLWLGKEttFNGPKSSQEAGIGIIHQEL 88
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIP--YKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 89 NLIPQLTIAENIflgrEFVnrfgkidwkkmyaeadqllaklnLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEP 168
Cdd:cd03233 93 VHFPTLTVRETL----DFA-----------------------LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 169 TDALTDTETESLFRVIRELKSQGRG--IVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTttFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
266-471 |
1.30e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 58.11 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLANGIVYISEDRKRDGLvLGM 345
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL-LNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLtalgyfsragGSLKHKDEQQAVGDFIRL--------FNVKTPSMEQAIGLlSGGNQQKVAIARGLMTRPKVL 417
Cdd:cd03290 94 TVEENITF----------GSPFNKQRYKAVTDACSLqpdidllpFGDQTEIGERGINL-SGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 418 ILDEPTRGVDVGAKKEIYQ--LINQFKADGLSIILVSSEMpEVLGMSDRIIVMHEG 471
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-231 |
1.39e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.24 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 29 PGRVMALVGENGAGKSTMMKVLTGI--YTrdaGSLLWLGKETTFNGPKSSQEAgIGIIHQElnliPQL---TIAENIFLG 103
Cdd:PRK11174 375 AGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGIELRELDPESWRKH-LSWVGQN----PQLphgTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 104 REFVNRfGKIDWKKMYAEADQLLAKLNLRFksDKLVGE----LSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTETES 179
Cdd:PRK11174 447 NPDASD-EQLQQALENAWVSEFLPLLPQGL--DTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASL-DAHSEQ 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 180 lfRVIRELK--SQGRGIVYISHRMKEIFEiCDDVTVFRDGQFIAEREVATLTED 231
Cdd:PRK11174 523 --LVMQALNaaSRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQA 573
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-218 |
1.50e-09 |
|
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: 57.86 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 11 DKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLlwlgketTFNGPKS--SQEAGIgiihqeL 88
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------SVPGSIAyvSQEPWI------Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 89 NlipqLTIAENIFLGREFvnrfgKIDWKKMYAEADQLLAKLNLRFKSDK-LVGE----LSIGDQQMVEIAKVLSFESKVI 163
Cdd:cd03250 79 N----GTIRENILFGKPF-----DEERYEKVIKACALEPDLEILPDGDLtEIGEkginLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 164 IMDEPTDALtDTETES-LF-RVIRELKSQGRGIVYISHRMkEIFEICDDVTVFRDGQ 218
Cdd:cd03250 150 LLDDPLSAV-DAHVGRhIFeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
270-498 |
1.79e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.74 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQdglaNGIVYISEDRKRDGL--VLGMSV 347
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK----NLVAYVPQSEEVDWSfpVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMSLTALGYFSRAggslKHKDEQQAVGDFIRLFNVKTpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:PRK15056 101 VMMGRYGHMGWLRRA----KKRDRQIVTAALARVDMVEF--RHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 428 VGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEVLMAAAVGKLNRV 498
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFSGVLRHV 245
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
396-489 |
2.12e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSG 475
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
90
....*....|....
gi 2070354550 476 EFTREQATQEVLMA 489
Cdd:PRK10938 216 TGEREEILQQALVA 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
257-495 |
2.27e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.07 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 257 RLKVDNLC-GPG----VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLANGIVY 331
Cdd:PRK10253 7 RLRGEQLTlGYGkytvAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 332 ISEDRKRDGlvlGMSVKEnmsLTALG------YFSRAggslkHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVA 405
Cdd:PRK10253 86 LAQNATTPG---DITVQE---LVARGryphqpLFTRW-----RKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEghlsGEFTREQATQ 484
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALRE----GKIVAQGAPK 229
|
250
....*....|.
gi 2070354550 485 EVLMAAAVGKL 495
Cdd:PRK10253 230 EIVTAELIERI 240
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
396-473 |
3.02e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 3.02e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-218 |
3.89e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGiytRDAGSLLwLGKETTFNGPKSSQEAG-IGIIHQELNLIPQLTIAE 98
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAG---RIQGNNF-TGTILANNRKPTKQILKrTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 99 N-IFLGREFVNRFGKIDWKKMYAEAdqLLAKLNLRFKSDKLVGE-----LSIGDQQMVEIAKVLSFESKVIIMDEPTDAL 172
Cdd:PLN03211 160 TlVFCSLLRLPKSLTKQEKILVAES--VISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2070354550 173 TDTETESLFRVIRELKSQGRGIVYISHR-MKEIFEICDDVTVFRDGQ 218
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
271-476 |
4.65e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.71 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 271 VSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVvTHSPQDGLAN------GIVYISEdrkrdGLVLG 344
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL-HQMDEEARAKlrakhvGFVFQSF-----MLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 MSVKENMSLTALgyfsraggsLKHKDEQQAVGDFIRLfnvktpsMEQaIGL----------LSGGNQQKVAIARGLMTRP 414
Cdd:PRK10584 103 LNALENVELPAL---------LRGESSRQSRNGAKAL-------LEQ-LGLgkrldhlpaqLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEmPEVLGMSDRIIVMHEGHLSGE 476
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQEE 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-200 |
4.87e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNgpkssqeagigiihQELNLIPQLTIAEN 99
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG--------------REASLIDAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 100 IFLGREFVNRFGkidwkkmYAEADQLLAKlnlrfksdklVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTETES 179
Cdd:COG2401 112 FKDAVELLNAVG-------LSDAVLWLRR----------FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL-DRQTAK 173
|
170 180
....*....|....*....|...
gi 2070354550 180 L--FRVIRELKSQGRGIVYISHR 200
Cdd:COG2401 174 RvaRNLQKLARRAGITLVVATHH 196
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
390-473 |
5.81e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.94 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 390 EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMH 469
Cdd:PRK13638 131 HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLR 210
|
....
gi 2070354550 470 EGHL 473
Cdd:PRK13638 211 QGQI 214
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-239 |
6.23e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.14 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTrdaGSLLWLGK----ETTFNGpkssqEAGIGIIHQEL----NLI 91
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGArvtgDVTLNG-----EPLAAIDAPRLarlrAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 92 PQ-------LTIAENIFLGR--------EFVNRFGKIDWKKM-YAEADQLLAKlnlrfksDklVGELSIGDQQMVEIAKV 155
Cdd:PRK13547 89 PQaaqpafaFSAREIVLLGRypharragALTHRDGEIAWQALaLAGATALVGR-------D--VTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 156 LS---------FESKVIIMDEPTDALTDTETESLFRVIRELKSQGR-GIVYISHRMKEIFEICDDVTVFRDGQFIAEREV 225
Cdd:PRK13547 160 LAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
250
....*....|....
gi 2070354550 226 ATLTEDSLIEMMVG 239
Cdd:PRK13547 240 ADVLTPAHIARCYG 253
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-221 |
6.80e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.95 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwLGKETTFNGPKSSQ----EAGIGIIHQ--ELNLI 91
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVITAGKKNKKlkplRKKVGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 92 PQlTIAENIflgrefvnRFGKIDWKKMYAEADQLLAKLNlrfksdKLVG-----------ELSIGDQQMVEIAKVLSFES 160
Cdd:PRK13634 100 EE-TVEKDI--------CFGPMNFGVSEEDAKQKAREMI------ELVGlpeellarspfELSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 161 KVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIA 221
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-238 |
7.79e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.39 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY-----TRDAGSLLWLGKeTTFNGPKSSQEA--GIGIIHQELNLIP 92
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGR-NIYSPDVDPIEVrrEVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 93 QLTIAENIFLGREF---VNRFGKID----WK-KMYAEADQLLAKLNlrfksDKlVGELSIGDQQMVEIAKVLSFESKVII 164
Cdd:PRK14267 99 HLTIYDNVAIGVKLnglVKSKKELDerveWAlKKAALWDEVKDRLN-----DY-PSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 165 MDEPTDALTDTETESLFRVIRELKSQgRGIVYISHRMKEIFEICDDVTVFRDGQFI---AEREVATLTEDSLIEMMV 238
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIevgPTRKVFENPEHELTEKYV 248
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-221 |
1.05e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.53 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 3 ALLQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKE-TTFNgpKSSQEA 79
Cdd:PRK11160 337 VSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiADYS--EAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 80 GIGIIHQELNLIPQlTIAENIFLGrefvnrfgkidwkKMYAEADQLLAKLNlRFKSDKLV----------GE----LSIG 145
Cdd:PRK11160 415 AISVVSQRVHLFSA-TLRDNLLLA-------------APNASDEALIEVLQ-QVGLEKLLeddkglnawlGEggrqLSGG 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 146 DQQMVEIAKVLSFESKVIIMDEPTDALtDTETES-LFRVIRELkSQGRGIVYISHRMKEIfEICDDVTVFRDGQFIA 221
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGL-DAETERqILELLAEH-AQNKTVLMITHRLTGL-EQFDRICVMDNGQIIE 553
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
31-220 |
1.14e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 31 RVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETT---------------------FNGPKSSQEAGIG------- 82
Cdd:PTZ00265 1195 KTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTndmtneqdyqgdeeqnvgmknVNEFSLTKEGGSGedstvfk 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 83 -------------------------IIHQELNLIpQLTIAENIFLGREFVNRFgkiDWKKM--YAEADQLLAKLNLRFks 135
Cdd:PTZ00265 1275 nsgkilldgvdicdynlkdlrnlfsIVSQEPMLF-NMSIYENIKFGKEDATRE---DVKRAckFAAIDEFIESLPNKY-- 1348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 136 DKLVG----ELSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRELKSQG-RGIVYISHRMKEIfEICD 209
Cdd:PTZ00265 1349 DTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIeKTIVDIKDKAdKTIITIAHRIASI-KRSD 1426
|
250
....*....|....*
gi 2070354550 210 DVTVF----RDGQFI 220
Cdd:PTZ00265 1427 KIVVFnnpdRTGSFV 1441
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-217 |
1.20e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 55.41 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLW---LGKETTFNGPKSSQEAGIGIIHQELNLI 91
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 92 pQLTIAENIFLGREF-VNRFgkidwkKMYAEADQLLAKLN-LRFKSDKLVGE----LSIGDQQMVEIAKVLSFESKVIIM 165
Cdd:cd03290 92 -NATVEENITFGSPFnKQRY------KAVTDACSLQPDIDlLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 166 DEPTDALTDTETESLFR--VIRELKSQGRGIVYISHRMKEIFEiCDDVTVFRDG 217
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-199 |
1.21e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 27 VYPGRVMALVGENGAGKSTMMKVL-----TGIYTRDagsllwlgkETTFNGPK--SSQEAGIGIIHQELNLIPQLTIAEN 99
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLaervtTGVITGG---------DRLVNGRPldSSFQRSIGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 100 -IFlgREFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGE----LSIGDQQMVEIAKVLSFESKVII-MDEPTDALT 173
Cdd:TIGR00956 857 lRF--SAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
170 180
....*....|....*....|....*.
gi 2070354550 174 DTETESLFRVIRELKSQGRGIVYISH 199
Cdd:TIGR00956 935 SQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
242-485 |
1.34e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.41 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 242 LEDQYPHLDNAPGEIRLKVDNLCGPG-----VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEV 316
Cdd:PRK10789 300 VKDGSEPVPEGRGELDVNIRQFTYPQtdhpaLENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 317 VThspqdglangiVYISEDRKRDGLVLGM------SVKENMsltALGyfsRAGGSlkhkdeQQAVGDFIRLFNV------ 384
Cdd:PRK10789 380 TK-----------LQLDSWRSRLAVVSQTpflfsdTVANNI---ALG---RPDAT------QQEIEHVARLASVhddilr 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 385 -----KTPSMEQAIgLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIIlvSSEMPEVL 459
Cdd:PRK10789 437 lpqgyDTEVGERGV-MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVII--SAHRLSAL 513
|
250 260
....*....|....*....|....*.
gi 2070354550 460 GMSDRIIVMHEGHLSGEFTREQATQE 485
Cdd:PRK10789 514 TEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
269-452 |
1.41e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.46 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLYGAmPR---TSGYVTLDGHEVVTHSPqdglangivyisEDRKRDGLVL-- 343
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKyevTSGSILLDGEDILELSP------------DERARAGIFLaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 344 -------GMSVKENMSlTALGyfsraggslKHKDEQQAVGDFIRLFNVKtpsMEQaIGL------------LSGGNQQKV 404
Cdd:COG0396 84 qypveipGVSVSNFLR-TALN---------ARRGEELSAREFLKLLKEK---MKE-LGLdedfldryvnegFSGGEKKRN 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2070354550 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVS 452
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIIT 197
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-195 |
1.42e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.81 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGPKSSQE-AGIGiiHQelNLI-PQLTIAE 98
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDlLYLG--HQ--PGIkTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 99 NIflgrefvnRFgkidWKKMYAEAD-----QLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALT 173
Cdd:PRK13538 94 NL--------RF----YQRLHGPGDdealwEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180
....*....|....*....|..
gi 2070354550 174 DTETESLFRVIRELKSQGrGIV 195
Cdd:PRK13538 162 KQGVARLEALLAQHAEQG-GMV 182
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-218 |
1.54e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.49 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNVYPG-----RVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNgpkssqeagigiihqelnli 91
Cdd:cd03237 7 KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 92 PQLTIAENIFLGREFVNRFGKIDWKKMYAEADqLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTdA 171
Cdd:cd03237 67 PQYIKADYEGTVRDLLSSITKDFYTHPYFKTE-IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS-A 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2070354550 172 LTDTETESLF-RVIRE--LKSQGRGIVyISHRMKEIFEICDDVTVFrDGQ 218
Cdd:cd03237 145 YLDVEQRLMAsKVIRRfaENNEKTAFV-VEHDIIMIDYLADRLIVF-EGE 192
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
396-473 |
1.54e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.62 E-value: 1.54e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD-VGAKKeIYQLINQFKADgLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDpVGTAK-IEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
366-473 |
1.72e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 366 LKHKDEQQAVGDFIRLFNVkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADG 445
Cdd:NF000106 116 LSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDG 194
|
90 100
....*....|....*....|....*...
gi 2070354550 446 LSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-211 |
1.74e-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: 54.56 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 27 VYPGRVMALVGENGAGKSTMMKVL-----TGIYTrdaGSLLWLGKETTFNGPKSsqeagIGIIHQELNLIPQLTIAEnif 101
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILINGRPLDKNFQRS-----TGYVEQQDVHSPNLTVRE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 102 lgrefvnrfgkidwkkmyaeadqllaklNLRFkSDKLVGeLSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLF 181
Cdd:cd03232 99 ----------------------------ALRF-SALLRG-LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
170 180 190
....*....|....*....|....*....|.
gi 2070354550 182 RVIRELKSQGRGIV-YISHRMKEIFEICDDV 211
Cdd:cd03232 149 RFLKKLADSGQAILcTIHQPSASIFEKFDRL 179
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-249 |
2.24e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.94 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 27 VYPGRVMALVGENGAGKSTMMKVLTGIyTRDAGsllwlgkETTFNGPKSSQEAGIGIIHQELNLIPQLTIAENI----FL 102
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSG-------SIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMpvfqYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 103 GRefvNRFGKIDWKKMYAEADQLLAKLNLrfkSDKL---VGELSIGDQQMVEIAKV-------LSFESKVIIMDEPTDAL 172
Cdd:PRK03695 91 TL---HQPDKTRTEAVASALNEVAEALGL---DDKLgrsVNQLSGGEWQRVRLAAVvlqvwpdINPAGQLLLLDEPMNSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 173 TDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAE---REVatLTEDSL---IEMMVGRKLEDQY 246
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASgrrDEV--LTPENLaqvFGVNFRRLDVEGH 242
|
...
gi 2070354550 247 PHL 249
Cdd:PRK03695 243 PML 245
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
272-473 |
2.37e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.59 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 272 SFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVTHSPQDGLANGIVYisedrKRDGLVLGMSVKENM 351
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-QDHTTTPPSRRPVSMLF-----QENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 352 SL---TALGYFSRAGGSLKHKDEQQAVGDFI-RLfnvktPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
Cdd:PRK10771 93 GLglnPGLKLNAAQREKLHAIARQMGIEDLLaRL-----PGQ------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2070354550 428 VGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK10771 162 PALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-214 |
3.02e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.33 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNV-----YPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLlwlgkettfngpkssqEAGIGIIH--QELN 89
Cdd:COG1245 348 TKSYGGFSLEVeggeiREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------------DEDLKISYkpQYIS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 90 LIPQLTIAEniFLGREFVNRFGKIDWKkmyaeaDQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPT 169
Cdd:COG1245 412 PDYDGTVEE--FLRSANTDDFGSSYYK------TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2070354550 170 dALTDTETESLF-RVIREL-KSQGRGIVYISHRMKEIFEICDDVTVF 214
Cdd:COG1245 484 -AHLDVEQRLAVaKAIRRFaENRGKTAMVVDHDIYLIDYISDRLMVF 529
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-220 |
4.07e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.01 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 29 PGRVMALVGENGAGKSTMMKVLTGiytRDAGSllWLGKETTFNGPKSSQEAGIGII-HQELNLI--PQLTIAENI----F 101
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDVLAG---RKTGG--YIEGDIRISGFPKKQETFARISgYCEQNDIhsPQVTVRESLiysaF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 102 LgrEFVNRFGKIDwKKMYaeADQLLAKLNLRFKSDKLVG-----ELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTE 176
Cdd:PLN03140 980 L--RLPKEVSKEE-KMMF--VDEVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2070354550 177 TESLFRVIRELKSQGRGIVYISHRMK-EIFEICDDVTVF-RDGQFI 220
Cdd:PLN03140 1055 AAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMkRGGQVI 1100
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-228 |
4.95e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.48 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVK-----------ALSGAALNVYPGRVMALVGENGAGKSTmmkvlTGIytrdagSLLWLGK---ETT 69
Cdd:PRK15134 275 LLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKST-----TGL------ALLRLINsqgEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 70 FNG------------PKSSQeagIGIIHQELN--LIPQLTIAENIFLGREfvnrfgkIDWKKMYAEADQ----------- 124
Cdd:PRK15134 344 FDGqplhnlnrrqllPVRHR---IQVVFQDPNssLNPRLNVLQIIEEGLR-------VHQPTLSAAQREqqviavmeevg 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 125 LLAKLNLRFKSdklvgELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGR-GIVYISHRMKE 203
Cdd:PRK15134 414 LDPETRHRYPA-----EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHV 488
|
250 260
....*....|....*....|....*
gi 2070354550 204 IFEICDDVTVFRDGQFIAEREVATL 228
Cdd:PRK15134 489 VRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
268-473 |
5.10e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 54.31 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDGLA--NGIVYISED-------RKR 338
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrRDIQMVFQDsisavnpRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 339 DGLVLGMSVKENMSLTALGYFSRAGGSLKHKDEQQAVGDfirlfnvKTPsmeqaiGLLSGGNQQKVAIARGLMTRPKVLI 418
Cdd:PRK10419 108 VREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLD-------KRP------PQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 419 LDEPTRGVDVGAKKEIYQLINQFKAD-GLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-218 |
5.98e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.35 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRD---AGSLLWLGKE------ 67
Cdd:PRK09473 9 ADALLDVKDLRVTFSTpdgdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREilnlpe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 68 TTFNGPKSSQeagIGIIHQE----LNliPQLTIAENIFlgrEFVNRFGKIDWKKMYAEADQLLAKLNL---RFKSDKLVG 140
Cdd:PRK09473 89 KELNKLRAEQ---ISMIFQDpmtsLN--PYMRVGEQLM---EVLMLHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPH 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 141 ELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQ 218
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-220 |
7.69e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 29 PGRVMALVGENGAGKSTMMKVLTGiytRDAGSLLWLGKETTFNGpkSSQE------AGIGIIHQELNL-IPQLTIAENIf 101
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIAS---NTDGFHIGVEGVITYDG--ITPEeikkhyRGDVVYNAETDVhFPHLTVGETL- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 102 lgrEFV-------NRFGKIDwKKMYAE--ADQLLAKLNLRFKSDKLVGE-----LSIGDQQMVEIAKVLSFESKVIIMDE 167
Cdd:TIGR00956 160 ---DFAarcktpqNRPDGVS-REEYAKhiADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 168 PTDALtDTETEslFRVIRELKSQGR-----GIVYISHRMKEIFEICDDVTVFRDGQFI 220
Cdd:TIGR00956 236 ATRGL-DSATA--LEFIRALKTSANildttPLVAIYQCSQDAYELFDKVIVLYEGYQI 290
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-66 |
7.90e-08 |
|
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: 54.80 E-value: 7.90e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 5 LQLKGIDKAFPGVKALSGAA-----LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGK 66
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTlgpidLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ 394
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
396-474 |
9.30e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.27 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD----VGAKKEIYQLINQFkadGLSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
...
gi 2070354550 472 HLS 474
Cdd:PRK11000 211 RVA 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-223 |
9.35e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.25 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAF---------PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFn 71
Cdd:PRK15112 1 VETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 72 GPKSSQEAGIGIIHQE--LNLIPQLTIAENIflgrEFVNRFGkidwKKMYAEADQLLAKLNLRfksdkLVG--------- 140
Cdd:PRK15112 80 GDYSYRSQRIRMIFQDpsTSLNPRQRISQIL----DFPLRLN----TDLEPEQREKQIIETLR-----QVGllpdhasyy 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 141 --ELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELK-SQGRGIVYISHRMKEIFEICDDVTVFRDG 217
Cdd:PRK15112 147 phMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
....*.
gi 2070354550 218 QfIAER 223
Cdd:PRK15112 227 E-VVER 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
396-490 |
1.01e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.65 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KADGLSIILVSSEMPEVLGMSDRIIVMHEGHls 474
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQ-- 236
|
90
....*....|....*.
gi 2070354550 475 gefTREQATQEVLMAA 490
Cdd:PRK15093 237 ---TVETAPSKELVTT 249
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-220 |
1.36e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.72 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG--IYTRDAGSLLWLGKETTFNGPKSSQEAGI 81
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GIIHQELNLIPQLTIAEniFLGREFVNRfgkidwKKMY--AEADQL-----------LAKLNLRFKSDKLVGELSIGDQQ 148
Cdd:CHL00131 87 FLAFQYPIEIPGVSNAD--FLRLAYNSK------RKFQglPELDPLefleiineklkLVGMDPSFLSRNVNEGFSGGEKK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH--RMKEiFEICDDVTVFRDGQFI 220
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLD-YIKPDYVHVMQNGKII 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-199 |
1.39e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWlgkETTF-------NGPKS 75
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY---EQDLivarlqqDPPRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 76 SQE-------AGIG-------IIHQELNLIPQLTIAENIflgrefvNRFGKIDWKKMYAEADQLLAKLN-----LRFKSD 136
Cdd:PRK11147 79 VEGtvydfvaEGIEeqaeylkRYHDISHLVETDPSEKNL-------NELAKLQEQLDHHNLWQLENRINevlaqLGLDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 137 KLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTET----ESLfrvireLKSQGRGIVYISH 199
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHL-DIETiewlEGF------LKTFQGSIIFISH 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
268-463 |
1.50e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.86 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVlYGAMP------RTSGYVTLDGHEvvthspqdgLANGIVYISEDRKRDGL 341
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRC-FNRLNdlipgfRVEGKVTFHGKN---------LYAPDVDPVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 342 VLGM------SVKENMSltalgYFSRAGGSLKHKDE------QQAVgdfirLFNVKTPSMEQAIGLLSGGNQQKVAIARG 409
Cdd:PRK14243 96 VFQKpnpfpkSIYDNIA-----YGARINGYKGDMDElverslRQAA-----LWDEVKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADgLSIILVSSEMPEVLGMSD 463
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
258-452 |
1.64e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.34 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 258 LKVDNLcGPGVND------VSFVLRKGEILGISGLMGAGRTELMKVLYG--AMPRTSGYVTLDGHEVVTHSPqdglangi 329
Cdd:CHL00131 8 LEIKNL-HASVNEneilkgLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEP-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 330 vyisEDRKRDGLVLGMSVK------ENMSLTALGYFSraggslKHKDEQQAVGDFIRLFNVKTPSMEqAIGL-------- 395
Cdd:CHL00131 79 ----EERAHLGIFLAFQYPieipgvSNADFLRLAYNS------KRKFQGLPELDPLEFLEIINEKLK-LVGMdpsflsrn 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2070354550 396 ----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVS 452
Cdd:CHL00131 148 vnegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIT 208
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
268-452 |
2.06e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.60 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQ------DGLANGIVY--ISEDRKRD 339
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQrpymtlGTLRDQIIYpdSSEDMKRR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 340 GLVlGMSVKENMSLTALGYFSRAGGSLkhkdeqQAVGDFirlfnvktpsMEqaigLLSGGNQQKVAIARGLMTRPKVLIL 419
Cdd:TIGR00954 548 GLS-DKDLEQILDNVQLTHILEREGGW------SAVQDW----------MD----VLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|...
gi 2070354550 420 DEPTRGVDVGAKKEIYQLINQFkadGLSIILVS 452
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREF---GITLFSVS 636
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-199 |
2.67e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.98 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLL----WLGKETTFNGP------KSSQEAGIGIIH--QELNLIPqlti 96
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdWDEILDEFRGSelqnyfTKLLEGDVKVIVkpQYVDLIP---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 97 aeNIFLG--REFVNRFGKIDWKkmyaeaDQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALTD 174
Cdd:cd03236 101 --KAVKGkvGELLKKKDERGKL------DELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*
gi 2070354550 175 TETESLFRVIRELKSQGRGIVYISH 199
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-180 |
2.95e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWlgkettfngpksSQEAGIGII 84
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------------SENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 85 HQElnlipqltiaenifLGREFVNRFGKIDWKKMYAEA---DQLL-AKL-NLRFKSD---KLVGELSIGDQQMVEIAKVL 156
Cdd:PRK15064 388 AQD--------------HAYDFENDLTLFDWMSQWRQEgddEQAVrGTLgRLLFSQDdikKSVKVLSGGEKGRMLFGKLM 453
|
170 180
....*....|....*....|....*
gi 2070354550 157 SFESKVIIMDEPTDALtDTET-ESL 180
Cdd:PRK15064 454 MQKPNVLVMDEPTNHM-DMESiESL 477
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-177 |
3.24e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 8 KGIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLwLGkETtfngpkssqeAGIGIIHQ 86
Cdd:PRK11819 328 ENLSKSF-GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IG-ET----------VKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 87 EL-NLIPQLTIAENIFLGREFVnRFGKidwKKMYAEAdqLLAKLNlrFK-SD--KLVGELSIGDQQMVEIAKVLSFESKV 162
Cdd:PRK11819 395 SRdALDPNKTVWEEISGGLDII-KVGN---REIPSRA--YVGRFN--FKgGDqqKKVGVLSGGERNRLHLAKTLKQGGNV 466
|
170
....*....|....*
gi 2070354550 163 IIMDEPTDALtDTET 177
Cdd:PRK11819 467 LLLDEPTNDL-DVET 480
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
388-477 |
3.39e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.40 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 388 SMEQAIGLLSGGNQQKVAIARGLMTRPK--VLILDEPTRGVDvgaKKEIYQLINQFKA---DGLSIILVSSEmPEVLGMS 462
Cdd:cd03238 80 TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH---QQDINQLLEVIKGlidLGNTVILIEHN-LDVLSSA 155
|
90
....*....|....*
gi 2070354550 463 DRIIVMheGHLSGEF 477
Cdd:cd03238 156 DWIIDF--GPGSGKS 168
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-198 |
4.05e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWlgKETTFNgpkSSQEAGIGIIHQELNLIPQLTIAENIFLGREFVN 108
Cdd:PRK13541 25 PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNIN---NIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 109 RFGKIDWKKMYAEADQLLaklnlrfksDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRVIRELK 188
Cdd:PRK13541 100 SAETLYAAIHYFKLHDLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL-SKENRDLLNNLIVMK 169
|
170
....*....|
gi 2070354550 189 SQGRGIVYIS 198
Cdd:PRK13541 170 ANSGGIVLLS 179
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
267-469 |
5.16e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.83 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 267 GVNdvSFVL------RKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGH--EVVTHSPQDGLANGIVYISEDRkr 338
Cdd:cd03236 11 GPN--SFKLhrlpvpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdEILDEFRGSELQNYFTKLLEGD-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 339 dglvLGMSVK-ENMSLTALGYFSRAGGSLKHKDEQQAVGDFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
Cdd:cd03236 87 ----VKVIVKpQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 418 ILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMpEVLGM-SDRIIVMH 469
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL-AVLDYlSDYIHCLY 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
266-489 |
5.87e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMP-RTSGYVTLDGheVVTHSPQdglangIVYISEDRKRDGLVLG 344
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPpRSDASVVIRG--TVAYVPQ------VSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 M---SVKENMSLTAlgyfsragGSLKHKDEQQAVGDFirlfnvkTPSMEQAIGLlSGGNQQKVAIARGLMTRPKVLILDE 421
Cdd:PLN03130 703 SpfdPERYERAIDV--------TALQHDLDLLPGGDL-------TEIGERGVNI-SGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070354550 422 PTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMpEVLGMSDRIIVMHEGHLsgeftREQATQEVLMA 489
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQL-HFLSQVDRIILVHEGMI-----KEEGTYEELSN 828
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
268-473 |
6.85e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHE--VVTHSPQDGLANGIvyisEDRKRDGLVLGM 345
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAalIAISSGLNGQLTGI----ENIELKGLMMGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLTAlgyfsraggslkHKDEQQAVGDFIrlfnvktpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
Cdd:PRK13545 116 TKEKIKEIIP------------EIIEFADIGKFI----------YQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2070354550 426 VDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK13545 174 GDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
270-468 |
9.24e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTL-DGHE--------------VVTHSP---QDGLANGIVY 331
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNlkdinlkwwrskigVVSQDPllfSNSIKNNIKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 332 ----------ISEDRKRDGLVL--GMSVKENMSLTALGYFS------RAGGSLKHKDEQQAVGD----------FIRLFN 383
Cdd:PTZ00265 483 slyslkdleaLSNYYNEDGNDSqeNKNKRNSCRAKCAGDLNdmsnttDSNELIEMRKNYQTIKDsevvdvskkvLIHDFV 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 384 VKTP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEV 458
Cdd:PTZ00265 563 SALPdKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLST 642
|
250
....*....|
gi 2070354550 459 LGMSDRIIVM 468
Cdd:PTZ00265 643 IRYANTIFVL 652
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
268-471 |
9.42e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.42 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTS--GYVTLDGHEvvthsPQDGLANGIVYISEDrkrDGLVLGM 345
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRK-----PTKQILKRTGFVTQD---DILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENMSLTALgyfSRAGGSLKHKDEQQAVGDFIRLFNVkTPSMEQAIGL-----LSGGNQQKVAIARGLMTRPKVLILD 420
Cdd:PLN03211 156 TVRETLVFCSL---LRLPKSLTKQEKILVAESVISELGL-TKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 421 EPTRGVDVGAKKEIYQLINQFKADGLSIIlVSSEMP--EVLGMSDRIIVMHEG 471
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIV-TSMHQPssRVYQMFDSVLVLSEG 283
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
266-481 |
9.95e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRT-SGYVTLDGheVVTHSPQdglangIVYISEDRKRDGLVLG 344
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRG--SVAYVPQ------VSWIFNATVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 345 MSVKENMSLTALGYfsragGSLKHKDEQQAVGDfirlfnvKTPSMEQAIGLlSGGNQQKVAIARGLMTRPKVLILDEPTR 424
Cdd:PLN03232 703 SDFESERYWRAIDV-----TALQHDLDLLPGRD-------LTEIGERGVNI-SGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 425 GVDVGAKKEIYQLINQFKADGLSIILVSSEMpEVLGMSDRIIVMHEGHLSGEFTREQ 481
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAE 825
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
270-471 |
1.01e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVL----YGAMPRTSGYVTLDG---HEVVTHSPQDglangIVYISEDrkrDGLV 342
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGitpEEIKKHYRGD-----VVYNAET---DVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LGMSVKENMSLTAL---------------------GYFSRAGGsLKHKDEQQAVGDFIRlfnvktpsmeqaiGLlSGGNQ 401
Cdd:TIGR00956 151 PHLTVGETLDFAARcktpqnrpdgvsreeyakhiaDVYMATYG-LSHTRNTKVGNDFVR-------------GV-SGGER 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI----NQFKADGLSIILVSSemPEVLGMSDRIIVMHEG 471
Cdd:TIGR00956 216 KRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALktsaNILDTTPLVAIYQCS--QDAYELFDKVIVLYEG 287
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
266-487 |
1.42e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgLANGIVYISEDRkrdgLVLGM 345
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD-LRRVLSIIPQSP----VLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 346 SVKENmsltaLGYFSraggslKHKD-------EQQAVGDFIRL--FNVKTPSMEQAIGLlSGGNQQKVAIARGLMTRPKV 416
Cdd:PLN03232 1325 TVRFN-----IDPFS------EHNDadlwealERAHIKDVIDRnpFGLDAEVSEGGENF-SVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070354550 417 LILDEPTRGVDVGAKKEIYQLI-NQFKAdgLSIILVSSEMPEVLGmSDRIIVMHeghlSGEFTREQATQEVL 487
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIrEEFKS--CTMLVIAHRLNTIID-CDKILVLS----SGQVLEYDSPQELL 1457
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
269-471 |
1.65e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 269 NDVSFVLRKGEILGISGLMGAGRTELMKVLygAMPRTSGYVTLDghevvthspqDGLANGIVYISEDRKRDGLV------ 342
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVL--AERVTTGVITGG----------DRLVNGRPLDSSFQRSIGYVqqqdlh 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 LGMS-VKENMSLTAlgyFSRAGGSLKHKDEQQAVGDFIRLFNVKTPSmEQAIGL----LSGGNQQKVAIARGLMTRPKVL 417
Cdd:TIGR00956 848 LPTStVRESLRFSA---YLRQPKSVSKSEKMEYVEEVIKLLEMESYA-DAVVGVpgegLNVEQRKRLTIGVELVAKPKLL 923
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 418 I-LDEPTRGVDVGAKKEIYQLINQFkADGLSIILVSSEMPEVLGMS--DRIIVMHEG 471
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
268-428 |
1.75e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMP--------RTSGYVTLDGHEVVTHSPQDgLANGIVYISEDRKRd 339
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPR-LARLRAVLPQAAQP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 340 glVLGMSVKEnmsLTALGYF--SRAGGSLKHKDEQQAVGDFIRLfnVKTPSMEQAIGLLSGGNQQKVAIARGL------- 410
Cdd:PRK13547 95 --AFAFSARE---IVLLGRYphARRAGALTHRDGEIAWQALALA--GATALVGRDVTTLSGGELARVQFARVLaqlwpph 167
|
170 180
....*....|....*....|
gi 2070354550 411 --MTRPKVLILDEPTRGVDV 428
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDL 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-214 |
1.77e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 17 VKALSGAALNV-----YPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWlgkettfngpkssqEAGIGIIHQELNLI 91
Cdd:PRK13409 347 TKKLGDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--------------ELKISYKPQYIKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 92 PQLTIAEniFLgREFVNRFGKIDWKkmyaeaDQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTdA 171
Cdd:PRK13409 413 YDGTVED--LL-RSITDDLGSSYYK------SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS-A 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2070354550 172 LTDTETESLF-RVIREL-KSQGRGIVYISHRMKEIFEICDDVTVF 214
Cdd:PRK13409 483 HLDVEQRLAVaKAIRRIaEEREATALVVDHDIYMIDYISDRLMVF 527
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-228 |
2.42e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 1 MDALLQLKGIDKAFPGVkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY----TRDAGSLLWLGKETTfngPKSS 76
Cdd:PRK10418 1 MPQQIELRNIALQAAQP-LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVA---PCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 77 QEAGIGIIHQE----LNliPQLTIAENiflGREFVNRFGKIdwkkmyAEADQLLAKLnlrfksdKLVG------------ 140
Cdd:PRK10418 77 RGRKIATIMQNprsaFN--PLHTMHTH---ARETCLALGKP------ADDATLTAAL-------EAVGlenaarvlklyp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 141 -ELSIGDQQMVEIAKVLSFESKVIIMDEPT---DALTDTETESLF-RVIRElksQGRGIVYISHRMKEIFEICDDVTVFR 215
Cdd:PRK10418 139 fEMSGGMLQRMMIALALLCEAPFIIADEPTtdlDVVAQARILDLLeSIVQK---RALGMLLVTHDMGVVARLADDVAVMS 215
|
250
....*....|...
gi 2070354550 216 DGQFIAEREVATL 228
Cdd:PRK10418 216 HGRIVEQGDVETL 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
266-471 |
2.55e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 266 PGVNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHspqdGLAngivyisEDRKRDGLV--- 342
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF----GLM-------DLRKVLGIIpqa 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 343 ---LGMSVKENmsltaLGYFSraggslKHKD-------EQQAVGDFIRlfnvktpsmEQAIGL----------LSGGNQQ 402
Cdd:PLN03130 1322 pvlFSGTVRFN-----LDPFN------EHNDadlweslERAHLKDVIR---------RNSLGLdaevseagenFSVGQRQ 1381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKADGLSIIlvSSEMPEVLGmSDRIIVMHEG 471
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIrEEFKSCTMLII--AHRLNTIID-CDRILVLDAG 1448
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
125-466 |
2.55e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 125 LLAKLNLRFKS-DKLVGELSIGDQQMVEIAKVLSFESKVI--IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRM 201
Cdd:PRK00635 459 ILIDLGLPYLTpERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDE 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 202 KEIfEICDDVTVFRDGQFIAEREVA--------TLTEDSLIEMMVGRKLEDQYP-HLDNAPGEIRLK---VDNLcgpgvN 269
Cdd:PRK00635 539 QMI-SLADRIIDIGPGAGIFGGEVLfngsprefLAKSDSLTAKYLRQELTIPIPeKRTNSLGTLTLSkatKHNL-----K 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMK-VLYGAMPRtsgyvTLDGHEVVTHSPQDGLANGIVYISED------------- 335
Cdd:PRK00635 613 DLTISLPLGRLTVVTGVSGSGKSSLINdTLVPAVEE-----FIEQGFCSNLSIQWGAISRLVHITRDlpgrsqrsiplty 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 336 ----------------RKRDGLvlgmsVKENMSL-TALGYFSRAG--GSLKHKDEQ------------------------ 372
Cdd:PRK00635 688 ikafddlrelfaeqprSKRLGL-----TKSHFSFnTPLGACAECQglGSITTTDNRtsipcpsclgkrflpqvlevrykg 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 373 QAVGDFIRL-------FNVKTPSMEQAI------GL-----------LSGGNQQKVAIARGLMT---RPKVLILDEPTRG 425
Cdd:PRK00635 763 KNIADILEMtayeaekFFLDEPSIHEKIhalcslGLdylplgrplssLSGGEIQRLKLAYELLApskKPTLYVLDEPTTG 842
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2070354550 426 VDVGAKKEIYQLINQFKADGLSIILVSSEMpEVLGMSDRII 466
Cdd:PRK00635 843 LHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVL 882
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
394-473 |
3.51e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAD--GLSIILVSSEMPEVLGMsDRIIVMHEG 471
Cdd:NF033858 135 GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMDAG 213
|
..
gi 2070354550 472 HL 473
Cdd:NF033858 214 RV 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-218 |
6.55e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfngpkssqEAGIGIIHQELNLIPQltiAEN 99
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--------KFGLMDLRKVLGIIPQ---APV 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 100 IFLGrefVNRFgKIDWKKMYAEAD--QLLAKLNLR-------FKSDKLVGE----LSIGDQQMVEIAKVLSFESKVIIMD 166
Cdd:PLN03130 1324 LFSG---TVRF-NLDPFNEHNDADlwESLERAHLKdvirrnsLGLDAEVSEagenFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 167 EPTDALtDTETESLF-RVIR-ELKSQGRGIvyISHRMKEIFEiCDDVTVFRDGQ 218
Cdd:PLN03130 1400 EATAAV-DVRTDALIqKTIReEFKSCTMLI--IAHRLNTIID-CDRILVLDAGR 1449
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
268-473 |
7.07e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 268 VNDVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGhEVVTHSPQDGLaNGIVYISEDRKRDGLVLGMSV 347
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAGL-SGQLTGIENIEFKMLCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMSLT-ALGYFSRaggslkhkdeqqaVGDFIRlfnvktpsmeQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
Cdd:PRK13546 118 KEIKAMTpKIIEFSE-------------LGEFIY----------QPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2070354550 427 DVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHL 473
Cdd:PRK13546 175 DQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-232 |
7.35e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.45 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKettfNGPKSSQEA------GIGIIHQELNLIPQLTIAE 98
Cdd:PRK11831 28 LTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE----NIPAMSRSRlytvrkRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 99 NI-FLGREFVNRFGKIdwkkMYAEADQLLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEP---TDALTd 174
Cdd:PRK11831 104 NVaYPLREHTQLPAPL----LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPfvgQDPIT- 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 175 teTESLFRVIRELKSQ-GRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVATLTEDS 232
Cdd:PRK11831 179 --MGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
253-471 |
7.65e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 253 PGEIRLKVDNLCGPGVNDVSFVLRK-------GEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQDgL 325
Cdd:TIGR00957 1280 PPRGRVEFRNYCLRYREDLDLVLRHinvtihgGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-L 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 326 ANGIVYISEDRkrdglVLgMSVKENMSLTALGYFSraggslkhkDEQqaVGDFIRLFNVKTPSMEQAIGL---------- 395
Cdd:TIGR00957 1359 RFKITIIPQDP-----VL-FSGSLRMNLDPFSQYS---------DEE--VWWALELAHLKTFVSALPDKLdhecaeggen 1421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFkaDGLSIILVSSEMPEVLGMSdRIIVMHEG 471
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIrTQF--EDCTVLTIAHRLNTIMDYT-RVIVLDKG 1495
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
366-451 |
1.44e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 366 LKHKDEQQAVGDFIRLFNVKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADG 445
Cdd:COG1245 184 LEKVDERGKLDELAEKLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEG 262
|
....*.
gi 2070354550 446 LSIILV 451
Cdd:COG1245 263 KYVLVV 268
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-206 |
1.80e-05 |
|
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: 47.63 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETtfngpkssqeAGIGI--IHQELNLIPQLTIaenIFL 102
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI----------AKIGLhdLRFKITIIPQDPV---LFS 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 103 G--REFVNRFGKIDWKKMYAEADQLLAKLNLRFKSDKLVGE-------LSIGDQQMVEIAKVLSFESKVIIMDEPTDALt 173
Cdd:TIGR00957 1374 GslRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAV- 1452
|
170 180 190
....*....|....*....|....*....|...
gi 2070354550 174 DTETESLFRVIRELKSQGRGIVYISHRMKEIFE 206
Cdd:TIGR00957 1453 DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMD 1485
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
270-430 |
2.23e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAmpRTSGYVtlDGHEVVTHSP--QDGLANGIVYISEDRKRDGLVlgmSV 347
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYI--EGDIRISGFPkkQETFARISGYCEQNDIHSPQV---TV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 348 KENMSLTAlgyFSRAGGSLKHKDEQQAVGDFIRLfnVKTPSMEQAI-GL-----LSGGNQQKVAIARGLMTRPKVLILDE 421
Cdd:PLN03140 971 RESLIYSA---FLRLPKEVSKEEKMMFVDEVMEL--VELDNLKDAIvGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
....*....
gi 2070354550 422 PTRGVDVGA 430
Cdd:PLN03140 1046 PTSGLDARA 1054
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-195 |
2.61e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 27 VYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTfNGPKSSQEAGIGIIHqelNLIPQLTIAENIflgrEF 106
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-RGDRSRFMAYLGHLP---GLKADLSTLENL----HF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 107 VNRFGKIDWKKMYAEAdqlLAKLNLRFKSDKLVGELSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIR 185
Cdd:PRK13543 106 LCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL-DLEGITLVnRMIS 181
|
170
....*....|.
gi 2070354550 186 -ELKSQGRGIV 195
Cdd:PRK13543 182 aHLRGGGAALV 192
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-223 |
7.89e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.09 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsllwlgkETTFNGPKSSQ------EAGIGIIHQELNLIP 92
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-------DIRFHDIPLTKlqldswRSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 93 QlTIAENIFLGREfvnrfgkiDWKKMYAEADQLLAK-----LNLRFKSDKLVGE----LSIGDQQMVEIAKVLSFESKVI 163
Cdd:PRK10789 403 D-TVANNIALGRP--------DATQQEIEHVARLASvhddiLRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 164 IMDeptDALT--DTETEslFRVIRELKS--QGRGIVYISHRMKEIFEiCDDVTVFRDGQfIAER 223
Cdd:PRK10789 474 ILD---DALSavDGRTE--HQILHNLRQwgEGRTVIISAHRLSALTE-ASEILVMQHGH-IAQR 530
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-199 |
9.92e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI--YTRDAGSLLWLGKETTFNGPKSSQEAGI 81
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 82 GIIHQELNLIPqlTIAENIFL-----------GREFVNRFG-------KIDWKKMyaEADQLLAKLNLRFksdklvgelS 143
Cdd:PRK09580 81 FMAFQYPVEIP--GVSNQFFLqtalnavrsyrGQEPLDRFDfqdlmeeKIALLKM--PEDLLTRSVNVGF---------S 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 144 IGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH 199
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
267-451 |
1.13e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 267 GVNdvSFVL------RKGEILGISGLMGAGRTELMKVLYGAM-P---RTSGYVTLDghEVVTH----SPQD---GLANG- 328
Cdd:PRK13409 84 GVN--GFKLyglpipKEGKVTGILGPNGIGKTTAVKILSGELiPnlgDYEEEPSWD--EVLKRfrgtELQNyfkKLYNGe 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 329 ------IVYISEDRKrdglVLGMSVKEnmsltalgyfsraggSLKHKDEQQAVGDFIRLFNVKtPSMEQAIGLLSGGNQQ 402
Cdd:PRK13409 160 ikvvhkPQYVDLIPK----VFKGKVRE---------------LLKKVDERGKLDEVVERLGLE-NILDRDISELSGGELQ 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2070354550 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkADGLSIILV 451
Cdd:PRK13409 220 RVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL-AEGKYVLVV 267
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
270-459 |
1.34e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 270 DVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLdgHEVVTHSPQDGLANgivYISEDRkrdGLVLGMSVKE 349
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAKPYCT---YIGHNL---GLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 350 NMSLTALGYFSraggslkhKDEQQAVGDFIRLFNVktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVG 429
Cdd:PRK13541 90 NLKFWSEIYNS--------AETLYAAIHYFKLHDL----LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
170 180 190
....*....|....*....|....*....|
gi 2070354550 430 AKKEIYQLInQFKADGLSIILVSSEMPEVL 459
Cdd:PRK13541 158 NRDLLNNLI-VMKANSGGIVLLSSHLESSI 186
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
124-199 |
1.59e-04 |
|
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: 42.31 E-value: 1.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 124 QLLAKLNLRFKS-DKLVGELSIGDQQMVEIAKVLSFESK--VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH 199
Cdd:cd03238 69 QFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH 147
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
126-238 |
3.84e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.20 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 126 LAKLNLRFKS-----DKLVGE----LSIGDQQMVEIAKVLSFESKVIIMDEPTdALTDTETESLFRVIRELKSQGRGIVY 196
Cdd:cd03288 132 IAQLKNMVKSlpgglDAVVTEggenFSVGQRQLFCLARAFVRKSSILIMDEAT-ASIDMATENILQKVVMTAFADRTVVT 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2070354550 197 ISHRMKEIFEiCDDVTVFRDGqFIAEREVAT---LTEDSLIEMMV 238
Cdd:cd03288 211 IAHRVSTILD-ADLVLVLSRG-ILVECDTPEnllAQEDGVFASLV 253
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
281-474 |
4.41e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 281 LGISGLMGAGRTELMKVLYGAMPRTSGyvtldgheVVTHSPQDGLAngivyISEDRKRDGLvlgmsvkeNMSLTALGYFS 360
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSG--------TVFRSAKVRMA-----VFSQHHVDGL--------DLSSNPLLYMM 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 361 RAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQ 440
Cdd:PLN03073 597 RCFPGVPEQKLRAHLGSFGVTGNLALQPMYT----LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVL 672
|
170 180 190
....*....|....*....|....*....|....
gi 2070354550 441 FKAdglSIILVSSEMPEVLGMSDRIIVMHEGHLS 474
Cdd:PLN03073 673 FQG---GVLMVSHDEHLISGSVDELWVVSEGKVT 703
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-263 |
5.38e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTgiytrdagsllwlgkettfnGPKSSQEAGIGIIHQELNLIPQL----- 94
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAML--------------------GELSHAETSSVVIRGSVAYVPQVswifn 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 95 -TIAENIFLGREF-VNRFGK-IDWKKMYAEADqLLAKLNLRFKSDKLVgELSIGDQQMVEIAKVLSFESKVIIMDEPTDA 171
Cdd:PLN03232 693 aTVRENILFGSDFeSERYWRaIDVTALQHDLD-LLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 172 LTDTETESLFRVIRELKSQGRGIVYISHRMkEIFEICDDVTVFRDGQFIAEREVATLTEDSLIemmvGRKLEDQYPHLDn 251
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKSGSL----FKKLMENAGKMD- 844
|
250
....*....|..
gi 2070354550 252 APGEIRLKVDNL 263
Cdd:PLN03232 845 ATQEVNTNDENI 856
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-204 |
6.98e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 6.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070354550 134 KSDKLVG----ELSIGDQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRELK-SQGRGIVYISHRMKEI 204
Cdd:PTZ00265 568 KYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSL-DNKSEYLVqKTINNLKgNENRITIIIAHRLSTI 643
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
138-209 |
1.57e-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: 39.27 E-value: 1.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070354550 138 LVGELSIGDQQMVEIAKVLSFESK----VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRmKEIFEICD 209
Cdd:cd03227 74 TRLQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL-PELAELAD 148
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
386-430 |
1.60e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2070354550 386 TPSME-QAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGA 430
Cdd:PLN03073 334 TPEMQvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA 379
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
30-73 |
2.14e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 40.73 E-value: 2.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2070354550 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSLLWLGKETTFNGP 73
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-52 |
3.59e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 3.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2070354550 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG 52
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG 360
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
396-485 |
4.82e-03 |
|
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: 37.94 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGL-SIILVSSEMPEVLGMSDRIIVMH-EGHL 473
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFEgEPGV 151
|
90
....*....|..
gi 2070354550 474 SGEFTREQATQE 485
Cdd:cd03222 152 YGIASQPKGTRE 163
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
396-472 |
4.98e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.06 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD----VGAKKEIYQLINQFKAdglSIILVSSEMPEVLGMSDRIIVMHEG 471
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrVQMRLEIQRLHRRLKT---TSLYVTHDQVEAMTLADRVVVMNGG 211
|
.
gi 2070354550 472 H 472
Cdd:PRK11650 212 V 212
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
275-485 |
7.00e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.23 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 275 LRKGEILGISGLMGAGRTELMKVLYGA--MPRTSGYVTLDGHEVVTHSPQDGLANGIV----YISEdrkrdglVLGMSVK 348
Cdd:PRK09580 24 VRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFmafqYPVE-------IPGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070354550 349 --ENMSLTALGYFsRAGGSLKHKDEQQAVGDFIRLFNVKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
Cdd:PRK09580 97 ffLQTALNAVRSY-RGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070354550 426 VDVGAKKEIYQLINQFKADGLSIILVsSEMPEVLGM--SDRIIVMHEGHL--SGEFTREQATQE 485
Cdd:PRK09580 176 LDIDALKIVADGVNSLRDGKRSFIIV-THYQRILDYikPDYVHVLYQGRIvkSGDFTLVKQLEE 238
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-201 |
8.65e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 8.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2070354550 142 LSIGDQQMVEIAKVLSFESK---VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRM 201
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
265-323 |
9.96e-03 |
|
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: 38.63 E-value: 9.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2070354550 265 GPgvndVSFVLRKGEILGISGLMGAGRTELMKVLYGAMPRTSGYVTLDGHEVVTHSPQD 323
Cdd:COG4615 349 GP----IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREA 403
|
|
| |
