|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-510 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 813.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGI 89
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELDLVPNLSSAENIFLSREPVNeFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAK 169
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRR-GGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 170 IIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVRLMVGRS 249
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 250 IDQFFIKERATITDEIFRVEGiklWSLDRKkllVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGG 329
Cdd:COG1129 241 LEDLFPKRAAAPGEVVLEVEG---LSVGGV---VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP-ADSGEIRLDG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 330 KEIKIHSPRDAVKNGIGLVPEDRKTAGLILQMSVLHNITLPSVVMkliVRKFGLIDSQLEKEIVRSFIEKLNIKTPSPYQ 409
Cdd:COG1129 314 KPVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDR---LSRGGLLDRRRERALAEEYIKRLRIKTPSPEQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 410 IVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEG 489
Cdd:COG1129 391 PVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREG 470
|
490 500
....*....|....*....|.
gi 490181991 490 RKTAEFLREEVTEEDLLKAAI 510
Cdd:COG1129 471 RIVGELDREEATEEAIMAAAT 491
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-510 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 660.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYP--DYEGQIFLEGKEVRFRNPREAQEN 87
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 GIALIPQELDLVPNLSSAENIFLSREPVnEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLD 167
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEIT-PGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 168 AKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVRLMVG 247
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 248 RSIDQFFIKERATITDEIFRVEGIKLWSLD-RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTEGKVF 326
Cdd:PRK13549 242 RELTALYPREPHTIGEVILEVRNLTAWDPVnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 327 IGGKEIKIHSPRDAVKNGIGLVPEDRKTAGLILQMSVLHNITLPSVVMkliVRKFGLIDSQLEKEIVRSFIEKLNIKTPS 406
Cdd:PRK13549 322 IDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDR---FTGGSRIDDAAELKTILESIQRLKVKTAS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 407 PYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVM 486
Cdd:PRK13549 399 PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
|
490 500
....*....|....*....|....
gi 490181991 487 SEGRKTAEFLREEVTEEDLLKAAI 510
Cdd:PRK13549 479 HEGKLKGDLINHNLTQEQVMEAAL 502
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-517 |
0e+00 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 596.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGI 89
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELDLVPNLSSAENIFLSREPVNEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAK 169
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 170 IIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVRLMVGRS 249
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 250 I-DQF--FIKERATITDEIFRVEGIKlwsldrkkllVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVF 326
Cdd:PRK10762 242 LeDQYprLDKAPGEVRLKVDNLSGPG----------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP-RTSGYVT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 327 IGGKEIKIHSPRDAVKNGIGLVPEDRKTAGLILQMSVLHNITLPSvvMKLIVRKFGLIDSQLEKEIVRSFIEKLNIKTPS 406
Cdd:PRK10762 311 LDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTA--LRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 407 PYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVM 486
Cdd:PRK10762 389 MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVM 468
|
490 500 510
....*....|....*....|....*....|.
gi 490181991 487 SEGRKTAEFLREEVTEEDLLKAAIPRSVKVE 517
Cdd:PRK10762 469 HEGRISGEFTREQATQEKLMAAAVGKLNRVN 499
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-513 |
0e+00 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 583.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIALI 92
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFLSREPvNEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIII 172
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQLP-HKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 173 MDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGP-IEEFDHDKLVRLMVGRSID 251
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDdMAQVDRDQLVQAMVGREIG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 252 QFFIKERATITDEIFRVEGIKlwsldrKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKE 331
Cdd:PRK11288 244 DIYGYRPRPLGEVRLRLDGLK------GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATR-RTAGQVYLDGKP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 332 IKIHSPRDAVKNGIGLVPEDRKTAGLILQMSVLHNITLPSvvMKLIVRKFGLIDSQLEKEIVRSFIEKLNIKTPSPYQIV 411
Cdd:PRK11288 317 IDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISA--RRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 412 ENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRK 491
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
490 500
....*....|....*....|..
gi 490181991 492 TAEFLREEVTEEDLLKAAIPRS 513
Cdd:PRK11288 475 AGELAREQATERQALSLALPRT 496
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-508 |
0e+00 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 574.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYP--DYEGQIFLEGKEVRFRNPREAQENGI 89
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgSYEGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELDLVPNLSSAENIFLSREPVnEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAK 169
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERA-KRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 170 IIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKV-----GEGPIEEfdhDKLVRL 244
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIetldcRADEVTE---DRIIRG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 245 MVGRSIDQFFIKERATITDEIFRVEGiklWS----LDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGR 320
Cdd:NF040905 237 MVGRDLEDRYPERTPKIGEVVFEVKN---WTvyhpLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 321 -TEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDRKTAGLILQMSVLHNITLPSvvMKLIVRKfGLIDSQLEKEIVRSFIEK 399
Cdd:NF040905 314 nISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLAN--LGKVSRR-GVIDENEEIKVAEEYRKK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 400 LNIKTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAM 479
Cdd:NF040905 391 MNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGM 470
|
490 500
....*....|....*....|....*....
gi 490181991 480 SDRILVMSEGRKTAEFLREEVTEEDLLKA 508
Cdd:NF040905 471 CDRIYVMNEGRITGELPREEASQERIMRL 499
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-505 |
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: 545.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 8 EREVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVY-PDyEGQIFLEGKEVRFRNPREAQE 86
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqPD-SGEILIDGKPVRIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 87 NGIALIPQELDLVPNLSSAENIFLSREPVNeFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSL 166
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVLGLEPTK-GGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 167 DAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVRLMV 246
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 247 GRSIDQFFIKERATITDEIFRVEGIKLWSlDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVF 326
Cdd:COG3845 239 GREVLLRVEKAPAEPGEVVLEVENLSVRD-DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP-PASGSIR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 327 IGGKEIKIHSPRDAVKNGIGLVPEDRKTAGLILQMSVLHNITLPSVVMKLIVRkFGLIDSQLEKEIVRSFIEKLNIKTPS 406
Cdd:COG3845 317 LDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPPFSR-GGFLDRKAIRAFAEELIEEFDVRTPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 407 PYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVM 486
Cdd:COG3845 396 PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVM 475
|
490
....*....|....*....
gi 490181991 487 SEGRKTAEFLREEVTEEDL 505
Cdd:COG3845 476 YEGRIVGEVPAAEATREEI 494
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-510 |
3.30e-178 |
|
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: 510.52 E-value: 3.30e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYP--DYEGQIFLEGKEVRFRNPREAQENGI 89
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELDLVPNLSSAENIFLSREPVNEFGVIEYQKMFEQASKLFSKLGVNIDPKTK-VEDLSTSQQQMVAIAKALSLDA 168
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 169 KIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVRLMVGR 248
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 249 SIDQFFIKERATITDEIFRVEGIKLWSLD-RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTEGKVFI 327
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCWDVInPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 328 GGKEIKIHSPRDAVKNGIGLVPEDRKTAGLILQMSVLHNITLpSVVMKLIVRkfGLIDSQLEKEIVRSFIEKLNIKTPSP 407
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITL-SVLKSFCFK--MRIDAAAELQIIGSAIQRLKVKTASP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 408 YQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMS 487
Cdd:TIGR02633 398 FLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIG 477
|
490 500
....*....|....*....|...
gi 490181991 488 EGRKTAEFLREEVTEEDLLKAAI 510
Cdd:TIGR02633 478 EGKLKGDFVNHALTQEQVLAAAL 500
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-511 |
3.04e-170 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 490.84 E-value: 3.04e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGI 89
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELDLVPNLSSAENIFLSREPVNEF---GVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSL 166
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKKVcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 167 DAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVRLMV 246
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 247 GRSIDQFFIKERATI----TDEIFRVEGIKlwSLDRKKllVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTE 322
Cdd:PRK09700 243 GRELQNRFNAMKENVsnlaHETVFEVRNVT--SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-RAG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 323 GKVFIGGKEIKIHSPRDAVKNGIGLVPEDRKTAGLILQMSVLHNITL-PSVVMKLIVRKFGLIDSQLEKEIVRSFIEKLN 401
Cdd:PRK09700 318 GEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAIsRSLKDGGYKGAMGLFHEVDEQRTAENQRELLA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 402 IKTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSD 481
Cdd:PRK09700 398 LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCD 477
|
490 500 510
....*....|....*....|....*....|.
gi 490181991 482 RILVMSEGRKTAEFL-REEVTEEDLLKAAIP 511
Cdd:PRK09700 478 RIAVFCEGRLTQILTnRDDMSEEEIMAWALP 508
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-509 |
4.58e-159 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 461.51 E-value: 4.58e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 16 RNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIALIPQE 95
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 96 LDLVPNLSSAENIFLSREPVNEFgVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDE 175
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGM-FVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 176 PTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVRLMVGRSIDQFFI 255
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 256 KERATITDEIFRVEGikLWSLDRKKllVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIH 335
Cdd:PRK10982 241 DKENKPGEVILEVRN--LTSLRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-KSAGTITLHGKKINNH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 336 SPRDAVKNGIGLVPEDRKTAGLILQMSVLHNITLPSvvMKLIVRKFGLIDSQLEKEIVRSFIEKLNIKTPSPYQIVENLS 415
Cdd:PRK10982 316 NANEAINHGFALVTEERRSTGIYAYLDIGFNSLISN--IRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 416 GGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEF 495
Cdd:PRK10982 394 GGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIV 473
|
490
....*....|....
gi 490181991 496 LREEVTEEDLLKAA 509
Cdd:PRK10982 474 DTKTTTQNEILRLA 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-509 |
8.50e-132 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 392.49 E-value: 8.50e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 2 MLNTEKEREVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNP 81
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 82 REAQENGIALIPQELDLVPNLSSAENIFlsrepvneFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIA 161
Cdd:PRK15439 81 AKAHQLGIYLVPQEPLLFPNLSVKENIL--------FGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 162 KALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKL 241
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 242 VRLMVGRSIDQffikeRATitdeifrvEGIKLW----------SLDRKKLLVDD--------VSFYVRKGEVLGIYGLVG 303
Cdd:PRK15439 233 IQAITPAAREK-----SLS--------ASQKLWlelpgnrrqqAAGAPVLTVEDltgegfrnISLEVRAGEILGLAGVVG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 304 AGRTELLEAIFGAHPGRTeGKVFIGGKEIKIHSPRDAVKNGIGLVPEDRKTAGLILQMSVLHNitlpsvVMKLIVRKFGL 383
Cdd:PRK15439 300 AGRTELAETLYGLRPARG-GRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWN------VCALTHNRRGF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 384 -IDSQLEKEIVRSFIEKLNIKTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS 462
Cdd:PRK15439 373 wIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 490181991 463 GMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLKAA 509
Cdd:PRK15439 453 NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLA 499
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-230 |
4.66e-85 |
|
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: 260.05 E-value: 4.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIALI 92
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQeldlvpnlssaeniflsrepvnefgvieyqkmfeqasklfsklgvnidpktkvedLSTSQQQMVAIAKALSLDAKIII 172
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 173 MDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGE 230
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
263-490 |
1.49e-84 |
|
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: 259.29 E-value: 1.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 263 DEIFRVEGIKLwsldrkKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVK 342
Cdd:cd03215 2 EPVLEVRGLSV------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-PASGEITLDGKPVTRRSPRDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 343 NGIGLVPEDRKTAGLILQMSVLHNITLPSVvmklivrkfglidsqlekeivrsfieklniktpspyqivenLSGGNQQKV 422
Cdd:cd03215 75 AGIAYVPEDRKREGLVLDLSVAENIALSSL-----------------------------------------LSGGNQQKV 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 423 VLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-512 |
5.39e-76 |
|
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: 248.66 E-value: 5.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPD---YEGQIFLEGKEVRFRNPREA 84
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 85 QENgIALIPQELD--LVPnLSSAENIflsREPVnEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAK 162
Cdd:COG1123 82 GRR-IGMVFQDPMtqLNP-VTVGDQI---AEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 163 ALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE-FDHDK 240
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEiLAAPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 241 LVRLMVGRSIDQFFIKERATITDEIFRVEGIK---LWSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAH 317
Cdd:COG1123 236 ALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSkryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 318 PgRTEGKVFIGGKEIKIHSPRDavkngiglVPEDRKTAGLILQ---------MSVLHNITLPsvvmkliVRKFGLIDSQL 388
Cdd:COG1123 316 R-PTSGSILFDGKDLTKLSRRS--------LRELRRRVQMVFQdpysslnprMTVGDIIAEP-------LRLHGLLSRAE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 389 EKEIVRSFIEKLNIKTP----SPYQivenLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-G 463
Cdd:COG1123 380 RRERVAELLERVGLPPDladrYPHE----LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElG 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 464 MGVVMVSSELPEILAMSDRILVMSEGR-----KTAEFL---REEVTEEdLLkAAIPR 512
Cdd:COG1123 456 LTYLFISHDLAVVRYIADRVAVMYDGRivedgPTEEVFanpQHPYTRA-LL-AAVPS 510
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-247 |
1.55e-56 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 196.39 E-value: 1.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKtfPGViaVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGI 89
Cdd:COG1129 254 EVVLEVEGLSV--GGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIP---QELDLVPNLSSAENIFLSR-EPVNEFGVIEYQKMFEQASKLFSKLGVNI-DPKTKVEDLSTSQQQMVAIAKAL 164
Cdd:COG1129 330 AYVPedrKGEGLVLDLSIRENITLASlDRLSRGGLLDRRRERALAEEYIKRLRIKTpSPEQPVGNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 165 SLDAKIIIMDEPTSAI---GKREteqLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKL 241
Cdd:COG1129 410 ATDPKVLILDEPTRGIdvgAKAE---IYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEEAI 486
|
....*.
gi 490181991 242 VRLMVG 247
Cdd:COG1129 487 MAAATG 492
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-236 |
3.55e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 185.27 E-value: 3.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQENgIALI 92
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENI-FLSRepVNEFGVIEYQKMFEQASKLFsklGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKII 171
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFAR--LYGLPRKEARERIDELLELF---GLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 172 IMDEPTS---AIGKREteqLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEF 236
Cdd:COG1131 154 ILDEPTSgldPEARRE---LWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-236 |
3.12e-53 |
|
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: 180.44 E-value: 3.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQENgIAL 91
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQ-IGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENI-FLSRepVNEFGVIEYQKMFEQASKLFsklGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKI 170
Cdd:COG4555 79 LPDERGLYDRLTVRENIrYFAE--LYGLFDEELKKRIEELIELL---GLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 171 IIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEF 236
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-242 |
9.85e-51 |
|
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: 173.39 E-value: 9.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIALI 92
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENI-----FLSREPVNEFGVI-EYQKMFEQASKLFSKLGvnIDPK--TKVEDLSTSQQQMVAIAKAL 164
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqARTGSGLLLARARrEEREARERAEELLERVG--LADLadRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 165 SLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLV 242
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-226 |
8.57e-50 |
|
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: 168.73 E-value: 8.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrFRNPREAQENgIALI 92
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRR-IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIflsrepvnefgvieyqkmfeqasklfsklgvnidpktkveDLSTSQQQMVAIAKALSLDAKIII 172
Cdd:cd03230 79 PEEPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 173 MDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-243 |
2.02e-47 |
|
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: 165.21 E-value: 2.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGI 89
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELDLVPNLSSAENI---FLSREPVNEFGVI--------EYQKMFEQASKLFSKLGvnIDPK--TKVEDLSTSQQQ 156
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVlvaAHARLGRGLLAALlrlprarrEEREARERAEELLERVG--LADRadEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 157 MVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
....*...
gi 490181991 236 FDHDKLVR 243
Cdd:COG0411 240 VRADPRVI 247
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-235 |
3.66e-47 |
|
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: 171.62 E-value: 3.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 5 TEKEREVLLEARNITKTFP-----GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFR 79
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 80 NPREAQENG--IALIPQ--ELDLVPNLSSAENIflsREPVNEFGVIEYQKMFEQASKLFSKLGVNidpkTKVED-----L 150
Cdd:COG1123 333 SRRSLRELRrrVQMVFQdpYSSLNPRMTVGDII---AEPLRLHGLLSRAERRERVAELLERVGLP----PDLADrypheL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 151 STSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVG 229
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
....*.
gi 490181991 230 EGPIEE 235
Cdd:COG1123 486 DGPTEE 491
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-239 |
7.99e-46 |
|
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: 159.91 E-value: 7.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIALI 92
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFLSREPVNEFGV-IEYQKMFEqaskLFSKLGVNIdpKTKVEDLSTSQQQMVAIAKALSLDAKII 171
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRkARLERVYE----LFPRLKERR--KQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 172 IMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHD 239
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-243 |
1.30e-45 |
|
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: 159.42 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIAL 91
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQ-------------ELDLVPnlssaENIFLSREpvnefgviEYQKMFEQASKLfsklgVNIDP--KTKVEDLSTSQQQ 156
Cdd:COG1122 80 VFQnpddqlfaptveeDVAFGP-----ENLGLPRE--------EIRERVEEALEL-----VGLEHlaDRPPHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 157 MVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEF 236
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
....*....
gi 490181991 237 --DHDKLVR 243
Cdd:COG1122 222 fsDYELLEE 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-244 |
1.70e-44 |
|
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: 156.96 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPRE--AQENGI 89
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELDLVPNLSSAENI---FLSREP-----VNEFGVIEYQKMFEQASKlfsklgVNIDPK--TKVEDLSTSQQQMVA 159
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgRLGRRStwrslFGLFPKEEKQRALAALER------VGLLDKayQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 160 IAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDH 238
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
....*.
gi 490181991 239 DKLVRL 244
Cdd:cd03256 235 EVLDEI 240
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-226 |
2.76e-44 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 155.73 E-value: 2.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEV---------RFR 79
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsekelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 80 NpreaqeNGIALIPQELDLVPNLSSAENI----FLSREPVNEfgvieyqkMFEQASKLFSKLGVNIDPKTKVEDLSTSQQ 155
Cdd:cd03255 81 R------RHIGFVFQSFNLLPDLTALENVelplLLAGVPKKE--------RRERAEELLERVGLGDRLNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 156 QMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRlEEIFEIADRVVVMRDGR 226
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-226 |
6.59e-44 |
|
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: 154.55 E-value: 6.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 14 EARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIAL 91
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQ-----------ELDLVpnlSSAENIFLSREpvnefgvieyqKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAI 160
Cdd:cd03225 80 VFQnpddqffgptvEEEVA---FGLENLGLPEE-----------EIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 161 AKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-235 |
2.40e-43 |
|
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: 154.43 E-value: 2.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPRE-AQEngIA 90
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElARR--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVPNLSSAENIFLSREPvnefgvieYQKMFEQASK--------LFSKLGvnIDPK--TKVEDLSTSQQQMVAI 160
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGRYP--------HLGLFGRPSAedreaveeALERTG--LEHLadRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 161 AKALSLDAKIIIMDEPTSA--IGKRetEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHldLAHQ--LEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-226 |
1.76e-42 |
|
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: 150.75 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPReaqENGIALI 92
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENI-F-LSREPVNEfgvieyQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKI 170
Cdd:cd03259 78 FQDYALFPHLTVAENIaFgLKLRGVPK------AEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 171 IIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-244 |
4.44e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 150.59 E-value: 4.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQE--NG 88
Cdd:COG3638 2 MLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQELDLVPNLSSAENI---FLSREPV-----NEFGVIEYQKMFEQASKlfsklgVNIDPK--TKVEDLSTSQQQMV 158
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagRLGRTSTwrsllGLFPPEDRERALEALER------VGLADKayQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 159 AIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFD 237
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELT 235
|
....*..
gi 490181991 238 HDKLVRL 244
Cdd:COG3638 236 DAVLREI 242
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-230 |
6.74e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.42 E-value: 6.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFP----GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEV--------- 76
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 77 RFRNpreaqENgIALIPQELDLVPNLSSAENI----FLSREPVNEfgvieyqkMFEQASKLFSKLGvnIDPKT--KVEDL 150
Cdd:COG1136 82 RLRR-----RH-IGFVFQFFNLLPELTALENValplLLAGVSRKE--------RRERARELLERVG--LGDRLdhRPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 151 STSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRlEEIFEIADRVVVMRDGRKVG 229
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGRIVS 224
|
.
gi 490181991 230 E 230
Cdd:COG1136 225 D 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-243 |
1.55e-41 |
|
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: 148.98 E-value: 1.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGI 89
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELDLVPNLSSAENIFLSREPVNEFGVIE--YQKMFEqaskLFSKLGVNIdpKTKVEDLSTSQQQMVAIAKALSLD 167
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRadLERVYE----LFPRLKERR--RQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 168 AKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVR 243
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVR 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-231 |
2.08e-41 |
|
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: 148.42 E-value: 2.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQEN 87
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 G--IALIPQE----LDlvPNLSSAENIflsREPVNEFGVIEYQKMFEQASKLFSKlGVNIDPktKVED-----LSTSQQQ 156
Cdd:cd03257 81 RkeIQMVFQDpmssLN--PRMTIGEQI---AEPLRIHGKLSKKEARKEAVLLLLV-GVGLPE--EVLNrypheLSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 157 MVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-247 |
3.58e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 154.80 E-value: 3.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 1 MM------LNTEKER----EVLLEARNIT-KTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQI 69
Cdd:COG3845 236 LMvgrevlLRVEKAPaepgEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 70 FLEGKEVRFRNPREAQENGIALIPQE---LDLVPNLSSAENIFLSR---EPVNEFGVIEYQKMFEQASKLFSKLGVNI-D 142
Cdd:COG3845 316 RLDGEDITGLSPRERRRLGVAYIPEDrlgRGLVPDMSVAENLILGRyrrPPFSRGGFLDRKAIRAFAEELIEEFDVRTpG 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 143 PKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPT-----SAIgkretEQLFNIIRSLKNEGKSVIYISHRLEEIFEIAD 217
Cdd:COG3845 396 PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTrgldvGAI-----EFIHQRLLELRDAGAAVLLISEDLDEILALSD 470
|
250 260 270
....*....|....*....|....*....|
gi 490181991 218 RVVVMRDGRKVGEGPIEEFDHDKLVRLMVG 247
Cdd:COG3845 471 RIAVMYEGRIVGEVPAAEATREEIGLLMAG 500
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-226 |
5.27e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 151.02 E-value: 5.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 9 REVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrNPREAQENG 88
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV---TGLPPEKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQELDLVPNLSSAENIflsrepvnEFGvIEYQKMF--EQASKLFSKLG-VNIDP--KTKVEDLSTSQQQMVAIAKA 163
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENV--------AFG-LRMRGVPkaEIRARVAELLElVGLEGlaDRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 164 LSLDAKIIIMDEPTSAIGKRETEQL-FNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMrEELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-226 |
2.05e-40 |
|
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: 143.15 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 14 EARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQENGIALIP 93
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-KLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 94 QeldlvpnlssaeniflsrepvnefgvieyqkmfeqasklfsklgvnidpktkvedLSTSQQQMVAIAKALSLDAKIIIM 173
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490181991 174 DEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-226 |
2.55e-40 |
|
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: 143.73 E-value: 2.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITktfpGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGI 89
Cdd:cd03215 2 EPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIP---QELDLVPNLSSAENIFLSRepvnefgvieyqkmfeqaskLFSklGVNidpktkvedlstsqQQMVAIAKALSL 166
Cdd:cd03215 78 AYVPedrKREGLVLDLSVAENIALSS--------------------LLS--GGN--------------QQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 167 DAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-226 |
4.88e-40 |
|
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: 143.10 E-value: 4.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEV-RFRNPREAQENGIAL 91
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENIFLSrepvnefgvieyqkmfeqasklfsklgvnidpktkvedLSTSQQQMVAIAKALSLDAKII 171
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 172 IMDEPTSAIGKRETEQLFNIIRSLK-NEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-235 |
1.27e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 145.64 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPReaqenGIALI 92
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR-----RIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIF-------LSREPVNefgvieyqkmfEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALS 165
Cdd:COG4152 77 PEERGLYPKMKVGEQLVylarlkgLSKAEAK-----------RRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 166 LDAKIIIMDEPTS---AIGkreTEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:COG4152 146 HDPELLILDEPFSgldPVN---VELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-490 |
1.98e-39 |
|
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: 150.22 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKS----TLMKILAGVYPDYEGQIFLEGKEVRFRNPRE 83
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 84 AQE---NGIALIPQEldlvPnLSS-----------AENIFL----SREPVNEfGVIEyqkMFEQasklfsklgVNI-DPK 144
Cdd:COG4172 86 LRRirgNRIAMIFQE----P-MTSlnplhtigkqiAEVLRLhrglSGAAARA-RALE---LLER---------VGIpDPE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 145 TKVED----LSTSQQQMVAIAKALSLDAKIIIMDEPTSA----IGKreteQLFNIIRSLKNE-GKSVIYISHRLEEIFEI 215
Cdd:COG4172 148 RRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTAldvtVQA----QILDLLKDLQRElGMALLLITHDLGVVRRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 216 ADRVVVMRDGRKVGEGPIEEF----DHDKLVRLMvgRSIDQFFIKERATITDEIFRVEGIKLWSLDRKKLL--------- 282
Cdd:COG4172 224 ADRVAVMRQGEIVEQGPTAELfaapQHPYTRKLL--AAEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGLFrrtvghvka 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgrTEGKVFIGGKEIKIHSPRD--AVKNGIGLVPED-------RK 353
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP--SEGEIRFDGQDLDGLSRRAlrPLRRRMQVVFQDpfgslspRM 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 354 TAGLIlqmsvlhnITLPsvvmkLIVRKFGLIDSQLEKEIVRSFIE-KLnikTPS-----PYQivenLSGGNQQKVVLAKW 427
Cdd:COG4172 380 TVGQI--------IAEG-----LRVHGPGLSAAERRARVAEALEEvGL---DPAarhryPHE----FSGGQRQRIAIARA 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 428 LAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG4172 440 LILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-244 |
2.10e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 143.31 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPReaqengI 89
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELDLVPNL-SSAENIFLS----------------REPVNEfgVIEYQKMFEQASKLFSklgvnidpktkveDLST 152
Cdd:COG1121 78 GYVPQRAEVDWDFpITVRDVVLMgrygrrglfrrpsradREAVDE--ALERVGLEDLADRPIG-------------ELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 153 SQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMrDGRKVGEGP 232
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGP 221
|
250
....*....|...
gi 490181991 233 IEE-FDHDKLVRL 244
Cdd:COG1121 222 PEEvLTPENLSRA 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-236 |
3.58e-39 |
|
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: 144.81 E-value: 3.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDY---EGQIFLEGKEVRFRNPREA 84
Cdd:COG0444 1 LLEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 85 QE---NGIALIPQE----LDlvPNLSSAENIflsREPVNEFGVIEYQKMFEQASKLFSKlgVNIDPKTKVED-----LST 152
Cdd:COG0444 81 RKirgREIQMIFQDpmtsLN--PVMTVGDQI---AEPLRIHGGLSKAEARERAIELLER--VGLPDPERRLDrypheLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 153 SQQQMVAIAKALSLDAKIIIMDEPTSA----IGKreteQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRK 227
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTAldvtIQA----QILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
....*....
gi 490181991 228 VGEGPIEEF 236
Cdd:COG0444 230 VEEGPVEEL 238
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-231 |
3.76e-38 |
|
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: 139.04 E-value: 3.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTF----PGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQEN 87
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 gIALIPQELDLVPNLSSAENI-FLSRepvneFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSL 166
Cdd:cd03266 80 -LGFVSDSTGLYDRLTARENLeYFAG-----LYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 167 DAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-244 |
5.28e-38 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 139.74 E-value: 5.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQE--NG 88
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQELDLVPNLSSAENI---FLSREP-----VNEFGVIEYQKMFEqaskLFSKLGVNIDPKTKVEDLSTSQQQMVAI 160
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgRLGYKPtwrslLGRFSEEDKERALS----ALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 161 AKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHD 239
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
....*
gi 490181991 240 KLVRL 244
Cdd:TIGR02315 237 VLRHI 241
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-235 |
6.95e-38 |
|
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: 138.41 E-value: 6.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQENgIA 90
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQS-LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVPNLSSAENI-FLSR---EPVNEfgvieyqkMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSL 166
Cdd:cd03263 79 YCPQFDALFDELTVREHLrFYARlkgLPKSE--------IKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 167 DAKIIIMDEPTS---AIGKReteQLFNIIRSLKnEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:cd03263 151 GPSVLLLDEPTSgldPASRR---AIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
284-522 |
1.09e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.78 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 284 DDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDRktaGLILQMSV 363
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQ-PDSGEILLDGEPVRFRSPRDAQAAGIAIIHQEL---NLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 364 LHNITLPSVVmklivRKFGLIDSQLEKEIVRSFIEKLNIKTPsPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRG 443
Cdd:COG1129 97 AENIFLGREP-----RRGGLIDWRAMRRRARELLARLGLDID-PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 444 IDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLKAAIPRSVKVETTQRE 522
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRELEDLFPKRA 249
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-234 |
1.82e-37 |
|
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: 137.22 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPReaqeng 88
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQELDLVPNLSSAENIFLSREPVnefGVIEYQKMfEQASKLFSKLGVnidpkTKVED-----LSTSQQQMVAIAKA 163
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQ---GVPKAEAR-ERAEELLELVGL-----SGFENayphqLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 164 LSLDAKIIIMDEPTSA--IGKRET--EQLFNIIRSlknEGKSVIYISHRLEEIFEIADRVVVM--RDGRKVGEGPIE 234
Cdd:cd03293 146 LAVDPDVLLLDEPFSAldALTREQlqEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEVD 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-231 |
2.01e-37 |
|
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: 137.03 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFrnpreAQENGIALI 92
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAEN-IFLSRepvneFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKII 171
Cdd:cd03269 76 PEERGLYPKMKVIDQlVYLAQ-----LKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 172 IMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-231 |
3.25e-37 |
|
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: 135.26 E-value: 3.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 14 EARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPRE-AQEngIALI 92
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElARK--IAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVpNLSSaenifLSREPVNEfgvieyqkmfeqasklfsklgvnidpktkvedLSTSQQQMVAIAKALSLDAKIII 172
Cdd:cd03214 79 PQALELL-GLAH-----LADRPFNE--------------------------------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 173 MDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-178 |
6.45e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 133.54 E-value: 6.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRnPREAQENGIALIPQELDLVPNLSSAEN 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD-ERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 108 IFLSRepvnEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVED----LSTSQQQMVAIAKALSLDAKIIIMDEPTS 178
Cdd:pfam00005 80 LRLGL----LLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-226 |
1.57e-36 |
|
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: 133.28 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIA 90
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQEldlvPNL---SSAENIflsrepvnefgvieyqkmfeqasklfsklgvnidpktkvedLSTSQQQMVAIAKALSLD 167
Cdd:cd03228 80 YVPQD----PFLfsgTIRENI-----------------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 168 AKIIIMDEPTSAIgKRETEQLfnIIRSLKN--EGKSVIYISHRLEEIfEIADRVVVMRDGR 226
Cdd:cd03228 115 PPILILDEATSAL-DPETEAL--ILEALRAlaKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-235 |
3.06e-36 |
|
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: 143.05 E-value: 3.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIA 90
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVpNLSSAENIFLSREPVNEFGVIEyqkmfeqASKLfsklgVNID------PK---TKVED----LSTSQQQM 157
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLGDPDATDEEIIE-------AARL-----AGLHdfiealPMgydTVVGEggsnLSGGQRQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 158 VAIAKALSLDAKIIIMDEPTSAIGKrETEQLfnIIRSLKN--EGKSVIYISHRLEEIfEIADRVVVMRDGRKVGEGPIEE 235
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDA-ETEAI--ILENLRRllKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEE 695
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-231 |
6.19e-36 |
|
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: 132.73 E-value: 6.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEvrFRNPREAQENGIALI 92
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS--YQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 pQELDLVPNLSSAENIFLSRepvnefgvIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIII 172
Cdd:cd03268 79 -EAPGFYPNLTARENLRLLA--------RLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 173 MDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-238 |
8.33e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.43 E-value: 8.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAG-VYPDyEGQIFLEGKEVrFRNpREAQENGIAL 91
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPD-SGRIVLNGRDL-FTN-LPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENI--FLSREPVNEfGVIEyqkmfEQASKLFSKLGVnidpkTKVED-----LSTSQQQMVAIAKAL 164
Cdd:COG1118 80 VFQHYALFPHMTVAENIafGLRVRPPSK-AEIR-----ARVEELLELVQL-----EGLADrypsqLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 165 SLDAKIIIMDEPTSAIG---KRETEQlfNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE-FDH 238
Cdd:COG1118 149 AVEPEVLLLDEPFGALDakvRKELRR--WLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEvYDR 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-243 |
9.95e-36 |
|
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: 133.01 E-value: 9.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQE--NGIA 90
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVPNLSSAENIFLsrePVNEFGVIEYQKMFEQASklfSKLG-VNIDP--KTKVEDLSTSQQQMVAIAKALSLD 167
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF---PLREHTRLSEEEIREIVL---EKLEaVGLRGaeDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 168 AKIIIMDEPTSA---IGKRETEQLfniIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDH--DKL 241
Cdd:cd03261 155 PELLLYDEPTAGldpIASGVIDDL---IRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDPL 231
|
..
gi 490181991 242 VR 243
Cdd:cd03261 232 VR 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-226 |
2.60e-35 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 131.06 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQEngIAL 91
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENI-FLSR---EPVNEfgvieyqkmfEQASKLFSKLGVnidpkTKVED-----LSTSQQQMVAIAK 162
Cdd:COG4133 80 LGHADGLKPELTVRENLrFWAAlygLRADR----------EAIDEALEAVGL-----AGLADlpvrqLSAGQKRRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 163 ALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFeiADRVVVMRDGR 226
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-249 |
6.93e-35 |
|
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: 130.88 E-value: 6.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGV-IAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIAL 91
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK-IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENIFLsrepVNEFGVIEYQKMFEQASKLFSKlgVNIDPKTKVE----DLSTSQQQMVAIAKALSLD 167
Cdd:cd03295 80 VIQQIGLFPHMTVEENIAL----VPKLLKWPKEKIRERADELLAL--VGLDPAEFADryphELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 168 AKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEF---DHDKLVR 243
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIlrsPANDFVA 233
|
....*.
gi 490181991 244 LMVGRS 249
Cdd:cd03295 234 EFVGAD 239
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-254 |
1.07e-34 |
|
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: 130.48 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 9 REVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAG-VYPDyEGQIFLEGKEVRFRNPREAQE- 86
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPD-SGEILVDGQDITGLSEKELYEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 87 ---------NGiALipqeLDlvpNLSSAENIFLsrePVNEFGVIEYQKMFEQASKlfsKLG-VNIDpktKVED-----LS 151
Cdd:COG1127 81 rrrigmlfqGG-AL----FD---SLTVFENVAF---PLREHTDLSEAEIRELVLE---KLElVGLP---GAADkmpseLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 152 TSQQQMVAIAKALSLDAKIIIMDEPTS---AIGKRETEQLfniIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRK 227
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAgldPITSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
250 260
....*....|....*....|....*....
gi 490181991 228 VGEGPIEEFDH--DKLVRlmvgrsidQFF 254
Cdd:COG1127 221 IAEGTPEELLAsdDPWVR--------QFL 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
279-505 |
4.74e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.64 E-value: 4.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPrdAVKNGIGLVPEDrktAGLI 358
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR-PTSGEVRVLGEDVARDPA--EVRRRIGYVPQE---PALY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQMSVLHNItlpsvvmKLIVRKFGLiDSQLEKEIVRSFIEKLNIkTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLD 438
Cdd:COG1131 86 PDLTVRENL-------RFFARLYGL-PRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 439 EPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDL 505
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-225 |
1.19e-33 |
|
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: 126.60 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 14 EARNITKTFPGVI-AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEvrfRNPREAQENgIALI 92
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKS-IGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDlvpnlssaENIFlsREPVNE---FGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAK 169
Cdd:cd03226 77 MQDVD--------YQLF--TDSVREellLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 170 IIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDG 225
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-498 |
1.57e-33 |
|
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: 133.39 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGV--YPDYEGQIFL--------EGKEVRFRNPR 82
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 83 EAQENGIALIPQELDLVpNLSSAEN--------IFLSREpvneFGVIEYQKMFEQASKLFSKLG----------VNIDPK 144
Cdd:TIGR03269 81 PCPVCGGTLEPEEVDFW-NLSDKLRrrirkriaIMLQRT----FALYGDDTVLDNVLEALEEIGyegkeavgraVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 145 TKVE--------DLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEI 215
Cdd:TIGR03269 156 VQLShrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 216 ADRVVVMRDGRKVGEGPIEEfdhdklvrlMVGRSIDQFFIKERAT---ITDEIFRVEGIK--LWSLDRKKL-LVDDVSFY 289
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDE---------VVAVFMEGVSEVEKECeveVGEPIIKVRNVSkrYISVDRGVVkAVDNVSLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 290 VRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVF--IGGKEIKIHSP----RDAVKNGIGLVPEDRktaGLILQMSV 363
Cdd:TIGR03269 307 VKEGEIFGIVGTSGAGKTTLSKIIAGVLE-PTSGEVNvrVGDEWVDMTKPgpdgRGRAKRYIGILHQEY---DLYPHRTV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 364 LHNIT------LPS--VVMKLIvrkFGLIDSQLEKEIVRSFIEKLniktpsPYQivenLSGGNQQKVVLAKWLAIKPKVL 435
Cdd:TIGR03269 383 LDNLTeaigleLPDelARMKAV---ITLKMVGFDEEKAEEILDKY------PDE----LSEGERHRVALAQVLIKEPRIV 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 436 LLDEPTRGID----VNAKSEIYKLISEMavsGMGVVMVSSELPEILAMSDRILVMSEGR-----KTAEFLRE 498
Cdd:TIGR03269 450 ILDEPTGTMDpitkVDVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKivkigDPEEIVEE 518
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-231 |
2.51e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 125.72 E-value: 2.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 14 EARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPReaqengIALIP 93
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 94 QELDLVPN--LSSAENIFLSREPVNEFGVIEYQKMFEQASKLFSKLGVnidpkTKVED-----LSTSQQQMVAIAKALSL 166
Cdd:cd03235 75 QRRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGL-----SELADrqigeLSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 167 DAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMrDGRKVGEG 231
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
13-226 |
2.72e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.42 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrNPREAQENGIALI 92
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENI-F------LSREpvnefgviEYQKMFEQASKLfsklgVNIDP--KTKVEDLSTSQQQMVAIAKA 163
Cdd:COG3839 81 FQSYALYPHMTVYENIaFplklrkVPKA--------EIDRRVREAAEL-----LGLEDllDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 164 LSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-235 |
2.76e-33 |
|
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: 126.19 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 23 PGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRnPREAQENGIALIPQELDLVPNl 102
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 103 SSAENIFLSREPVNEFGVIEYQKMFeQASKLFSKL--GVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAI 180
Cdd:cd03254 92 TIMENIRLGRPNATDEEVIEAAKEA-GAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 181 GKrETEQLF-NIIRSLkNEGKSVIYISHRLEEIFEiADRVVVMRDGRKVGEGPIEE 235
Cdd:cd03254 171 DT-ETEKLIqEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDE 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-235 |
2.83e-33 |
|
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: 126.54 E-value: 2.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGV-YPDyEGQIFLEGKEVRFRNPRE--A 84
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPT-SGSVLVDGTDLTLLSGKElrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 85 QENGIALIPQELDLVPNLSSAENIFLSREpvnefgvIEYQKMFEQASK---LFSKLGVNIDPKTKVEDLSTSQQQMVAIA 161
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLE-------IAGVPKAEIEERvleLLELVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 162 KALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-226 |
3.15e-33 |
|
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: 125.44 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrNPREAQENGIALI 92
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFLSREpVNEFGVIEYQKMFEQASKLfskLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIII 172
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLK-LRKVPKDEIDERVREVAEL---LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 173 MDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
283-503 |
3.63e-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: 3.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDRktaGLILQMS 362
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-PRSGSIRFDGRDITGLPPHERARAGIGYVPEGR---RIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNItlpsvVMKLIVRKFGLIDSQLEkEIVRSF---IEKLNiktpspyQIVENLSGGNQQKVVLAKWLAIKPKVLLLDE 439
Cdd:cd03224 92 VEENL-----LLGAYARRRAKRKARLE-RVYELFprlKERRK-------QLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 440 PTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEE 503
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-235 |
5.83e-33 |
|
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: 132.19 E-value: 5.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIAL 91
Cdd:COG4988 337 IELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQElDLVPNLSSAENIFLSREPVNEfgvieyQKMfEQASKLfsklgVNID------PK---TKVED----LSTSQQQMV 158
Cdd:COG4988 416 VPQN-PYLFAGTIRENLRLGRPDASD------EEL-EAALEA-----AGLDefvaalPDgldTPLGEggrgLSGGQAQRL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 159 AIAKALSLDAKIIIMDEPTSAIGkRETEQ-LFNIIRSLKnEGKSVIYISHRLEEIfEIADRVVVMRDGRKVGEGPIEE 235
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLD-AETEAeILQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEE 557
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
284-518 |
9.89e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.92 E-value: 9.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 284 DDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDRKtagLILQMS 362
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLyQP--DSGEILIDGKPVRIRSPRDAIALGIGMVHQHFM---LVPNLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNITL---PsvvmklivRKFGLIDSQLEKEIVRSFIEKLNIKTPsPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDE 439
Cdd:COG3845 97 VAENIVLgleP--------TKGGRLDRKAARARIRELSERYGLDVD-PDAKVEDLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 440 PTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLKAAIPRSVKVET 518
Cdd:COG3845 168 PTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGREVLLRV 246
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-243 |
1.87e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 131.06 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIALIPQELDLVpNLSSAE 106
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-IGVVPQDTFLF-SGTIRE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 107 NIFLSREPVNEFGVIEyqkmfeqASKLfsklgVNID------PK---TKVED----LSTSQQQMVAIAKALSLDAKIIIM 173
Cdd:COG1132 433 NIRYGRPDATDEEVEE-------AAKA-----AQAHefiealPDgydTVVGErgvnLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 174 DEPTSAIGkRETEQLfnIIRSLKN--EGKSVIYISHRLEEIfEIADRVVVMRDGRKVGEGPieefdHDKLVR 243
Cdd:COG1132 501 DEATSALD-TETEAL--IQEALERlmKGRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGT-----HEELLA 563
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-235 |
4.99e-32 |
|
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: 122.83 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFpGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPreaQENGIALI 92
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIflsrepvnEFGV----IEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDA 168
Cdd:cd03299 77 PQNYALFPHMTVYKNI--------AYGLkkrkVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 169 KIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
13-245 |
1.44e-31 |
|
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: 121.48 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIALI 92
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFLSREPVNEFGvieyQKMFEQASKLFSKLGVNIDPKTKveDLSTSQQQMVAIAKALSLDAKIII 172
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRS----RKIPDEIYELFPVLKEMLGRRGG--DLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 173 MDEPTSAIGKRETEQLFNIIRSLKNEGK-SVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVRLM 245
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYL 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-238 |
1.48e-31 |
|
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: 121.68 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQengIALI 92
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN---VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIflsrepvnEFGvIEYQKMFEQASKLfsklgvniDPKTKVED-----------------LSTSQQ 155
Cdd:cd03296 80 FQHYALFRHMTVFDNV--------AFG-LRVKPRSERPPEA--------EIRAKVHEllklvqldwladrypaqLSGGQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 156 QMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGR--KVGEgP 232
Cdd:cd03296 143 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRieQVGT-P 221
|
....*.
gi 490181991 233 IEEFDH 238
Cdd:cd03296 222 DEVYDH 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
278-503 |
2.30e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.35 E-value: 2.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 278 RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRdavkngIGLVPEdRKTAGL 357
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-PTSGTVRLFGKPPRRARRR------IGYVPQ-RAEVDW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQMSVLhnitlpSVVMKLIVRKFGLID--SQLEKEIVRSFIEKLNIktpSPY---QIVEnLSGGNQQKVVLAKWLAIKP 432
Cdd:COG1121 89 DFPITVR------DVVLMGRYGRRGLFRrpSRADREAVDEALERVGL---EDLadrPIGE-LSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 433 KVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR----KTAEFLREEVTEE 503
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLvahgPPEEVLTPENLSR 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-236 |
2.52e-31 |
|
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: 120.75 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDY-----EGQIFLEGKEVRFRN-PREAQE 86
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 87 NGIALIPQELDLVPnLSSAENIFLsrePVNEFGVIEYQKMFEQASKLFSKLGV--NIDPKTKVEDLSTSQQQMVAIAKAL 164
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAY---GLRLHGIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 165 SLDAKIIIMDEPTSA---IGKRETEQLfniIRSLKNEgKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEF 236
Cdd:cd03260 157 ANEPEVLLLDEPTSAldpISTAKIEEL---IAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
283-509 |
4.03e-31 |
|
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: 120.47 E-value: 4.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDRktaGLILQMS 362
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-PRSGSIRFDGEDITGLPPHRIARLGIGYVPEGR---RIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNITLPSvvmkLIVRKFGLIDSQLEkEIVRSF---IEKLNiktpspyQIVENLSGGNQQKVVLAKWLAIKPKVLLLDE 439
Cdd:COG0410 95 VEENLLLGA----YARRDRAEVRADLE-RVYELFprlKERRR-------QRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 440 PTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLKAA 509
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREA 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-226 |
4.72e-31 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 120.03 E-value: 4.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrNPREAQENGIALI 92
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENI-F---LSREPVNEFG-----VIEYQKMFEQASKlfsklgvnidpktKVEDLSTSQQQMVAIAKA 163
Cdd:cd03300 78 FQNYALFPHLTVFENIaFglrLKKLPKAEIKervaeALDLVQLEGYANR-------------KPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 164 LSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-255 |
5.52e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 121.25 E-value: 5.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 7 KEREVLLEARNITKTFPGV--IAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREA 84
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 85 QENgIALIPQELDlvpnlssaeNIFL--SREPVNEFGV----IEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMV 158
Cdd:PRK13632 82 RKK-IGIIFQNPD---------NQFIgaTVEDDIAFGLenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 159 AIAKALSLDAKIIIMDEPTSAI---GKRETEQlfnIIRSLKNEG-KSVIYISHRLEEIFeIADRVVVMRDGRKVGEG-PI 233
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLdpkGKREIKK---IMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIAQGkPK 227
|
250 260
....*....|....*....|..
gi 490181991 234 EEFDHDKLVRLMvgrSIDQFFI 255
Cdd:PRK13632 228 EILNNKEILEKA---KIDSPFI 246
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
279-505 |
6.59e-31 |
|
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: 119.96 E-value: 6.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGKEIkiHSPRDAVKNGIGLVPEDRktaGL 357
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlKP--DSGSILIDGEDV--RKEPREARRQIGVLPDER---GL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQMSVLHNItlpsvvmKLIVRKFGLIDSQLEKEIVRsFIEKLNIktpSPY--QIVENLSGGNQQKVVLAKWLAIKPKVL 435
Cdd:COG4555 86 YDRLTVRENI-------RYFAELYGLFDEELKKRIEE-LIELLGL---EEFldRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 436 LLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR----KTAEFLREEVTEEDL 505
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKvvaqGSLDELREEIGEENL 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
283-486 |
7.16e-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: 7.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRdavkngIGLVPEdrktaglILQMS 362
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK-PTSGSIRVFGKPLEKERKR------IGYVPQ-------RRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNITLPSVVMKLIVRKFGLID--SQLEKEIVRSFIEKLNIKTPSPYQIVEnLSGGNQQKVVLAKWLAIKPKVLLLDEP 440
Cdd:cd03235 81 RDFPISVRDVVLMGLYGHKGLFRrlSKADKAKVDEALERVGLSELADRQIGE-LSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490181991 441 TRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVM 486
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-441 |
1.71e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 124.41 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 15 ARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEgKEVRfrnpreaqengIALIPQ 94
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR-----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 95 ELDLVPNLSSAENIFLSREPV----------------NEFGVIEYQKMFEQ------------ASKLFSKLGV-NIDPKT 145
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELraleaeleeleaklaePDEDLERLAELQEEfealggweaearAEEILSGLGFpEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 146 KVEDLSTSQQQMVAIAKALSLDAKIIIMDEPT-----SAIGKRETEqlfniirsLKNEGKSVIYISH-R--LEE----IF 213
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTnhldlESIEWLEEF--------LKNYPGTVLVVSHdRyfLDRvatrIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 214 EIADRVVVMRDG------------------------RKVGEgpIEEF-------------------DHDKLVRLMVGRSI 250
Cdd:COG0488 221 ELDRGKLTLYPGnysayleqraerleqeaaayakqqKKIAK--EEEFirrfrakarkakqaqsrikALEKLEREEPPRRD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 251 DQFFIK--ERATITDEIFRVEGIKLwSLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIG 328
Cdd:COG0488 299 KTVEIRfpPPERLGKKVLELEGLSK-SYGDKTLL-DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP-DSGTVKLG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 329 GKeikihsprdaVKngIGLVPEDRKTagLILQMSVLHNITlpsvvmklivrkfGLIDSQLEKEiVRSFIEKLNIKTPSPY 408
Cdd:COG0488 376 ET----------VK--IGYFDQHQEE--LDPDKTVLDELR-------------DGAPGGTEQE-VRGYLGRFLFSGDDAF 427
|
490 500 510
....*....|....*....|....*....|...
gi 490181991 409 QIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPT 441
Cdd:COG0488 428 KPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-231 |
1.79e-30 |
|
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: 118.06 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGeVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQENgIALI 92
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRR-IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSsaeniflSREPVNEFGV---IEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAK 169
Cdd:cd03264 78 PQEFGVYPNFT-------VREFLDYIAWlkgIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 170 IIIMDEPTSAIGKRETEQLFNIIRSLkNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-231 |
2.07e-30 |
|
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: 118.08 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIA 90
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN-IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVpNLSSAENIFLSREPVNEFGVIEyqkmfeqASKLfskLGV----NIDPK---TKVED----LSTSQQQMVA 159
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGAPLADDERILR-------AAEL---AGVtdfvNKHPNgldLQIGErgrgLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 160 IAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKnEGKSVIYISHRLeEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-238 |
6.12e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 120.71 E-value: 6.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 4 NTEKEREVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPre 83
Cdd:PRK11607 11 KTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 84 aQENGIALIPQELDLVPNLSSAENIflsrepvnEFGvIEYQKM--FEQASKLFSKLG-VNID--PKTKVEDLSTSQQQMV 158
Cdd:PRK11607 89 -YQRPINMMFQSYALFPHMTVEQNI--------AFG-LKQDKLpkAEIASRVNEMLGlVHMQefAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 159 AIAKALSLDAKIIIMDEPTSAIGK--RETEQLfNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR--KVGEgPIE 234
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKklRDRMQL-EVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKfvQIGE-PEE 236
|
....
gi 490181991 235 EFDH 238
Cdd:PRK11607 237 IYEH 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-235 |
1.75e-29 |
|
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: 116.97 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 25 VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQE---NGIALIPQELDLVPN 101
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 102 LSSAENIflsrepvnEFGV----IEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPT 177
Cdd:cd03294 117 RTVLENV--------AFGLevqgVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 178 SAIG---KRETEQLFniIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:cd03294 189 SALDpliRREMQDEL--LRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
283-508 |
2.39e-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: 115.51 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHSPRDAVKNgIGLV---PEDRktaglIL 359
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP-TSGEVLVDGKDITKKNLRELRRK-VGLVfqnPDDQ-----LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 360 QMSVLHNITlpsvvmklivrkFGLIDSQLEKE----IVRSFIEKLNI---KTPSPYQivenLSGGNQQKVVLAKWLAIKP 432
Cdd:COG1122 90 APTVEEDVA------------FGPENLGLPREeireRVEEALELVGLehlADRPPHE----LSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 433 KVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEV-TEEDLLKA 508
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVfSDYELLEE 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
278-490 |
4.13e-29 |
|
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: 114.15 E-value: 4.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 278 RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIkihSPRDAVKNGIGLVPEDrktAG 356
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERP--DSGEILIDGRDV---TGVPPERRNIGMVFQD---YA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSVLHNITLPSVVMKLivrkfgliDSQLEKEIVRSFIEKLNIKTP---SPYQivenLSGGNQQKVVLAKWLAIKPK 433
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRGV--------PKAEIRARVRELLELVGLEGLlnrYPHE----LSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 434 VLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
279-490 |
4.26e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 112.88 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKihSPRDAVKNGIGLVPEDrktAGLI 358
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-PDSGEIKVLGKDIK--KEPEEVKRRIGYLPEE---PSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQMSVLHNItlpsvvmklivrkfglidsqlekeivrsfieklniktpspyqiveNLSGGNQQKVVLAKWLAIKPKVLLLD 438
Cdd:cd03230 86 ENLTVRENL---------------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490181991 439 EPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-235 |
5.29e-29 |
|
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: 114.80 E-value: 5.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAG-VYPDYEGQIFLEGKEVRFRNPREAQENg 88
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQELDL-VPNLSSAENIFLSrepvNEFGVIE-YQK----MFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAK 162
Cdd:COG1119 80 IGLVSPALQLrFPRDETVLDVVLS----GFFDSIGlYREptdeQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 163 ALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEE 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
277-490 |
6.12e-29 |
|
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: 113.72 E-value: 6.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGaHPGRTEGKVFIGGKEIKIHSPRDAVKNgIGLV---PEDRk 353
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNG-LLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVfqnPDDQ- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 354 taglILQMSV-------LHNITLPSVVMKLIVR---KFGLIDSQLEKeivrsfieklniktpSPYQivenLSGGNQQKVV 423
Cdd:cd03225 88 ----FFGPTVeeevafgLENLGLPEEEIEERVEealELVGLEGLRDR---------------SPFT----LSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 424 LAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
283-500 |
7.29e-29 |
|
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: 114.07 E-value: 7.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNGIGlvpedRK--TAGLILQ 360
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR-PTSGSVLFDGEDITGLPPHEIARLGIG-----RTfqIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 MSVLHNITLpSVVMKLIVRKFGLIDSQLEKEI---VRSFIEKLNIkTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLL 437
Cdd:cd03219 90 LTVLENVMV-AAQARTGSGLLLARARREEREArerAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 438 DEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEV 500
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-243 |
1.87e-28 |
|
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: 113.02 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIALI 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFLsrepvnefgVIEYQKMF--EQASKLFSKLG-VNIDP--KTKVEDLSTSQQQMVAIAKALSLD 167
Cdd:cd03218 81 PQEASIFRKLTVEENILA---------VLEIRGLSkkEREEKLEELLEeFHITHlrKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 168 AKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVR 243
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
12-236 |
4.29e-28 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 112.01 E-value: 4.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAG-VYPDyEGQIFLEGKEV--RFRNPREAQENg 88
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLlEEPD-SGTITVDGEDLtdSKKDINKLRRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQELDLVPNLSSAENIFLsrepvnefGVIEYQKM-----FEQASKLFSKLG----VNIDPKTkvedLSTSQQQMVA 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTL--------APIKVKKMskaeaEERAMELLERVGladkADAYPAQ----LSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 160 IAKALSLDAKIIIMDEPTSA-----IGkretEQLfNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIE 234
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSAldpelVG----EVL-DVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
|
..
gi 490181991 235 EF 236
Cdd:COG1126 222 EF 223
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
13-291 |
4.46e-28 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 115.13 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQENGIALi 92
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDIT-RLPPQKRDYGIVF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 pQELDLVPNLSSAENIflsrepvnEFGvIEYQKM-----FEQASKLFSKLGVnidpkTKVED-----LSTSQQQMVAIAK 162
Cdd:TIGR03265 83 -QSYALFPNLTVADNI--------AYG-LKNRGMgraevAERVAELLDLVGL-----PGSERkypgqLSGGQQQRVALAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 163 ALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG-PIEEFDH-- 238
Cdd:TIGR03265 148 ALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGtPQEIYRHpa 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490181991 239 DKLVRLMVGRSidQFFIKERAtiTDEIFRVEGIKLWSLDRKKLLVDDVSFYVR 291
Cdd:TIGR03265 228 TPFVADFVGEV--NWLPGTRG--GGSRARVGGLTLACAPGLAQPGASVRLAVR 276
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
283-494 |
5.83e-28 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 109.44 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNGIGLVpedrktaglilqms 362
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-PDSGEILVDGKEVSFASPRDARRAGIAMV-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 vlhnitlpsvvmklivrkfglidsqlekeivrsfieklniktpspYQivenLSGGNQQKVVLAKWLAIKPKVLLLDEPTR 442
Cdd:cd03216 81 ---------------------------------------------YQ----LSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490181991 443 GIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
8-238 |
7.96e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.67 E-value: 7.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 8 EREVLLEARNITKTFPG-----------VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEV 76
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVrgglfgrtvgvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 77 RFRNPREAQE--NGIALIPQelD----LVPNLSSAENIflsREPVNEFGVIEYQKMFEQASKLFSKLGVNID-----PKt 145
Cdd:COG4608 83 TGLSGRELRPlrRRMQMVFQ--DpyasLNPRMTVGDII---AEPLRIHGLASKAERRERVAELLELVGLRPEhadryPH- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 146 kveDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRD 224
Cdd:COG4608 157 ---EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250
....*....|....*
gi 490181991 225 GRKVGEGPIEE-FDH 238
Cdd:COG4608 234 GKIVEIAPRDElYAR 248
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
279-490 |
8.03e-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: 109.58 E-value: 8.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSprdavkngiGLVPEDRKTAGLI 358
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE-PDSGSILIDGEDLTDLE---------DELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQ-------MSVLHNITLPsvvmklivrkfglidsqlekeivrsfieklniktpspyqivenLSGGNQQKVVLAKWLAIK 431
Cdd:cd03229 82 FQdfalfphLTVLENIALG-------------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 432 PKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-235 |
8.06e-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: 110.92 E-value: 8.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQENgIALI 92
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-REPREVRRR-IGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFL-----------SREPVNEfgVIEYQKMFEQASKLfsklgvnidpktkVEDLSTSQQQMVAIA 161
Cdd:cd03265 79 FQDLSVDDELTGWENLYIharlygvpgaeRRERIDE--LLDFVGLLEAADRL-------------VKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 162 KALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
278-509 |
8.62e-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: 111.67 E-value: 8.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 278 RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNgIGLVPEDRKTAGl 357
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK-PSSGEVLLDGRDLASLSRRELARR-IAYVPQEPPAPF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ilQMSVLHnitlpsVVM--KLIVRKFGLIDSQLEKEIVRSFIEKLNIktpSPY--QIVENLSGGNQQKVVLAKWLAIKPK 433
Cdd:COG1120 89 --GLTVRE------LVAlgRYPHLGLFGRPSAEDREAVEEALERTGL---EHLadRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 434 VLLLDEPTRGIDVNAKSEIYKLISEMA-VSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLKAA 509
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEV 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-244 |
1.23e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.03 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGV--IAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGK--------EVR-- 77
Cdd:PRK13635 3 EEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVRrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 78 ----FRNPreaqENGIALIPQELDLVPNLssaENIFLSREpvnefgviEYQKMFEQASKLfsklgVNIDPKTKVE--DLS 151
Cdd:PRK13635 83 vgmvFQNP----DNQFVGATVQDDVAFGL---ENIGVPRE--------EMVERVDQALRQ-----VGMEDFLNREphRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 152 TSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGK-SVIYISHRLEEIFEiADRVVVMRDGRKVGE 230
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
250
....*....|....*.
gi 490181991 231 GPIEE-FDH-DKLVRL 244
Cdd:PRK13635 222 GTPEEiFKSgHMLQEI 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-490 |
1.35e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.88 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 6 EKEREVLLEARNITKTF----PGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNP 81
Cdd:PRK10261 6 ELDARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 82 -------------REAQENGIALIPQE--LDLVPNLSS----AENIFLSREPVNEFGVIEYQKMFEQASKLFSKLGVNID 142
Cdd:PRK10261 86 qvielseqsaaqmRHVRGADMAMIFQEpmTSLNPVFTVgeqiAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 143 PktkvEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVV 221
Cdd:PRK10261 166 P----HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 222 MRDGRKVGEGPIEEFDHD-----------KLVRL--MVGRSIDQFF-------------IKERATITD--EIFRVEGIK- 272
Cdd:PRK10261 242 MYQGEAVETGSVEQIFHApqhpytrallaAVPQLgaMKGLDYPRRFplislehpakqepPIEQDTVVDgePILQVRNLVt 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 273 --------LWSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRtEGKVFIGGKEIKIHSPR--DAVK 342
Cdd:PRK10261 322 rfplrsglLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-GGEIIFNGQRIDTLSPGklQALR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 343 NGIGLVPEDrKTAGLILQMSVLHNITLPsvvmkliVRKFGLIDSQLEKEIVRSFIEKLNIKTPSPYQIVENLSGGNQQKV 422
Cdd:PRK10261 401 RDIQFIFQD-PYASLDPRQTVGDSIMEP-------LRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRI 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 423 VLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK10261 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
265-490 |
1.39e-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: 110.29 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 265 IFRVEGIKLWSLDRKKL--LVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVK 342
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-PTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 343 NG--IGLVPED-------RKTAGLILQMSVLHNITLPSVVMKLIVRKFGLIDSQLEKEIVRSFieklniktpsPYQiven 413
Cdd:cd03257 80 RRkeIQMVFQDpmsslnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRY----------PHE---- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 414 LSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-489 |
2.03e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.57 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCALVGENGAGKS----TLMKILAG---VYPD----YEGQIFLEGKEVRFRNPREaqeNGIALIPQEl 96
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYPSgdirFHGESLLHASEQTLRGVRG---NKIAMIFQE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 97 dlvPNLSsaeniflsrepVNEFGVIEYQ---------KMFEQASK-----LFSKLGVNiDPKTKVED----LSTSQQQMV 158
Cdd:PRK15134 101 ---PMVS-----------LNPLHTLEKQlyevlslhrGMRREAARgeilnCLDRVGIR-QAAKRLTDyphqLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 159 AIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEF- 236
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLf 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 237 ---DHDKLVRLMVGR-SIDQFFIKERATitdEIFRVEGIKLWSLDRKKLL---------VDDVSFYVRKGEVLGIYGLVG 303
Cdd:PRK15134 246 sapTHPYTQKLLNSEpSGDPVPLPEPAS---PLLDVEQLQVAFPIRKGILkrtvdhnvvVKNISFTLRPGETLGLVGESG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 304 AGRT----ELLEAIfgahpgRTEGKVFIGGKEIKIHSPRD--AVKNGIGLVPEDRKTAgLILQMSVLHNITlpsvvMKLI 377
Cdd:PRK15134 323 SGKSttglALLRLI------NSQGEIWFDGQPLHNLNRRQllPVRHRIQVVFQDPNSS-LNPRLNVLQIIE-----EGLR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 378 VRKFGLIDSQLEKEIVRSfIEKLNIKTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLIS 457
Cdd:PRK15134 391 VHQPTLSAAQREQQVIAV-MEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLK 469
|
490 500 510
....*....|....*....|....*....|...
gi 490181991 458 EM-AVSGMGVVMVSSELPEILAMSDRILVMSEG 489
Cdd:PRK15134 470 SLqQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-242 |
2.25e-27 |
|
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: 109.94 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 23 PGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIALIPQELDLVPNl 102
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 103 SSAENIFLSREPVNefgvieyQKMFEQASKLfsklgVNID------PK---TKVED----LSTSQQQMVAIAKALSLDAK 169
Cdd:cd03249 92 TIAENIRYGKPDAT-------DEEVEEAAKK-----ANIHdfimslPDgydTLVGErgsqLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 170 IIIMDEPTSAIgKRETEQLfnIIRSLKN--EGKSVIYISHRLEEIfEIADRVVVMRDGRKVGEGpieefDHDKLV 242
Cdd:cd03249 160 ILLLDEATSAL-DAESEKL--VQEALDRamKGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQG-----THDELM 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-231 |
2.65e-27 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 109.31 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 32 TLQI---YKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGK---EVRFRNPREAQENGIALIPQELDLVPNLSSA 105
Cdd:cd03297 14 TLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKKINLPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 106 ENIflsrepvnEFG--VIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKR 183
Cdd:cd03297 94 ENL--------AFGlkRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490181991 184 ETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03297 166 LRLQLLPELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
267-512 |
4.05e-27 |
|
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: 109.13 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 267 RVEGIKLwSLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIkihsprdavkngI 345
Cdd:cd03261 2 ELRGLTK-SFGGRTVL-KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRP--DSGEVLIDGEDI------------S 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 346 GLVPED----RKTAGLILQ-------MSVLHNITLPsvvmkliVRKFGLIDSQLEKEIVRSFIEKLNIKtPSPYQIVENL 414
Cdd:cd03261 66 GLSEAElyrlRRRMGMLFQsgalfdsLTVFENVAFP-------LREHTRLSEEEIREIVLEKLEAVGLR-GAEDLYPAEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 415 SGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGRkta 493
Cdd:cd03261 138 SGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGK--- 214
|
250
....*....|....*....
gi 490181991 494 efLREEVTEEDLLKAAIPR 512
Cdd:cd03261 215 --IVAEGTPEELRASDDPL 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-226 |
4.75e-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: 108.39 E-value: 4.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQE-NGIAL 91
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENIFLsrepvnefGVIEYQKM-----FEQASKLFSKLGvnIDPKTKV--EDLSTSQQQMVAIAKAL 164
Cdd:cd03262 81 VFQQFNLFPHLTVLENITL--------APIKVKGMskaeaEERALELLEKVG--LADKADAypAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 165 SLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-242 |
5.31e-27 |
|
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: 108.86 E-value: 5.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIA 90
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVpNLSSAENIFLSREPVNEFGVIEYQKMfEQASKLFSKLGVNIDpkTKVED----LSTSQQQMVAIAKALSL 166
Cdd:cd03251 80 LVSQDVFLF-NDTVAENIAYGRPGATREEVEEAARA-ANAHEFIMELPEGYD--TVIGErgvkLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 167 DAKIIIMDEPTSAIgKRETEQLfnIIRSLKN--EGKSVIYISHRLEEIfEIADRVVVMRDGRKVGEGpieefDHDKLV 242
Cdd:cd03251 156 DPPILILDEATSAL-DTESERL--VQAALERlmKNRTTFVIAHRLSTI-ENADRIVVLEDGKIVERG-----THEELL 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
283-493 |
1.31e-26 |
|
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: 106.98 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIhsprdAVKNGIGLVPEDRktaGLILQMS 362
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL-PDSGEVLFDGKPLDI-----AARNRIGYLPEER---GLYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHnitlpsvVMKLIVRKFGLIDSQLEKEIvRSFIEKLNIkTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTR 442
Cdd:cd03269 87 VID-------QLVYLAQLKGLKKEEARRRI-DEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181991 443 GIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTA 493
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
278-494 |
1.34e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 105.98 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 278 RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHSPRDAVKNgIGLVPEdrktagl 357
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP-SSGEILLDGKDLASLSPKELARK-IAYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ilqmsvlhnitlpsvVMKLivrkFGLIDsqlekeivrsFIEKlniktpspyqIVENLSGGNQQKVVLAKWLAIKPKVLLL 437
Cdd:cd03214 81 ---------------ALEL----LGLAH----------LADR----------PFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 438 DEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-243 |
1.70e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.18 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIALI 92
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELdLVP-NLSSAENIFLSREP-VNEFGVI--EYQKMFEQAsklFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDA 168
Cdd:PRK11231 82 PQHH-LTPeGITVRELVAYGRSPwLSLWGRLsaEDNARVNQA---MEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 169 KIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVR 243
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLR 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-235 |
2.19e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.49 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREA---QENG 88
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlirQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALipQELDLVPNLSSAENIFlsrepvneFGVIEYQKMF-----EQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKA 163
Cdd:PRK09493 81 MVF--QQFYLFPHLTALENVM--------FGPLRVRGASkeeaeKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 164 LSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-245 |
2.61e-26 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 112.19 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNIT---KTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTL-MKILAGVYPDY-EGQIFLEGKEVRFRNPREA 84
Cdd:NF040905 255 EVVFEVKNWTvyhPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGKEVDVSTVSDA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 85 QENGIALIPQ---ELDLVPNLSSAENIFLSREP-VNEFGVIEYQKMFEQASKLFSKLgvNIdpKT-----KVEDLSTSQQ 155
Cdd:NF040905 335 IDAGLAYVTEdrkGYGLNLIDDIKRNITLANLGkVSRRGVIDENEEIKVAEEYRKKM--NI--KTpsvfqKVGNLSGGNQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 156 QMVAIAKALSLDAKIIIMDEPTSAI---GKREteqLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGP 232
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGIdvgAKYE---IYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELP 487
|
250
....*....|...
gi 490181991 233 IEEFDHDKLVRLM 245
Cdd:NF040905 488 REEASQERIMRLI 500
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
277-490 |
3.88e-26 |
|
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: 106.05 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIkiHSPRDAVKNGIGLVPEDRktaG 356
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR-PTSGTAYINGYSI--RTDRKAARQSLGYCPQFD---A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSVLHNitlpsvvMKLIVRKFGLIDSQLEKEIVRsFIEKLNIktpSPYQ--IVENLSGGNQQKVVLAKWLAIKPKV 434
Cdd:cd03263 86 LFDELTVREH-------LRFYARLKGLPKSEIKEEVEL-LLRVLGL---TDKAnkRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 435 LLLDEPTRGIDVNAKSEIYKLISEMaVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-231 |
4.27e-26 |
|
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: 105.65 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 33 LQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPreaQENGIALIPQELDLVPNLSSAENIFLSR 112
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 113 EPVNEFGVIEYQKMfeqaSKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNII 192
Cdd:cd03298 96 SPGLKLTAEDRQAI----EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490181991 193 RSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03298 172 LDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-235 |
4.58e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.04 E-value: 4.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrNPREAQENGIALI 92
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIF-------LSREpvnefgviEYQKMFEQASKLFSKLGVNidpKTKVEDLSTSQQQMVAIAKALS 165
Cdd:PRK11432 84 FQSYALFPHMSLGENVGyglkmlgVPKE--------ERKQRVKEALELVDLAGFE---DRYVDQISGGQQQRVALARALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 166 LDAKIIIMDEPTSAIGK----------RETEQLFNIIrSLknegksviYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDAnlrrsmrekiRELQQQFNIT-SL--------YVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-226 |
4.65e-26 |
|
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: 104.61 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIA--VNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIA 90
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVPNlSSAENIflsrepvnefgvieyqkmfeqasklfsklgvnidpktkvedLSTSQQQMVAIAKALSLDAKI 170
Cdd:cd03246 80 YLPQDDELFSG-SIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 171 IIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIfEIADRVVVMRDGR 226
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGR 172
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
267-509 |
4.71e-26 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 106.81 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 267 RVEGIKLW--SLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHSPRDAVKNg 344
Cdd:COG1124 3 EVRNLSVSygQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP-WSGEVTFDGRPVTRRRRKAFRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 345 IGLVPEDRKTAgLILQMSVLHNITLPsvvmkLIVRKFGLIDSQLEK--EIV---RSFIEKLniktpsPYQivenLSGGNQ 419
Cdd:COG1124 81 VQMVFQDPYAS-LHPRHTVDRILAEP-----LRIHGLPDREERIAEllEQVglpPSFLDRY------PHQ----LSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 420 QKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGRktaefLRE 498
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGR-----IVE 219
|
250
....*....|.
gi 490181991 499 EVTEEDLLKAA 509
Cdd:COG1124 220 ELTVADLLAGP 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
266-490 |
7.19e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 104.90 E-value: 7.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 266 FRVEGIKlWSLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKeikihsPRDAVKngi 345
Cdd:COG4619 1 LELEGLS-FRVGGKPIL-SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP-TSGEIYLDGK------PLSAMP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 346 glVPEDRKTAGLILQ------MSVLHNITLPsvvmklivrkFGLIDSQLEKEIVRSFIEKLNIktpsPYQI----VENLS 415
Cdd:COG4619 69 --PPEWRRQVAYVPQepalwgGTVRDNLPFP----------FQLRERKFDRERALELLERLGL----PPDIldkpVERLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 416 GGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG4619 133 GGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-243 |
8.49e-26 |
|
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: 105.65 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 24 GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPrEAQENGIALIPQElDLVPNLS 103
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 104 SAENIFLSREPVNEFGVIEYQKMfEQASKLFSKL--GVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIg 181
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKL-AGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 182 krETEQLFNIIRSLKN--EGKSVIYISHRLEEIfEIADRVVVMRDGRKVGEGpieefDHDKLVR 243
Cdd:cd03252 170 --DYESEHAIMRNMHDicAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQG-----SHDELLA 225
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
14-249 |
9.34e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 107.10 E-value: 9.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 14 EARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKI---LagVYPDyEGQIFLEGKEVRFRNPRE------ 83
Cdd:COG1125 3 EFENVTKRYPdGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMinrL--IEPT-SGRILIDGEDIRDLDPVElrrrig 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 84 --AQENGialipqeldLVPNLSSAENIFL-------SREPVNEfGVIEYQKMfeqasklfsklgVNIDPKTKVE----DL 150
Cdd:COG1125 80 yvIQQIG---------LFPHMTVAENIATvprllgwDKERIRA-RVDELLEL------------VGLDPEEYRDryphEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 151 STSQQQMVAIAKALSLDAKIIIMDEPTSAIG--KRET--EQLFNIIRSLkneGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:COG1125 138 SGGQQQRVGVARALAADPPILLMDEPFGALDpiTREQlqDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGR 214
|
250 260 270
....*....|....*....|....*....|..
gi 490181991 227 kvgegpIEEFDH---------DKLVRLMVGRS 249
Cdd:COG1125 215 ------IVQYDTpeeilanpaNDFVADFVGAD 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-235 |
9.42e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.55 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFP----------------------GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIF 70
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 71 LEGKEVrfrnpreaqengiALIpqEL--DLVPNLSSAENIFL-------SREpvnefgviEYQKMFEQASKlFSKLGVNI 141
Cdd:COG1134 85 VNGRVS-------------ALL--ELgaGFHPELTGRENIYLngrllglSRK--------EIDEKFDEIVE-FAELGDFI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 142 DpkTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAiGKRE-TEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVV 220
Cdd:COG1134 141 D--QPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAV-GDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAI 217
|
250
....*....|....*
gi 490181991 221 VMRDGRKVGEGPIEE 235
Cdd:COG1134 218 WLEKGRLVMDGDPEE 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
279-490 |
1.00e-25 |
|
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: 103.09 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRdAVKNGIGLVPEdrktagli 358
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-PTSGEILIDGKDIAKLPLE-ELRRRIGYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 lqmsvlhnitlpsvvmklivrkfglidsqlekeivrsfieklniktpspyqivenLSGGNQQKVVLAKWLAIKPKVLLLD 438
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490181991 439 EPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-240 |
1.81e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFR---NPREAQE--N 87
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSqkpSEKAIRLlrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 GIALIPQELDLVPNLSSAENifLSREPVNEFGVIEYQKMfEQASKLFSKLGvnIDPKTKV--EDLSTSQQQMVAIAKALS 165
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEN--LIEAPCKVLGLSKEQAR-EKAMKLLARLR--LTDKADRfpLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 166 LDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDK 240
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQPQ 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
275-490 |
2.15e-25 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 104.34 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 275 SLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTeGKVFIGGKEIKIHSPRdavKNGIGLVPEDRkt 354
Cdd:cd03299 7 SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS-GKILLNGKDITNLPPE---KRDISYVPQNY-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 355 aGLILQMSVLHNITLpSVVMKLIVRKfglidsQLEKEiVRSFIEKLNI-----KTPspyqivENLSGGNQQKVVLAKWLA 429
Cdd:cd03299 81 -ALFPHMTVYKNIAY-GLKKRKVDKK------EIERK-VLEIAEMLGIdhllnRKP------ETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 430 IKPKVLLLDEPTRGIDVNAKSeiyKLISEMAV----SGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKE---KLREELKKirkeFGVTVLHVTHDFEEAWALADKVAIMLNGK 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-236 |
2.38e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.07 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAvnNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPreaQENGIALI 92
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP---AERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFLSREPVNEFGVIEYQKMFEQASKlfsklgVNIDP--KTKVEDLSTSQQQMVAIAKALSLDAKI 170
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALER------VGLAGllDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 171 IIMDEPTSAIG---KRETEQLFNIIRslKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEF 236
Cdd:COG3840 151 LLLDEPFSALDpalRQEMLDLVDELC--RERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
8-239 |
3.11e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 106.33 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 8 EREVLLEARNITKTF------------PGVI-AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGK 74
Cdd:PRK15079 4 GKKVLLEVADLKVHFdikdgkqwfwqpPKTLkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 75 EVRFRNPREAQE--NGIALIPQE--LDLVPNLSSAENIflsREPVNEFgvieYQKMFEQASK-----LFSKLG-----VN 140
Cdd:PRK15079 84 DLLGMKDDEWRAvrSDIQMIFQDplASLNPRMTIGEII---AEPLRTY----HPKLSRQEVKdrvkaMMLKVGllpnlIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 141 IDPktkvEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRV 219
Cdd:PRK15079 157 RYP----HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRV 232
|
250 260
....*....|....*....|
gi 490181991 220 VVMRDGRKVGEGPIEEFDHD 239
Cdd:PRK15079 233 LVMYLGHAVELGTYDEVYHN 252
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-222 |
3.21e-25 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 108.91 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGV-IAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQEnGIAL 91
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-QIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNlSSAENIFLSREPVNEfgvieyqKMFEQASK------LFSKLGVNIDpkTKVED----LSTSQQQMVAIA 161
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDASD-------AEIREALEragldeFVAALPQGLD--TPIGEggagLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 162 KALSLDAKIIIMDEPTSAIgKRETEQLFN-IIRSLKnEGKSVIYISHRLEEIfEIADRVVVM 222
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHL-DAETEAEVLeALRALA-QGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
266-490 |
3.77e-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: 103.41 E-value: 3.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 266 FRVEGIKLWSLDRKKLlvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAH---PG-RTEGKVFIGGKEIKihsprdav 341
Cdd:cd03260 1 IELRDLNVYYGDKHAL--KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdliPGaPDEGEVLLDGKDIY-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 342 kNGIGLVPEDRKTAGLILQ------MSVLHNITLPsvvmkliVRKFGLIDSQLEKEIVRSFIEKL----NIKTPSPyqiV 411
Cdd:cd03260 71 -DLDVDVLELRRRVGMVFQkpnpfpGSIYDNVAYG-------LRLHGIKLKEELDERVEEALRKAalwdEVKDRLH---A 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 412 ENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSgMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03260 140 LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-235 |
4.42e-25 |
|
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: 108.68 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIA 90
Cdd:COG4618 331 LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH-IG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVPNlSSAENIflSRepvneFGVIEYQKMFEQASK-----LFSKLgvnidPK---TKVED----LSTSQQQMV 158
Cdd:COG4618 410 YLPQDVELFDG-TIAENI--AR-----FGDADPEKVVAAAKLagvheMILRL-----PDgydTRIGEggarLSGGQRQRI 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 159 AIAKALSLDAKIIIMDEPTS---AIGkretEQ-LFNIIRSLKNEGKSVIYISHRLeEIFEIADRVVVMRDGRKVGEGPIE 234
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSnldDEG----EAaLAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRD 551
|
.
gi 490181991 235 E 235
Cdd:COG4618 552 E 552
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
277-490 |
6.15e-25 |
|
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: 102.57 E-value: 6.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSPRDavkngigLVPEDRKTA 355
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGlDRP--TSGEVRVDGTDISKLSEKE-------LAAFRRRHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 356 GLILQ-------MSVLHNITLPSVVMKLIVRKfglidsqlEKEIVRSFIEKLNIKTpSPYQIVENLSGGNQQKVVLAKWL 428
Cdd:cd03255 85 GFVFQsfnllpdLTALENVELPLLLAGVPKKE--------RRERAEELLERVGLGD-RLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 429 AIKPKVLLLDEPTRGIDVNAKSEIYKLISEMA-VSGMGVVMVSSElPEILAMSDRILVMSEGR 490
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
12-235 |
6.64e-25 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 103.53 E-value: 6.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYP-----DYEGQIFLEGKEV--RFRNPREA 84
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIydKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 85 QENgIALIPQELDLVPnLSSAENIFLSrepVNEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVED----LSTSQQQMVAI 160
Cdd:TIGR00972 81 RRR-VGMVFQKPNPFP-MSIYDNIAYG---PRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDsalgLSGGQQQRLCI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 161 AKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKnEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:TIGR00972 156 ARALAVEPEVLLLDEPTSALDPIATGKIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQ 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-236 |
8.88e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.16 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 16 RNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGV-YPDyEGQIFLEGKEVRFRNPRE--AQENG 88
Cdd:COG1135 5 ENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLeRPT-SGSVLVDGVDLTALSERElrAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQELDLvpnLSS---AENIFLS-----------REPVNEfgVIEYqkmfeqasklfsklgVNIDPKTKV--EDLST 152
Cdd:COG1135 84 IGMIFQHFNL---LSSrtvAENVALPleiagvpkaeiRKRVAE--LLEL---------------VGLSDKADAypSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 153 SQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
....*
gi 490181991 232 PIEEF 236
Cdd:COG1135 224 PVLDV 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-226 |
9.29e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.44 E-value: 9.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQEN---G 88
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRREIPYlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQELDLVPNLSSAENIFLSREpvnefgVIEYQK--MFEQASKLFSKLGvnIDPKTK--VEDLSTSQQQMVAIAKAL 164
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLR------VTGKSRkeIRRRVREVLDLVG--LSDKAKalPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 165 SLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-226 |
1.38e-24 |
|
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: 101.72 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEV----RFRNPREAQEN 87
Cdd:cd03292 1 IEFINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 GIALipQELDLVPNLSSAENIFLSREPVNEFGvieyQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLD 167
Cdd:cd03292 81 GVVF--QDFRLLPDRNVYENVAFALEVTGVPP----REIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 168 AKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-235 |
1.60e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 107.50 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrnpreAQEN 87
Cdd:PRK10535 4 LLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV-------ATLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 GIAL----------IPQELDLVPNLSSAENIflsrEPVNEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQM 157
Cdd:PRK10535 77 ADALaqlrrehfgfIFQRYHLLSHLTAAQNV----EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 158 VAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRlEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQE 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
13-235 |
3.35e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 101.37 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGI--- 89
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIrql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ----ALIPQELDLVPNLSSAENIFlsREPVNEFGVIEYQKMfEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALS 165
Cdd:PRK11264 84 rqhvGFVFQNFNLFPHRTVLENII--EGPVIVKGEPKEEAT-ARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 166 LDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-231 |
3.44e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 103.37 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 11 VLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrnPREAQ--ENG 88
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARlaRAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQELDLVPNLSSAENIFLsrepvneFGviEYQKMFEQASKL-------FSKLGVNIDpkTKVEDLSTSQQQMVAIA 161
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLV-------FG--RYFGMSTREIEAvipslleFARLESKAD--ARVSDLSGGMKRRLTLA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 162 KALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
10-252 |
3.83e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 101.63 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVY---PDYEGQIFLEGKEVR-----FRNP 81
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 82 REAQENgIALIPQELDLVPNLSSAENIFLS--------REPVNEFGVIEYQKmfeqASKLFSKLGVNIDPKTKVEDLSTS 153
Cdd:PRK09984 82 RKSRAN-TGYIFQQFNLVNRLSVLENVLIGalgstpfwRTCFSWFTREQKQR----ALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 154 QQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGP 232
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
250 260
....*....|....*....|
gi 490181991 233 IEEFDHDKLVRLMvgRSIDQ 252
Cdd:PRK09984 237 SQQFDNERFDHLY--RSINR 254
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
12-242 |
4.90e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 101.22 E-value: 4.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIAL 91
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENIFLSREPVNEFGVI------------EYQKMfEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVA 159
Cdd:PRK11300 85 TFQHVRLFREMTVIENLLVAQHQQLKTGLFsgllktpafrraESEAL-DRAATWLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 160 IAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDH 238
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
....
gi 490181991 239 DKLV 242
Cdd:PRK11300 244 NPDV 247
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
278-507 |
6.00e-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: 100.31 E-value: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 278 RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKiHSPRDA-VKNGIGLVPEDrktAG 356
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKP-DSGKILLDGQDIT-KLPMHKrARLGIGYLPQE---AS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSVLHNItlpsvvmKLIVRKFGLIDSQLEKEIVrSFIEKLNIkTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLL 436
Cdd:cd03218 86 IFRKLTVEENI-------LAVLEIRGLSKKEREEKLE-ELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 437 LDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLK 507
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
283-490 |
6.96e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 102.87 E-value: 6.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIkihsprdavkngIGLVPEDRKTaGLILQ- 360
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETP--DSGRILLDGRDV------------TGLPPEKRNV-GMVFQd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 ------MSVLHNITlpsvvmklivrkFGL----IDSQLEKEIVRSFIEKLNI-----KTPSpyqiveNLSGGNQQKVVLA 425
Cdd:COG3842 86 yalfphLTVAENVA------------FGLrmrgVPKAEIRARVAELLELVGLegladRYPH------QLSGGQQQRVALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 426 KWLAIKPKVLLLDEPTRGIDVNAK----SEIYKLISEmavSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLReemrEELRRLQRE---LGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-231 |
8.13e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 101.81 E-value: 8.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGV-YPDyEGQIFLEGKEVRFRNPREAQENGIal 91
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPD-AGSISLCGEPVPSRARHARQRVGV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENIFL-SREpvneFGVIEYQKMFEQASKL-FSKLGVNIDpkTKVEDLSTSQQQMVAIAKALSLDAK 169
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVfGRY----FGLSAAAARALVPPLLeFAKLENKAD--AKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 170 IIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
283-494 |
1.03e-23 |
|
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: 100.11 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNGIGlvpedRK--TAGLILQ 360
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYR-PTSGRILFDGRDITGLPPHRIARLGIA-----RTfqNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 MSVLHNITL------PSVVMKLIVRKFGLIDSQLE-KEIVRSFIEKLNIkTPSPYQIVENLSGGNQQKVVLAKWLAIKPK 433
Cdd:COG0411 94 LTVLENVLVaaharlGRGLLAALLRLPRARREEREaRERAEELLERVGL-ADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 434 VLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-225 |
1.56e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 101.70 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQengIALI 92
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK---VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENI-----FLSREPVNEFGVIEYQ--KMFE--QASKLFSKLgvnidPKtkveDLSTSQQQMVAIAKA 163
Cdd:PRK10851 80 FQHYALFRHMTVFDNIafgltVLPRRERPNAAAIKAKvtQLLEmvQLAHLADRY-----PA----QLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 164 LSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGK-SVIYISHRLEEIFEIADRVVVMRDG 225
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
13-243 |
1.57e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.33 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAG-VYPDyEGQIFLEGKEV-RFRNPREAQEnGIA 90
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlVKPD-SGRIFLDGEDItHLPMHKRARL-GIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVPNLSSAENIFLsrepVNEFGVIEYQKMFEQASKLFSKLGVnidpkTKVED-----LSTSQQQMVAIAKALS 165
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILA----VLELRKLSKKEREERLEELLEEFGI-----THLRKskaysLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 166 LDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVR 243
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVR 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-235 |
2.24e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.46 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 11 VLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPRE-AQEngI 89
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARR--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQEldlvPNLSSAeniFLSREPVnEFGVIEYQKMFEQASKLFSK-LGvnidpKTKVEDLSTSQ--------QQMVAI 160
Cdd:PRK13548 79 AVLPQH----SSLSFP---FTVEEVV-AMGRAPHGLSRAEDDALVAAaLA-----QVDLAHLAGRDypqlsggeQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 161 AKAL------SLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPI 233
Cdd:PRK13548 146 ARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
..
gi 490181991 234 EE 235
Cdd:PRK13548 226 AE 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
277-508 |
2.52e-23 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 104.15 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHSPRDaVKNGIGLVPEDrktaG 356
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP-TSGRILIDGIDLRQIDPAS-LRRQIGVVLQD----V 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSVLHNITL--PSVVMKLIV---RKFGLIDsqlekeivrsFIEKLniktPSPYQIV-----ENLSGGNQQKVVLAK 426
Cdd:COG2274 559 FLFSGTIRENITLgdPDATDEEIIeaaRLAGLHD----------FIEAL----PMGYDTVvgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 427 WLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELpEILAMSDRILVMSEGRktaefLREEVTEEDLL 506
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGR-----IVEDGTHEELL 697
|
..
gi 490181991 507 KA 508
Cdd:COG2274 698 AR 699
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-249 |
2.77e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.21 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 30 NVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIALIPQE-------LDL---- 98
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDrqssglyLDAplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 99 -VPNLSSAENIFLSRePVNEFGVIEyqkMFEQAsklfskLGVNI-DPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEP 176
Cdd:PRK15439 361 nVCALTHNRRGFWIK-PARENAVLE---RYRRA------LNIKFnHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 177 TSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVRLMVGRS 249
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFGEH 503
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-226 |
3.39e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.18 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 2 MLNTEK-EREVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrN 80
Cdd:PRK09452 3 KLNKQPsSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI---T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 81 PREAQENGIALIPQELDLVPNLSSAENI-F---LSREPVNEFG--VIEYQKMFeQASKLFSKlgvnidpktKVEDLSTSQ 154
Cdd:PRK09452 80 HVPAENRHVNTVFQSYALFPHMTVFENVaFglrMQKTPAAEITprVMEALRMV-QLEEFAQR---------KPHQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 155 QQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-235 |
3.63e-23 |
|
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: 100.95 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 30 NVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGK-----EVRFRNPREAQenGIALIPQELDLVPNLSS 104
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsARGIFLPPHRR--RIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 105 AENIF--LSREPVNEFGVieyqkMFEQASKLfskLGvnIDP--KTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAI 180
Cdd:COG4148 95 RGNLLygRKRAPRAERRI-----SFDEVVEL---LG--IGHllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 181 G---KREteqLFNIIRSLKNEGK-SVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:COG4148 165 DlarKAE---ILPYLERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
267-494 |
3.64e-23 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 98.13 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 267 RVEGIKLwSLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIK--IHSPRDAVKNG 344
Cdd:COG1127 7 EVRNLTK-SFGDRVVL-DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR-PDSGEILVDGQDITglSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 345 IGLVpedrktagliLQ-------MSVLHNITLPsvvmkliVRKFGLIDSQLEKEIVRsfiEKLNI--------KTPSpyq 409
Cdd:COG1127 84 IGML----------FQggalfdsLTVFENVAFP-------LREHTDLSEAEIRELVL---EKLELvglpgaadKMPS--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 410 iveNLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSE 488
Cdd:COG1127 141 ---ELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLAD 217
|
....*.
gi 490181991 489 GRKTAE 494
Cdd:COG1127 218 GKIIAE 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-235 |
4.63e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.26 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPRE-AQEngIA 90
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElARR--RA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVPNLSSAENIFLSREPVNEFGVIEYQKMFEQ---------ASKLFSklgvnidpktkveDLSTSQQQMVAIA 161
Cdd:COG4559 79 VLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREAlalvglahlAGRSYQ-------------TLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 162 KAL-------SLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIE 234
Cdd:COG4559 146 RVLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225
|
.
gi 490181991 235 E 235
Cdd:COG4559 226 E 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-231 |
5.21e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 102.79 E-value: 5.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEG---KEVRFRNPReaqeN 87
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASLR----N 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 GIALIPQELDLVpNLSSAENIFLSREPVNEFGVIEYQKMFEQASKLFSKLGVNIDpkTKVED----LSTSQQQMVAIAKA 163
Cdd:PRK11176 418 QVALVSQNVHLF-NDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLD--TVIGEngvlLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 164 LSLDAKIIIMDEPTSAIgkrETEQLFNIIRSL----KNegKSVIYISHRLEEIfEIADRVVVMRDGRKVGEG 231
Cdd:PRK11176 495 LLRDSPILILDEATSAL---DTESERAIQAALdelqKN--RTSLVIAHRLSTI-EKADEILVVEDGEIVERG 560
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
266-505 |
5.74e-23 |
|
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: 97.64 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 266 FRVEGI-KLWSLDRKKLlvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHSPRD--AVK 342
Cdd:cd03256 1 IEVENLsKTYPNGKKAL--KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP-TSGSVLIDGTDINKLKGKAlrQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 343 NGIGLVPEDrktAGLILQMSVLHNITLPSVVMKLIVRK-FGLIDSQlEKEIVRSFIEKLNIKTpSPYQIVENLSGGNQQK 421
Cdd:cd03256 78 RQIGMIFQQ---FNLIERLSVLENVLSGRLGRRSTWRSlFGLFPKE-EKQRALAALERVGLLD-KAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 422 VVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEV 500
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
....*
gi 490181991 501 TEEDL 505
Cdd:cd03256 233 TDEVL 237
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-240 |
6.34e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 6.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPreAQENGIALIPQELDLV------- 99
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKT--PSDKAIRELRRNVGMVfqqynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 100 PNLSSAENifLSREPVNEFGVIEYQKMfEQASKLFSKLgvnidpktKVED--------LSTSQQQMVAIAKALSLDAKII 171
Cdd:PRK11124 95 PHLTVQQN--LIEAPCRVLGLSKDQAL-ARAEKLLERL--------RLKPyadrfplhLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 172 IMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDK 240
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQ 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-238 |
6.83e-23 |
|
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: 102.07 E-value: 6.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 8 EREVLLEARNITKTFPG-----------VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPdYEGQIFLEGKEV 76
Cdd:COG4172 271 DAPPLLEARDLKVWFPIkrglfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 77 ---------RFR--------------NPREAqengIALIPQE-LDLV-PNLSSAEniflsREpvnefgvieyqkmfEQAS 131
Cdd:COG4172 350 dglsrralrPLRrrmqvvfqdpfgslSPRMT----VGQIIAEgLRVHgPGLSAAE-----RR--------------ARVA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 132 KLFSKlgVNIDPKTK---VEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSA----IGKreteQLFNIIRSLKNE-GKSVI 203
Cdd:COG4172 407 EALEE--VGLDPAARhryPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAldvsVQA----QILDLLRDLQREhGLAYL 480
|
250 260 270
....*....|....*....|....*....|....*.
gi 490181991 204 YISHRLEEIFEIADRVVVMRDGRKVGEGPIEE-FDH 238
Cdd:COG4172 481 FISHDLAVVRALAHRVMVMKDGKVVEQGPTEQvFDA 516
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-231 |
7.15e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 97.69 E-value: 7.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFR------------ 79
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyalseaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 80 -----------NPREAqengialipqeldLVPNLSSAENIflsREPVNEFGVIEYQKMFEQASKLFSKlgVNIDPKtKVE 148
Cdd:PRK11701 86 llrtewgfvhqHPRDG-------------LRMQVSAGGNI---GERLMAVGARHYGDIRATAGDWLER--VEIDAA-RID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 149 DLSTS----QQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMR 223
Cdd:PRK11701 147 DLPTTfsggMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMK 226
|
....*...
gi 490181991 224 DGRKVGEG 231
Cdd:PRK11701 227 QGRVVESG 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
277-495 |
7.78e-23 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 96.77 E-value: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRdavkngIGLVPEDrktAG 356
Cdd:cd03293 14 GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER-PTSGEVLVDGEPVTGPGPD------RGYVFQQ---DA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSVLHNITLPsvvmklivRKFGLIDSQLEKEIVRSFIEKLNIKTPS---PYQivenLSGGNQQKVVLAKWLAIKPK 433
Cdd:cd03293 84 LLPWLTVLDNVALG--------LELQGVPKAEARERAEELLELVGLSGFEnayPHQ----LSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 434 VLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSE--GRKTAEF 495
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEV 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-235 |
8.84e-23 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 96.92 E-value: 8.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 23 PGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEG---KEVRFRNPREAqengIALIPQELDLV 99
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRA----IGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 100 pNLSSAENIFLSREPVNEFGVIEyqkmfeqASKLfsklgVNIDPK---------TKVED----LSTSQQQMVAIAKALSL 166
Cdd:cd03253 88 -NDTIGYNIRYGRPDATDEEVIE-------AAKA-----AQIHDKimrfpdgydTIVGErglkLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 167 DAKIIIMDEPTSAIgKRETEQlfNIIRSLKN--EGKSVIYISHRLEEIFEiADRVVVMRDGRKVGEGPIEE 235
Cdd:cd03253 155 NPPILLLDEATSAL-DTHTER--EIQAALRDvsKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-242 |
8.87e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.88 E-value: 8.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQeNGIAL 91
Cdd:PRK13647 5 IEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR-SKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDlvpnlssaENIFLSR-------EPVN-EFGVIEYQKMFEQASKLfsklgVNI-DPKTKVE-DLSTSQQQMVAIA 161
Cdd:PRK13647 84 VFQDPD--------DQVFSSTvwddvafGPVNmGLDKDEVERRVEEALKA-----VRMwDFRDKPPyHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 162 KALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKL 241
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDI 230
|
.
gi 490181991 242 V 242
Cdd:PRK13647 231 V 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-230 |
9.90e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.87 E-value: 9.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 11 VLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIA 90
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVPNLSSAENI-----FLSREpvnefgviEYQKMFEQASKLFSKLGVNIDPKTKVedLSTSQQQMVAIAKALS 165
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLamggfFAERD--------QFQERIKWVYELFPRLHERRIQRAGT--MSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 166 LDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGE 230
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-235 |
1.56e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.50 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFP---G-------VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrFR 79
Cdd:PRK11308 3 QPLLQAIDLKKHYPvkrGlfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL-LK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 80 NPREAQengiALIPQELDLVpnlssAENIFLSREPVNEFGVI-----------EYQKMFEQASKLFSKLGVnidpKTKVE 148
Cdd:PRK11308 82 ADPEAQ----KLLRQKIQIV-----FQNPYGSLNPRKKVGQIleepllintslSAAERREKALAMMAKVGL----RPEHY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 149 D-----LSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVM 222
Cdd:PRK11308 149 DryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVM 228
|
250
....*....|...
gi 490181991 223 RDGRKVGEGPIEE 235
Cdd:PRK11308 229 YLGRCVEKGTKEQ 241
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-226 |
1.87e-22 |
|
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: 96.00 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTF---PGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENg 88
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQEldlvPNLSS---AENIFLSREPVNEFGVIEYQKMFeQASKLFSKL--GVNIDPKTKVEDLSTSQQQMVAIAKA 163
Cdd:cd03248 90 VSLVGQE----PVLFArslQDNIAYGLQSCSFECVKEAAQKA-HAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 164 LSLDAKIIIMDEPTSAIgKRETEQLFNIIRSLKNEGKSVIYISHRLEEIfEIADRVVVMRDGR 226
Cdd:cd03248 165 LIRNPQVLILDEATSAL-DAESEQQVQQALYDWPERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
277-491 |
1.87e-22 |
|
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: 95.80 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHP--GRTEGKVFIGGKEIKihspRDAVKNGIGLVPEDRKT 354
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEggGTTSGQILFNGQPRK----PDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 355 A-GLILQMSVLHnitlpSVVMKLIVRKfglIDSQLEKEIVRSFIEKLNIkTPSPYQIVENLSGGNQQKVVLAKWLAIKPK 433
Cdd:cd03234 93 LpGLTVRETLTY-----TAILRLPRKS---SDAIRKKRVEDVLLRDLAL-TRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 434 VLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVM-VSSELPEILAMSDRILVMSEGRK 491
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
283-490 |
1.91e-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: 96.25 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSPRDavkNGIGLVPEDRktaGLILQM 361
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERP--DSGTILFGGEDATDVPVQE---RNVGFVFQHY---ALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNitlpsVVMKLIVRKFGLIDSQLE-KEIVRSFI-----EKLNIKTPSpyqiveNLSGGNQQKVVLAKWLAIKPKVL 435
Cdd:cd03296 90 TVFDN-----VAFGLRVKPRSERPPEAEiRAKVHELLklvqlDWLADRYPA------QLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 436 LLDEPTRGIDVNAKSE----IYKLISEMAVSgmgVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03296 159 LLDEPFGALDAKVRKElrrwLRRLHDELHVT---TVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-269 |
3.47e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 97.56 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 14 EARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNP---REAQE 86
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 87 NgIALIPQELDLvpnLSS---AENIFLSREPVNEfgvieyqkmfeqasklfSKLGVnidpKTKVEDL------------- 150
Cdd:PRK11153 83 Q-IGMIFQHFNL---LSSrtvFDNVALPLELAGT-----------------PKAEI----KARVTELlelvglsdkadry 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 151 ----STSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDG 225
Cdd:PRK11153 138 paqlSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 226 RKVGEGPIEE-FDHDK--LVRLMVGRSIDQ--------FFIKERATITDEIFRVE 269
Cdd:PRK11153 218 RLVEQGTVSEvFSHPKhpLTREFIQSTLHLdlpedylaRLQAEPTTGSGPLLRLE 272
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-235 |
4.54e-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: 99.49 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 6 EKEREVLLE-----ARNITKTF----PGVI-AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQI-FLEGK 74
Cdd:TIGR03269 268 EKECEVEVGepiikVRNVSKRYisvdRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGD 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 75 EVRFRNPREAQENG-----IALIPQELDLVPNLSSAENIF--LSREPVNEFGVIEYQKMFEQASklFS-KLGVNIDPKTK 146
Cdd:TIGR03269 348 EWVDMTKPGPDGRGrakryIGILHQEYDLYPHRTVLDNLTeaIGLELPDELARMKAVITLKMVG--FDeEKAEEILDKYP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 147 VEdLSTSQQQMVAIAKALSLDAKIIIMDEPTSA---IGKRETEQlfNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMR 223
Cdd:TIGR03269 426 DE-LSEGERHRVALAQVLIKEPRIVILDEPTGTmdpITKVDVTH--SILKAREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
250
....*....|..
gi 490181991 224 DGRKVGEGPIEE 235
Cdd:TIGR03269 503 DGKIVKIGDPEE 514
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-238 |
5.05e-22 |
|
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: 94.48 E-value: 5.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQENGIALIPQEldlvPNLSSA- 105
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRISIIPQD----PVLFSGt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 106 --ENIflsrEPVNEFGVIEYQKMFEQAS--KLFSKLGVNIDpkTKVED----LSTSQQQMVAIAKALSLDAKIIIMDEPT 177
Cdd:cd03244 94 irSNL----DPFGEYSDEELWQALERVGlkEFVESLPGGLD--TVVEEggenLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 178 SAIGKRETEQLFNIIRS-LKNegKSVIYISHRLEEIFEiADRVVVMRDGRkvgegpIEEFDH 238
Cdd:cd03244 168 ASVDPETDALIQKTIREaFKD--CTVLTIAHRLDTIID-SDRILVLDKGR------VVEFDS 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-231 |
5.78e-22 |
|
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: 93.15 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrnpreaqengia 90
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 lipqeLDLVPNLSSAeniflsrepvneFGVIEyQKMFEQASKLFSKLGvnidpktkvEDLSTSQQQMVAIAKALSLDAKI 170
Cdd:cd03247 67 -----SDLEKALSSL------------ISVLN-QRPYLFDTTLRNNLG---------RRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 171 IIMDEPTSAIGKRETEQLFNIIRSLKnEGKSVIYISHRLEEIfEIADRVVVMRDGRKVGEG 231
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-240 |
6.29e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.59 E-value: 6.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQEN-GIALIPQELDLVPNLSSA 105
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHiGIVFQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 106 ENIFLSrepvnEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRET 185
Cdd:PRK13648 104 DVAFGL-----ENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 186 EQLFNIIRSLKNEGK-SVIYISHRLEEIFEiADRVVVMRDGRKVGEG-PIEEFDHDK 240
Cdd:PRK13648 179 QNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGtPTEIFDHAE 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-234 |
7.97e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.44 E-value: 7.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEG---------KEVR---- 77
Cdd:PRK13644 1 MIRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklQGIRklvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 78 --FRNPrEAQ------ENGIALIPQELDLVPnlssaeniflsrepvnefgvIEYQKMFEQAsklFSKLGVNI----DPKT 145
Cdd:PRK13644 81 ivFQNP-ETQfvgrtvEEDLAFGPENLCLPP--------------------IEIRKRVDRA---LAEIGLEKyrhrSPKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 146 kvedLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIfEIADRVVVMRDG 225
Cdd:PRK13644 137 ----LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRG 211
|
....*....
gi 490181991 226 RKVGEGPIE 234
Cdd:PRK13644 212 KIVLEGEPE 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-244 |
8.92e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.65 E-value: 8.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 31 VTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQ------------ENGIALIPQELDL 98
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadknqlrllRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 99 VPNLSSAENIFlsREPVNEFGVIEyQKMFEQASKLFSKLGVNIDPKTKVE-DLSTSQQQMVAIAKALSLDAKIIIMDEPT 177
Cdd:PRK10619 104 WSHMTVLENVM--EAPIQVLGLSK-QEARERAVKYLAKVGIDERAQGKYPvHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 178 SAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE-FDHDKLVRL 244
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQlFGNPQSPRL 248
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
267-489 |
9.95e-22 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 93.09 E-value: 9.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 267 RVEGIKLwSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKihsprdavkngig 346
Cdd:cd03226 1 RIENISF-SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-ESSGSILLNGKPIK------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 347 lVPEDRKTAGLILQmSVLHNITLPSVVMKLIvrkFGLIDSQLEKEIVRSFIEKLNIktpspYQIVE----NLSGGNQQKV 422
Cdd:cd03226 66 -AKERRKSIGYVMQ-DVDYQLFTDSVREELL---LGLKELDAGNEQAETVLKDLDL-----YALKErhplSLSGGQKQRL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 423 VLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEG 489
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
283-490 |
9.99e-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: 93.84 E-value: 9.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHpGRTEGKVFIGGKEIkihSPRDAVKNGIGLVPEDRktaGLILQMS 362
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE-TPTSGEILLDGKDI---TNLPPHKRPVNTVFQNY---ALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNITLPsvvMKLIVRKFGLIDSQLEK--EIVRsfIEKLNIKTPSpyqiveNLSGGNQQKVVLAKWLAIKPKVLLLDEP 440
Cdd:cd03300 89 VFENIAFG---LRLKKLPKAEIKERVAEalDLVQ--LEGYANRKPS------QLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181991 441 TRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-243 |
1.30e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.76 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNP---REAQEN 87
Cdd:PRK13639 1 ILETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 GIALI-PQELDLVPNLSS-----AENIFLSREpvnefgviEYQKMFEQASKLFSKLGVNIDPKtkvEDLSTSQQQMVAIA 161
Cdd:PRK13639 81 GIVFQnPDDQLFAPTVEEdvafgPLNLGLSKE--------EVEKRVKEALKAVGMEGFENKPP---HHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 162 KALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG-PIEEFDHDK 240
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGtPKEVFSDIE 229
|
...
gi 490181991 241 LVR 243
Cdd:PRK13639 230 TIR 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
283-441 |
1.32e-21 |
|
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: 91.17 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKiHSPRDAVKNGIGLVPEDrktAGLILQMS 362
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP-TEGTILLDGQDLT-DDERKSLRKEIGYVFQD---PQLFPRLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNItlpsvvmkLIVRKFGLIDSQLEKEIVRSFIEKLNI----KTPsPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLD 438
Cdd:pfam00005 76 VRENL--------RLGLLLKGLSKREKDARAEEALEKLGLgdlaDRP-VGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
...
gi 490181991 439 EPT 441
Cdd:pfam00005 147 EPT 149
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
282-490 |
1.36e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.98 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 282 LVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSPrdavkngiglvPEDRKTaGLILQ 360
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETP--DSGRIVLNGRDLFTNLP-----------PRERRV-GFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 -------MSVLHNItlpsvvmklivrKFGL----IDSQLEKEIVRSFIEKLNIKT-----PSpyqiveNLSGGNQQKVVL 424
Cdd:COG1118 83 hyalfphMTVAENI------------AFGLrvrpPSKAEIRARVEELLELVQLEGladryPS------QLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 425 AKWLAIKPKVLLLDEPTRGIDVNAKSEIYK----LISEMAVSgmgVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRwlrrLHDELGGT---TVFVTHDQEEALELADRVVVMNQGR 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-244 |
1.55e-21 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 97.49 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 5 TEKEREVLLEARNIT-KTFPgviAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPRE 83
Cdd:PRK10982 243 ENKPGEVILEVRNLTsLRQP---SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 84 AQENGIALIPQE---LDLVPNLSSAENIFLS--REPVNEFGVIEYQKMFEQASKLFSKLGVNI-DPKTKVEDLSTSQQQM 157
Cdd:PRK10982 320 AINHGFALVTEErrsTGIYAYLDIGFNSLISniRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTpGHRTQIGSLSGGNQQK 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 158 VAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFD 237
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTT 479
|
....*..
gi 490181991 238 HDKLVRL 244
Cdd:PRK10982 480 QNEILRL 486
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-243 |
2.25e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.03 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIAL 91
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENIFLSREPVNEfgvIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKII 171
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDD---LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 172 IMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVR 243
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVK 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-234 |
2.53e-21 |
|
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: 91.82 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVyPDYE---GQIFLEGKEVRFRNPREAQENGI 89
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEvteGEILFKGEDITDLPPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELDLVPNLSsaeNIFLSREpVNEfgvieyqkmfeqasklfsklGVNIDPKTKVEdlstsqqqmvaIAKALSLDAK 169
Cdd:cd03217 80 FLAFQYPPEIPGVK---NADFLRY-VNE--------------------GFSGGEKKRNE-----------ILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 170 IIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRlEEIFE--IADRVVVMRDGRKVGEGPIE 234
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY-QRLLDyiKPDRVHVLYDGRIVKSGDKE 190
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-231 |
3.04e-21 |
|
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: 91.46 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIA------VNNVTLQIYKGEVCALVGENGAGKSTLMKILAG--VYPDYEGQIFLEGKEVRFRNPREA 84
Cdd:cd03213 4 LSFRNLTVTVKSSPSksgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 85 qengIALIPQELDLVPNLSSAENIflsrepvnefgvieyqkMFeqASKLFSklgvnidpktkvedLSTSQQQMVAIAKAL 164
Cdd:cd03213 84 ----IGYVPQDDILHPTLTVRETL-----------------MF--AAKLRG--------------LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 165 SLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRL-EEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-235 |
3.73e-21 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 94.48 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 43 LVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPreaQENGIALIPQELDLVPNLSSAENIflsrepvnEFGV-I 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP---HLRHINMVFQSYALFPHMTVEENV--------AFGLkM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 122 EYQKMFEQASKLFSKLG-VNID--PKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE 198
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRlVQLEefADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 490181991 199 -GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:TIGR01187 150 lGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEE 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
283-515 |
3.88e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.39 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDrktAGLILQMS 362
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-PTKGTITINNINYNKLDHKLAAQLGIGIIYQE---LSVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNItlpsVVMKLIVRKF---GLIDSQLEKEIVRSFIEKLNIKTpSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDE 439
Cdd:PRK09700 97 VLENL----YIGRHLTKKVcgvNIIDWREMRVRAAMMLLRVGLKV-DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 440 PTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLKAAIPRSVK 515
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRELQ 247
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
285-490 |
4.03e-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: 91.59 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVrKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGK-----EIKIHSPrdavkngiglvPEDRKTaGLI 358
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGlEKP--DGGTIVLNGTvlfdsRKKINLP-----------PQQRKI-GLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQ-------MSVLHNITLpsvVMKlivRKFGLIDSQLEKEIVRSF-IEKLniKTPSPYQivenLSGGNQQKVVLAKWLAI 430
Cdd:cd03297 81 FQqyalfphLNVRENLAF---GLK---RKRNREDRISVDELLDLLgLDHL--LNRYPAQ----LSGGEKQRVALARALAA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 431 KPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03297 149 QPELLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
283-494 |
4.18e-21 |
|
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: 91.66 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGKEIkIHSPRdAVKNGIGLVPEDRktaGLILQM 361
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLlEP--DAGFATVDGFDV-VKEPA-EARRRLGFVSDST---GLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNItlpsvvmKLIVRKFGLIDSQLEKEiVRSFIEKLNIKtPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPT 441
Cdd:cd03266 94 TARENL-------EYFAGLYGLKGDELTAR-LEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490181991 442 RGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:cd03266 165 TGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
277-490 |
7.45e-21 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 89.75 E-value: 7.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHSPRDAVKNgIGLVPEDrktaG 356
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP-TSGEILIDGVDLRDLDLESLRKN-IAYVPQD----P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSVLHNItlpsvvmklivrkfglidsqlekeivrsfieklniktpspyqivenLSGGNQQKVVLAKWLAIKPKVLL 436
Cdd:cd03228 86 FLFSGTIRENI----------------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 437 LDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELpEILAMSDRILVMSEGR 490
Cdd:cd03228 120 LDEATSALDPETEALILEALRALA-KGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-254 |
8.08e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.16 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 2 MLNTEKEREVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNP 81
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 82 RE-AQEngIALIPQELDLVPNLSSAENIFLSREP----VNEFGVIEYQKMfEQASKLfsklgVNIDPKTK--VEDLSTSQ 154
Cdd:PRK10575 81 KAfARK--VAYLPQQLPAAEGMTVRELVAIGRYPwhgaLGRFGAADREKV-EEAISL-----VGLKPLAHrlVDSLSGGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 155 QQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPI 233
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
|
250 260
....*....|....*....|.
gi 490181991 234 EEfdhdklvrLMVGRSIDQFF 254
Cdd:PRK10575 233 AE--------LMRGETLEQIY 245
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
284-490 |
9.20e-21 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 90.67 E-value: 9.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 284 DDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRdavkngiglVPEDRKTAGLILQ--- 360
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE-PDSGTIIIDGLKLTDDKKN---------INELRQKVGMVFQqfn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 ----MSVLHNITLPSVvmklIVRKfglIDSQLEKEIVRSFIEKLNI---KTPSPYQivenLSGGNQQKVVLAKWLAIKPK 433
Cdd:cd03262 87 lfphLTVLENITLAPI----KVKG---MSKAEAEERALELLEKVGLadkADAYPAQ----LSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 434 VLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
279-490 |
1.20e-20 |
|
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: 90.39 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKihsprdavkngiGLVPEDRKTAgLI 358
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE-PTSGRIYIGGRDVT------------DLPPKDRDIA-MV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQ-------MSVLHNITLPsvvmkLIVRKFGlidsqlEKEI---VRSFIEKLNI-----KTPSpyqiveNLSGGNQQKVV 423
Cdd:cd03301 78 FQnyalyphMTVYDNIAFG-----LKLRKVP------KDEIderVREVAELLQIehlldRKPK------QLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 424 LAKWLAIKPKVLLLDEPTRGID----VNAKSEIYKLISEMavsGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-226 |
1.40e-20 |
|
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: 90.57 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGV-YPDyEGQIFLEGKEV---------R 77
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPT-SGTVRLAGQDLfaldedaraR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 78 FRNpreaqeNGIALIPQELDLVPNLSSAENIFLsrePVNEFGVIEyqkMFEQASKLFSKLGVN--ID--PKTkvedLSTS 153
Cdd:COG4181 87 LRA------RHVGFVFQSFQLLPTLTALENVML---PLELAGRRD---ARARARALLERVGLGhrLDhyPAQ----LSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 154 QQQMVAIAKALSLDAKIIIMDEPT----SAIGKRETEQLFNIIRslkNEGKSVIYISHRlEEIFEIADRVVVMRDGR 226
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTgnldAATGEQIIDLLFELNR---ERGTTLVLVTHD-PALAARCDRVLRLRAGR 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-226 |
1.63e-20 |
|
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: 90.19 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFP-----GVI--AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVY-PDyEGQIFlegkeVRFRN- 80
Cdd:COG4778 2 TTLLEVENLSKTFTlhlqgGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYlPD-SGSIL-----VRHDGg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 81 --------PRE---AQENGIALIPQELDLVPNLSSAEnifLSREPVNEFGViEYQKMFEQASKLFSKLGV-----NIDPK 144
Cdd:COG4778 76 wvdlaqasPREilaLRRRTIGYVSQFLRVIPRVSALD---VVAEPLLERGV-DREEARARARELLARLNLperlwDLPPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 145 TkvedLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRD 224
Cdd:COG4778 152 T----FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
..
gi 490181991 225 GR 226
Cdd:COG4778 228 FS 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
286-508 |
1.93e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 90.76 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 286 VSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrtEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDRKTAglilQMSVLH 365
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF----AMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 366 NITL--PSVVMKlivrkfGLIDSQLEkEIVRSFieKLNIKTPSPyqiVENLSGGNQQKVVLAK-----WLAIKP--KVLL 436
Cdd:PRK03695 89 YLTLhqPDKTRT------EAVASALN-EVAEAL--GLDDKLGRS---VNQLSGGEWQRVRLAAvvlqvWPDINPagQLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 437 LDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEV-TEEDLLKA 508
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVlTPENLAQV 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
283-494 |
1.96e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.71 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEvlgIYGLVG---AGRTELLEAIFGA-HPgrTEGKVFIGGKEIkihspRDAVKNGIGLVPEDRktaGLI 358
Cdd:COG4152 17 VDDVSFTVPKGE---IFGLLGpngAGKTTTIRIILGIlAP--DSGEVLWDGEPL-----DPEDRRRIGYLPEER---GLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQMSVLHNITLpsvvmklIVRKFGLIDSQLEKEIvRSFIEKLNIKtPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLD 438
Cdd:COG4152 84 PKMKVGEQLVY-------LARLKGLSKAEAKRRA-DEWLERLGLG-DRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 439 EPTRGID-VNAkSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:COG4152 155 EPFSGLDpVNV-ELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
16-234 |
2.20e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.79 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 16 RNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrNPREAQENGIALIPQE 95
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM---NDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 96 LDLVPNLSSAENIflsrepvnEFGV-------IEYQKMFEQASKLFsKLGVNIDPKTKveDLSTSQQQMVAIAKALSLDA 168
Cdd:PRK11000 84 YALYPHLSVAENM--------SFGLklagakkEEINQRVNQVAEVL-QLAHLLDRKPK--ALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 169 KIIIMDEPTSAIGKRETEQL-FNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR--KVGEgPIE 234
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRVQMrIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRvaQVGK-PLE 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-226 |
3.04e-20 |
|
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: 95.08 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 16 RNITKTFP--GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfRNPREAQENGIALIP 93
Cdd:TIGR01257 932 KNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 94 QELDLVPNLSSAENIFLSRE---PVNEFGVIEYQKMFEQAsklfsklGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKI 170
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYAQlkgRSWEEAQLEMEAMLEDT-------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 171 IIMDEPTSAIGKRETEQLFNIIRSLKNeGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
282-507 |
3.41e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.95 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 282 LVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDrktAGLILQM 361
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP-RDAGNIIIDDEDISLLPLHARARRGIGYLPQE---ASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNItlpsvVMKLIVRKFglIDSQLEKEIVRSFIEKLNIKTPSPyQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPT 441
Cdd:PRK10895 94 SVYDNL-----MAVLQIRDD--LSAEQREDRANELMEEFHIEHLRD-SMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 442 RGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLK 507
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVK 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
25-231 |
3.53e-20 |
|
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: 89.13 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 25 VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKevrfrnpreaqengIALIpqeLDL----VP 100
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--------------VSSL---LGLgggfNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 101 NLSSAENIFLSrepvnefGVI-----EYQKMFEQASKLFSKLGVNIDpkTKVEDLSTSQQQMVAIAKALSLDAKIIIMDE 175
Cdd:cd03220 98 ELTGRENIYLN-------GRLlglsrKEIDEKIDEIIEFSELGDFID--LPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 176 PTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-251 |
3.58e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.54 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPD-----YEGQIFLEGKEV-RFRNPREAQE 86
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 87 NgIALIPQELDLVPnLSSAENIFLSrepVNEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVED----LSTSQQQMVAIAK 162
Cdd:PRK14271 102 R-VGMLFQRPNPFP-MSIMDNVLAG---VRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 163 ALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEgKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEF----DH 238
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLfsspKH 255
|
250
....*....|...
gi 490181991 239 DKLVRLMVGRSID 251
Cdd:PRK14271 256 AETARYVAGLSGD 268
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
283-494 |
4.97e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.95 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIfGA--HPgrTEGKVFIGGKEIKIHSPRDAVK---NGIGLVPEDrktAGL 357
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL-GGldRP--TSGEVLIDGQDISSLSERELARlrrRHIGFVFQF---FNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQMSVLHNITLPSVVMKLIVRKfglidsqlEKEIVRSFIEKLNI-----KTPSpyqiveNLSGGNQQKVVLAKWLAIKP 432
Cdd:COG1136 98 LPELTALENVALPLLLAGVSRKE--------RRERARELLERVGLgdrldHRPS------QLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 433 KVLLLDEPTRGIDVNAKSEIYKLISEMAV-SGMGVVMVSSElPEILAMSDRILVMSEGRKTAE 494
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
283-513 |
5.43e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 89.38 E-value: 5.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSPRdavkngIGLVP-EDRktagLILQ 360
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGlEKP--TSGEVLVDGKPVTGPGPD------RGVVFqEPA----LLPW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 MSVLHNITLPsvvmkLIVRKfglIDSQLEKEIVRSFIEKLNIKTPS---PYQivenLSGGNQQKVVLAKWLAIKPKVLLL 437
Cdd:COG1116 95 LTVLDNVALG-----LELRG---VPKAERRERARELLELVGLAGFEdayPHQ----LSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 438 DEP-------TRgIDVNAksEIYKLISEmavSGMGVVMVSSELPEILAMSDRILVMSEG--------------------R 490
Cdd:COG1116 163 DEPfgaldalTR-ERLQD--ELLRLWQE---TGKTVLFVTHDVDEAVFLADRVVVLSARpgriveeidvdlprprdrelR 236
|
250 260
....*....|....*....|....*
gi 490181991 491 KTAEF--LREEVTeeDLLKAAIPRS 513
Cdd:COG1116 237 TSPEFaaLRAEIL--DLLREEAERA 259
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
283-486 |
6.04e-20 |
|
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: 90.50 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHP--GRTEGKVFIGGKEIKIHSPRDAVK---NGIGLVPEDRKTAgl 357
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppGITSGEILFDGEDLLKLSEKELRKirgREIQMIFQDPMTS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 iL--QMSVLHNITLPsvvmkliVRKFGLIDSQLEKEIVRSFIEKLNIktPSPYQIVEN----LSGGNQQKVVLAKWLAIK 431
Cdd:COG0444 99 -LnpVMTVGDQIAEP-------LRIHGGLSKAEARERAIELLERVGL--PDPERRLDRypheLSGGMRQRVMIARALALE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 432 PKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVM 486
Cdd:COG0444 169 PKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
26-245 |
7.65e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.76 E-value: 7.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 26 IAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGK---------EVR------FRNPrEAQ----- 85
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtsdeenlwDIRnkagmvFQNP-DNQivati 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 86 -ENGIALIPQELDLVPnlssaENIflsREPVNE----FGVIEYQKmfeQASKLfsklgvnidpktkvedLSTSQQQMVAI 160
Cdd:PRK13633 103 vEEDVAFGPENLGIPP-----EEI---RERVDEslkkVGMYEYRR---HAPHL----------------LSGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 161 AKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEiADRVVVMRDGRKVGEG-PIEEFdh 238
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGtPKEIF-- 232
|
....*..
gi 490181991 239 dKLVRLM 245
Cdd:PRK13633 233 -KEVEMM 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-234 |
8.59e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.59 E-value: 8.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGvYPDYE---GQIFLEGKEVRFRNPRE-AQEnG 88
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPKYEvtsGSILLDGEDILELSPDErARA-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALI---PQELDLVPN---LSSAEN-IFLSREPVNEFgvieYQKMFEQASKL-----FSKLGVNidpktkvEDLSTSQQQ 156
Cdd:COG0396 79 IFLAfqyPVEIPGVSVsnfLRTALNaRRGEELSAREF----LKLLKEKMKELgldedFLDRYVN-------EGFSGGEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 157 MVAIAKALSLDAKIIIMDEPTS-----AIGKreteqLFNIIRSLKNEGKSVIYISH--R-LEEIfeIADRVVVMRDGRKV 228
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSgldidALRI-----VAEGVNKLRSPDRGILIITHyqRiLDYI--KPDFVHVLVDGRIV 220
|
....*.
gi 490181991 229 GEGPIE 234
Cdd:COG0396 221 KSGGKE 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
10-231 |
9.52e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.08 E-value: 9.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTF---------PGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEV---- 76
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 77 -RFRNPREA---QENGIALIP-----QELDLVPNLSSaeniflsrepvnEFGVIEYQKMFEQASKLFSKLG--VNIDPKT 145
Cdd:PRK15112 82 ySYRSQRIRmifQDPSTSLNPrqrisQILDFPLRLNT------------DLEPEQREKQIIETLRQVGLLPdhASYYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 146 kvedLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRD 224
Cdd:PRK15112 150 ----LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
....*..
gi 490181991 225 GRKVGEG 231
Cdd:PRK15112 226 GEVVERG 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-228 |
1.11e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.60 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTF-PG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEV-------R--- 77
Cdd:COG1101 2 LELKNLSKTFnPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykRaky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 78 ----FRNPREaqenGIAlipqeldlvPNLSSAENIFLS-----REPVNeFGVIEYQKmfEQASKLFSKLGVNID--PKTK 146
Cdd:COG1101 82 igrvFQDPMM----GTA---------PSMTIEENLALAyrrgkRRGLR-RGLTKKRR--ELFRELLATLGLGLEnrLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 147 VEDLSTSQQQmvaiakALSL------DAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGK-SVIYISHRLEEIFEIADRV 219
Cdd:COG1101 146 VGLLSGGQRQ------ALSLlmatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRL 219
|
....*....
gi 490181991 220 VVMRDGRKV 228
Cdd:COG1101 220 IMMHEGRII 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-236 |
1.15e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 31 VTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKevrfrnPREAQENGIALIPQELDLV---PNlssaEN 107
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK------PLDYSKRGLLALRQQVATVfqdPE----QQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 108 IFLS------REPVNEFGVIEYQ--KMFEQASKLFSKLGVNIDPktkVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSA 179
Cdd:PRK13638 90 IFYTdidsdiAFSLRNLGVPEAEitRRVDEALTLVDAQHFRHQP---IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 180 IGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG-PIEEF 236
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGaPGEVF 224
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
18-226 |
1.22e-19 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 87.47 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 18 ITKTFPgVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILaGVYPDYE-GQIFLEGKEVRfrNPREAQE-----NGIAL 91
Cdd:NF038007 12 ITKTIK-TKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNII-GMFDSLDsGSLTLAGKEVT--NLSYSQKiilrrELIGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENIFLsrePVNEFGVIEYQKMfEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKII 171
Cdd:NF038007 88 IFQSFNLIPHLSIFDNVAL---PLKYRGVAKKERI-ERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 172 IMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRlEEIFEIADRVVVMRDGR 226
Cdd:NF038007 164 LADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDGK 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
278-500 |
1.31e-19 |
|
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: 87.64 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 278 RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSPRDavkngiglVPEDRKTAG 356
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERP--TSGSVLVDGTDLTLLSGKE--------LRKARRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQ-------MSVLHNITLPsvvMKlivrkfglIDSQLEKEIVRSFIEKLNI--------KTPSpyqiveNLSGGNQQK 421
Cdd:cd03258 86 MIFQhfnllssRTVFENVALP---LE--------IAGVPKAEIEERVLELLELvgledkadAYPA------QLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 422 VVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEV 500
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-226 |
1.37e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.02 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIALIPQELDlvpnlssaeN 107
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-IGMVFQNPD---------N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 108 IFL--SREPVNEFGV----IEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIG 181
Cdd:PRK13650 93 QFVgaTVEDDVAFGLenkgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490181991 182 KRETEQLFNIIRSLKNE-GKSVIYISHRLEEIfEIADRVVVMRDGR 226
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
282-518 |
1.46e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.67 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 282 LVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGKEIKIHSPRdAVKNGIGLVPEDrktAGLILQ 360
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTlTP--TAGTVLVAGDDVEALSAR-AASRRVASVPQD---TSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 MSVlhnitlpsvvmKLIVR--------KFGLIDSQlEKEIVRSFIEKLNIkTPSPYQIVENLSGGNQQKVVLAKWLAIKP 432
Cdd:PRK09536 92 FDV-----------RQVVEmgrtphrsRFDTWTET-DRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 433 KVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLKAAIPR 512
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDA 238
|
....*.
gi 490181991 513 SVKVET 518
Cdd:PRK09536 239 RTAVGT 244
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-272 |
1.47e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.95 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEG----------KEVR------FRNPR-----EAQ 85
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklSDIRkkvglvFQYPEyqlfeETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 86 ENGIALIPQELdlvpNLSSAENIFLSREPVNEFGvIEYQKMFEQASklFsklgvnidpktkveDLSTSQQQMVAIAKALS 165
Cdd:PRK13637 102 EKDIAFGPINL----GLSEEEIENRVKRAMNIVG-LDYEDYKDKSP--F--------------ELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 166 LDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGK-SVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEF--DHDKLV 242
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVfkEVETLE 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 490181991 243 RlmVGRSIDQFF-----IKERA-TITDEIFRVEGIK 272
Cdd:PRK13637 241 S--IGLAVPQVTylvrkLRKKGfNIPDDIFTIEEAK 274
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
13-244 |
1.72e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 87.93 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTL---MKILagVYPDyEGQIFLEGKEVRFR---------- 79
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFlrcINLL--ETPD-SGEIRVGGEEIRLKpdrdgelvpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 80 NPREAQE--NGIALIPQELDLVPNLSSAENIFLSrePVNEFGVIEYQKMfEQASKLFSKLGVnidpkTKVED-----LST 152
Cdd:COG4598 86 DRRQLQRirTRLGMVFQSFNLWSHMTVLENVIEA--PVHVLGRPKAEAI-ERAEALLAKVGL-----ADKRDaypahLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 153 SQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGP 232
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
250
....*....|...
gi 490181991 233 IEE-FDHDKLVRL 244
Cdd:COG4598 238 PAEvFGNPKSERL 250
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-235 |
1.84e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.83 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 14 EARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEV-RFRNPREAQEngIALI 92
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELAKR--LAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFLSREPVNEfGVI--EYQKMFEQASKLFsklgvNIDPktkVED-----LSTSQQQMVAIAKALS 165
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSK-GRLtaEDREIIDEAIAYL-----DLED---LADryldeLSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 166 LDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHrleeifEI------ADRVVVMRDGRKVGEGPIEE 235
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH------DInfascyADHIVAMKDGRVVAQGTPEE 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
283-494 |
1.98e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 87.04 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIkIHSPRDaVKNGIGLVPEDRKTAGlilQMS 362
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKP-TSGRATVAGHDV-VREPRE-VRRRIGIVFQDLSVDD---ELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNitlpsvvMKLIVRKFGLIDSQLEKEI--VRSFIEKLNIKTpspyQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEP 440
Cdd:cd03265 90 GWEN-------LYIHARLYGVPGAERRERIdeLLDFVGLLEAAD----RLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 441 TRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-235 |
2.32e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.19 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPD----YEGQIFLEGKEVRFRNPRE 83
Cdd:COG4170 3 LLDIRNLTIEIDTpqgrVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 84 AQE---NGIALIPQE----LDlvPNLSS----AENIflsrePVNEFGVIEYQKMF---EQASKLFSKLGVNiDPKTKVE- 148
Cdd:COG4170 83 RRKiigREIAMIFQEpsscLD--PSAKIgdqlIEAI-----PSWTFKGKWWQRFKwrkKRAIELLHRVGIK-DHKDIMNs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 149 ---DLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRD 224
Cdd:COG4170 155 yphELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYC 234
|
250
....*....|.
gi 490181991 225 GRKVGEGPIEE 235
Cdd:COG4170 235 GQTVESGPTEQ 245
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-235 |
2.39e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIALI 92
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFLSREP-VNEFGVIEY--QKMFEQAsklFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAK 169
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPhRSRFDTWTEtdRAAVERA---MERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 170 IIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-239 |
2.66e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 91.06 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPdYEGQIFLEGKEVRFRNPREAQENgIAL 91
Cdd:PRK11174 350 IEAEDLEILSPdGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESWRKH-LSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQEldlvPNL---SSAENIFLSREPVNEfgvIEYQKMFEQA--SKLFSKLGVNIDpkTKVED----LSTSQQQMVAIAK 162
Cdd:PRK11174 428 VGQN----PQLphgTLRDNVLLGNPDASD---EQLQQALENAwvSEFLPLLPQGLD--TPIGDqaagLSVGQAQRLALAR 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 163 ALSLDAKIIIMDEPTSAIGKReTEQLfnIIRSLKN--EGKSVIYISHRLEEIFEIaDRVVVMRDGRKVGEGPIEEFDHD 239
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAH-SEQL--VMQALNAasRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQA 573
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
3.54e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.89 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKI---LAGVYPD--YEGQIFLEGKEVrFRNPREAQEN 87
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEarVSGEVYLDGQDI-FKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 GIALIPQELDLVPNLSSAENIFLSREpVNEFgVIEYQKMFEQASKLFSKLGVNIDPKTKVE----DLSTSQQQMVAIAKA 163
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLK-LNRL-VKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 164 LSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEgKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
266-490 |
3.60e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 84.96 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 266 FRVEGIKLWSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNgI 345
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR-PTSGRVRLDGADISQWDPNELGDH-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 346 GLVPEDRKtaglILQMSVLHNItlpsvvmklivrkfglidsqlekeivrsfieklniktpspyqivenLSGGNQQKVVLA 425
Cdd:cd03246 79 GYLPQDDE----LFSGSIAENI----------------------------------------------LSGGQRQRLGLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 426 KWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSElPEILAMSDRILVMSEGR 490
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGR 172
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-226 |
3.82e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.58 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 26 IAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrNPREAQENgIALIPQELDLVPNLSSA 105
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI---TPETGNKN-LKKLRKKVSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 106 ---ENIFLSR---EPVNeFGVIEyQKMFEQASKLFSKLGVNIDPKTKVE-DLSTSQQQMVAIAKALSLDAKIIIMDEPTS 178
Cdd:PRK13641 97 qlfENTVLKDvefGPKN-FGFSE-DEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490181991 179 AIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-243 |
4.15e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVI-AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIA 90
Cdd:PRK13652 3 LIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDlvpnlssaENIF-------LSREPVNeFGVIEyQKMFEQASKLFSKLGVNiDPKTKV-EDLSTSQQQMVAIAK 162
Cdd:PRK13652 82 LVFQNPD--------DQIFsptveqdIAFGPIN-LGLDE-ETVAHRVSSALHMLGLE-ELRDRVpHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 163 ALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE-FDHDK 240
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEiFLQPD 230
|
...
gi 490181991 241 LVR 243
Cdd:PRK13652 231 LLA 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
283-514 |
4.72e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 89.88 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHP-GRTEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDrktAGLILQM 361
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhGTWDGEIYWSGSPLKASNIRDTERAGIVIIHQE---LTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNITLPSVvmklIVRKFGLIDSQLEKEIVRSFIEKLNIKTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPT 441
Cdd:TIGR02633 94 SVAENIFLGNE----ITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 442 RGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLKAAIPRSV 514
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGREI 242
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
283-490 |
4.78e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 85.72 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHpGRTEGKVFIGGKEIKIHSPRDaVKNGIGLVPED-RKTAGlilqm 361
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY-KPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQDvTLFYG----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNITLPSVVMKlivrkfgliDSQLEKEIVRSFIEKLNIKTPSPY--QIVE---NLSGGNQQKVVLAKWLAIKPKVLL 436
Cdd:cd03245 93 TLRDNITLGAPLAD---------DERILRAAELAGVTDFVNKHPNGLdlQIGErgrGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 437 LDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPeILAMSDRILVMSEGR 490
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSGR 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
280-494 |
5.31e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.55 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSPRdaVKNGIGLVPEdrkTAGLI 358
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHP--DAGSISLCGEPVPSRARH--ARQRVGVVPQ---FDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQMSVLHNitlpsvvMKLIVRKFGLIDSQLeKEIVRSFIE--KLNIKTPSPyqiVENLSGGNQQKVVLAKWLAIKPKVLL 436
Cdd:PRK13537 93 PDFTVREN-------LLVFGRYFGLSAAAA-RALVPPLLEfaKLENKADAK---VGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 437 LDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
283-490 |
5.42e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.41 E-value: 5.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGKEIkihsprdaVKNGIGLvPEDRKTAGLILQM 361
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLlKP--TSGKIIIDGVDI--------TDKKVKL-SDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVlHNItLPSVVMKLIV---RKFGLIDSQLEKEIVRSF----IEKLNIKTPSPYQivenLSGGNQQKVVLAKWLAIKPKV 434
Cdd:PRK13637 92 PE-YQL-FEETIEKDIAfgpINLGLSEEEIENRVKRAMnivgLDYEDYKDKSPFE----LSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 435 LLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-242 |
5.97e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.88 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 4 NTEKEREVLLEARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNp 81
Cdd:PRK11160 330 STAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 82 rEAQ-ENGIALIPQELDLVpNLSSAENIFLSREPVNEFGVIE------YQKMFEQASKLFSKLGvnidpktkvE---DLS 151
Cdd:PRK11160 409 -EAAlRQAISVVSQRVHLF-SATLRDNLLLAAPNASDEALIEvlqqvgLEKLLEDDKGLNAWLG---------EggrQLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 152 TSQQQMVAIAKALSLDAKIIIMDEPTSAIgKRETEQLfniIRSLKNE---GKSVIYISHRLEEIfEIADRVVVMRDGRKv 228
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGL-DAETERQ---ILELLAEhaqNKTVLMITHRLTGL-EQFDRICVMDNGQI- 551
|
250
....*....|....
gi 490181991 229 gegpIEEFDHDKLV 242
Cdd:PRK11160 552 ----IEQGTHQELL 561
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-240 |
7.32e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.83 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKevrfrnPREAQENGIA 90
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK------PIDYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVpnLSSAENIFLSREPVNE--FGVIEYQ----KMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKAL 164
Cdd:PRK13636 79 KLRESVGMV--FQDPDNQLFSASVYQDvsFGAVNLKlpedEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 165 SLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDK 240
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-243 |
1.10e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG--VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVY-PD--YEGQIFLEGKEVRFRNPREAQEN 87
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlPDdnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 gIALIPQELDlvpnlssaeNIFLSREPVNE--FGV----IEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIA 161
Cdd:PRK13640 86 -VGIVFQNPD---------NQFVGATVGDDvaFGLenraVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 162 KALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIfEIADRVVVMRDGRKVGEG-PIEEFDHD 239
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGsPVEIFSKV 234
|
....
gi 490181991 240 KLVR 243
Cdd:PRK13640 235 EMLK 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-228 |
1.14e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 85.02 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTfpgVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYE---GQIFLEGKEvrfRNPREAQE 86
Cdd:cd03234 8 DVGLKAKNWNKY---ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP---RKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 87 NgIALIPQELDLVPNLSSAE-----NIFLSREPVNEFgvieyQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIA 161
Cdd:cd03234 82 C-VAYVRQDDILLPGLTVREtltytAILRLPRKSSDA-----IRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 162 KALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHR-LEEIFEIADRVVVMRDGRKV 228
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
277-490 |
1.21e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 84.72 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGKEIKIHSPRD--AVKNGIGLVPEDRK 353
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEeRP--TSGQVLVNGQDLSRLKRREipYLRRRIGVVFQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 354 tagLILQMSVLHNITLPsvvmkLIVRKFGlidsqlEKEI---VRSFIEKLNIKTPSpYQIVENLSGGNQQKVVLAKWLAI 430
Cdd:COG2884 90 ---LLPDRTVYENVALP-----LRVTGKS------RKEIrrrVREVLDLVGLSDKA-KALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 431 KPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-232 |
1.31e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.14 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 4 NTEKEREVLLEARNITKTFP-----------GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLE 72
Cdd:PRK10261 305 DTVVDGEPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFN 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 73 GKEVRFRNPREAQ--ENGIALIPQE--LDLVPNLSSAENIFlsrEPVNEFGVIEYQKMFEQASKLFSKLGVNIDPKTKV- 147
Cdd:PRK10261 385 GQRIDTLSPGKLQalRRDIQFIFQDpyASLDPRQTVGDSIM---EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYp 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 148 EDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:PRK10261 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
....*.
gi 490181991 227 KVGEGP 232
Cdd:PRK10261 542 IVEIGP 547
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
271-490 |
1.32e-18 |
|
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: 83.75 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 271 IKLWSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPGRTEGKVFIGGKEIKIHSPRDAvkngIGLVP 349
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVSGEVLINGRPLDKRSFRKI----IGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 350 EDrktaglilqmsvlhNITLPSvvmkLIVRKFGLIDSQLekeivRSfieklniktpspyqivenLSGGNQQKVVLAKWLA 429
Cdd:cd03213 89 QD--------------DILHPT----LTVRETLMFAAKL-----RG------------------LSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 430 IKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMV----SSelpEILAMSDRILVMSEGR 490
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSihqpSS---EIFELFDKLLLLSQGR 189
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
283-490 |
2.11e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 86.67 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKihsprdavkngiGLVPEDRKTA------ 355
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDP--TSGEILIGGRDVT------------DLPPKDRNIAmvfqsy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 356 GLILQMSVLHNITLPsvvmkLIVRKFGlidsqlEKEI---VRSFIEKLNI-----KTPSpyqiveNLSGGNQQKVVLAKW 427
Cdd:COG3839 85 ALYPHMTVYENIAFP-----LKLRKVP------KAEIdrrVREAAELLGLedlldRKPK------QLSGGQRQRVALGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 428 LAIKPKVLLLDEPTRGID----VNAKSEIYKLISEMavsGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-231 |
2.40e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.63 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 23 PGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIALIPQELDLVpNL 102
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-VALVGQEPVLF-SG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 103 SSAENIF--LSREPVNEfgvIEYQKMFEQASKLFSKL--GVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTS 178
Cdd:TIGR00958 570 SVRENIAygLTDTPDEE---IMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490181991 179 AIgKRETEQLFNIIRSLKneGKSVIYISHRLEEIfEIADRVVVMRDGRKVGEG 231
Cdd:TIGR00958 647 AL-DAECEQLLQESRSRA--SRTVLLIAHRLSTV-ERADQILVLKKGSVVEMG 695
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
277-508 |
2.71e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 87.90 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKiHSPRDAVKNGIGLVPEDrktaG 356
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-PQSGSITLGGVDLR-DLDEDDLRRRIAVVPQR----P 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSVLHNItlpsvvmkLIVRKfGLIDSQLEK--EIVR--SFIEKLniktPSPYQIV-----ENLSGGNQQKVVLAKW 427
Cdd:COG4987 419 HLFDTTLRENL--------RLARP-DATDEELWAalERVGlgDWLAAL----PDGLDTWlgeggRRLSGGERRRLALARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 428 LAIKPKVLLLDEPTRGIDVNAKSEIYKLISEmAVSGMGVVMVSSELPEILAMsDRILVMSEGRktaefLREEVTEEDLLK 507
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGLERM-DRILVLEDGR-----IVEQGTHEELLA 558
|
.
gi 490181991 508 A 508
Cdd:COG4987 559 Q 559
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-234 |
2.99e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 8 EREVLLEARNITKTFP---GV--------IAVNNVTLQIYKGEVCALVGENGAGKST----LMKILAGvypdyEGQIFLE 72
Cdd:PRK15134 271 PASPLLDVEQLQVAFPirkGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 73 GKEVRFRNPREaqengiaLIP--QELDLV---PNlsSAENIFLSREPVNEFGVIEYQKMF---EQASKLFSKLG-VNIDP 143
Cdd:PRK15134 346 GQPLHNLNRRQ-------LLPvrHRIQVVfqdPN--SSLNPRLNVLQIIEEGLRVHQPTLsaaQREQQVIAVMEeVGLDP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 144 KTKVE---DLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGK-SVIYISHRLEEIFEIADRV 219
Cdd:PRK15134 417 ETRHRypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQV 496
|
250
....*....|....*
gi 490181991 220 VVMRDGRKVGEGPIE 234
Cdd:PRK15134 497 IVLRQGEVVEQGDCE 511
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
278-490 |
3.32e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 278 RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIK---IHspRDAvKNGIGLVPED-- 351
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlVKP--DSGRIFLDGEDIThlpMH--KRA-RLGIGYLPQEas 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 352 --RKtaglilqMSVLHNItlpsvvmkLIVRKFGLIDSQLEKEIVRSFIEKLNI----KTPSPYqivenLSGGNQQKVVLA 425
Cdd:COG1137 89 ifRK-------LTVEDNI--------LAVLELRKLSKKEREERLEELLEEFGIthlrKSKAYS-----LSGGERRRVEIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 426 KWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVM----VSselpEILAMSDRILVMSEGR 490
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLItdhnVR----ETLGICDRAYIISEGK 213
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-234 |
3.95e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 83.92 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 1 MMLNTekereVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGvYPDY---EGQIFLEGKEVR 77
Cdd:CHL00131 1 MNKNK-----PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAYkilEGDILFKGESIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 78 FRNPREAQENGIAL---IPQELDLVPN---LSSAENIFLSREPVNEFGVIEYQKMFEQASKLfsklgVNIDP----KTKV 147
Cdd:CHL00131 75 DLEPEERAHLGIFLafqYPIEIPGVSNadfLRLAYNSKRKFQGLPELDPLEFLEIINEKLKL-----VGMDPsflsRNVN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 148 EDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISH--RLEEiFEIADRVVVMRDG 225
Cdd:CHL00131 150 EGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLD-YIKPDYVHVMQNG 228
|
....*....
gi 490181991 226 RKVGEGPIE 234
Cdd:CHL00131 229 KIIKTGDAE 237
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-231 |
4.57e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 83.54 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 25 VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGkEVRFRNPREAQENGIALIPQELDLVPNLSS 104
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 105 AENIFLSREpVNEFGVIEYQKMFEQASKLfsklgVNIDP--KTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGK 182
Cdd:cd03267 113 IDSFYLLAA-IYDLPPARFKKRLDELSEL-----LDLEEllDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490181991 183 RETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:cd03267 187 VAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
280-494 |
4.99e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPGRteGKVFIGGKEIkihsPRDA--VKNGIGLVPE-DRkta 355
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGmTSPDA--GKITVLGVPV----PARArlARARIGVVPQfDN--- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 356 gLILQMSVLHNitlpsvvmkLIV--RKFGLIDSQLEkEIVRSFIE--KLNIKTPSPyqiVENLSGGNQQKVVLAKWLAIK 431
Cdd:PRK13536 125 -LDLEFTVREN---------LLVfgRYFGMSTREIE-AVIPSLLEfaRLESKADAR---VSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 432 PKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-274 |
5.29e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.14 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 14 EARNITKTF------PG---------------VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGV-YPDyEGQIfl 71
Cdd:COG4586 3 EVENLSKTYrvyekePGlkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIlVPT-SGEV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 72 egkEVRFRNP-REAQENG--IALI-PQELDLVPNLSSAENIFLSRE----PVNEFG--VIEYQKMFEQASKLfsklgvni 141
Cdd:COG4586 80 ---RVLGYVPfKRRKEFArrIGVVfGQRSQLWWDLPAIDSFRLLKAiyriPDAEYKkrLDELVELLDLGELL-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 142 dpKTKVEDLSTSqQQMVA-IAKALSLDAKIIIMDEPTsaIG-----KretEQLFNIIRSLKNE-GKSVIYISHRLEEIFE 214
Cdd:COG4586 149 --DTPVRQLSLG-QRMRCeLAAALLHRPKILFLDEPT--IGldvvsK---EAIREFLKEYNRErGTTILLTSHDMDDIEA 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 215 IADRVVVMRDGRKVGEGPIEE----FDHDKLVRLMVGRSIDQFFIKERAtitdEIFRVEGIKLW 274
Cdd:COG4586 221 LCDRVIVIDHGRIIYDGSLEElkerFGPYKTIVLELAEPVPPLELPRGG----EVIEREGNRVR 280
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
283-521 |
5.47e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 86.71 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHpGRTEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDrktAGLILQMS 362
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIY-QKDSGSILFQGKEIDFKSSKEALENGISMVHQE---LNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNITLPSVVMKLIvrkfgLIDSQLEKEIVRSFIEKLNIKTpSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTR 442
Cdd:PRK10982 90 VMDNMWLGRYPTKGM-----FVDQDKMYRDTKAIFDELDIDI-DPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 443 GIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLKAAIPRsvkvETTQR 521
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGR----SLTQR 238
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
283-490 |
5.73e-18 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 83.85 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSP---RDAVKNGIGLVpedRKTAGLI 358
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRlIEP--TSGKVLIDGQDIAAMSRkelRELRRKKISMV---FQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQMSVLHNITlpsvvmklivrkFGL----IDSQLEKEIVRSFIEKLNIKtPSPYQIVENLSGGNQQKVVLAKWLAIKPKV 434
Cdd:cd03294 115 PHRTVLENVA------------FGLevqgVPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 435 LLLDEPTRGID----VNAKSEIYKLISEMavsGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03294 182 LLMDEAFSALDplirREMQDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGR 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
280-490 |
6.66e-18 |
|
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: 82.14 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIkiHSPRDAVKNGIGLVPEDrktAGLIL 359
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP-PSAGEVLWNGEPI--RDAREDYRRRLAYLGHA---DGLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 360 QMSVLHNITLpsvVMKLivrkFGLIDSQLEkeiVRSFIEKLNIktpSPY--QIVENLSGGNQQKVVLAKWLAIKPKVLLL 437
Cdd:COG4133 89 ELTVRENLRF---WAAL----YGLRADREA---IDEALEAVGL---AGLadLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490181991 438 DEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAmsDRILVMSEGR 490
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA--ARVLDLGDFK 206
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
287-503 |
7.13e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.88 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 287 SFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPGRteGKVFIGGKEIkihsprdavkngIGLVPEDRKTAgLILQ----- 360
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDS--GRILWNGQDL------------TALPPAERPVS-MLFQennlf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 --MSVLHNITL---PSvvMKLivrkfglidSQLEKEIVRSFIEKLNI---KTPSPYQivenLSGGNQQKVVLAKWLAIKP 432
Cdd:COG3840 84 phLTVAQNIGLglrPG--LKL---------TAEQRAQVEQALERVGLaglLDRLPGQ----LSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 433 KVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR-----KTAEFLREEVTEE 503
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRiaadgPTAALLDGEPPPA 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-242 |
7.71e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 7.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLeGKEVRFRNPREAQEngIALIPQELDLVPNLSSAE 106
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAIPANLKKIKE--VKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 107 NIFLSREPVNEFGVIEYQKMFEQASKLFSKLGVNID-PKTKVE----DLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIG 181
Cdd:PRK13645 103 LFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQlPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 182 KRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG-PIEEFDHDKLV 242
Cdd:PRK13645 183 PKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGsPFEIFSNQELL 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
278-494 |
8.41e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 82.77 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 278 RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGkeIKIHSPRDAVKNGIGLVPEDRKTag 356
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQP--TSGEVRVAG--LVPWKRRKKFLRRIGVVFGQKTQ-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSVLHNITLpsvvMKLIVRkfglIDSQLEKEIVRSFIEKLNIkTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLL 436
Cdd:cd03267 106 LWWDLPVIDSFYL----LAAIYD----LPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 437 LDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
279-507 |
8.48e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.14 E-value: 8.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIfgahpGR----TEGKVFIGGKEIKIHSPRDAVKNgIGLVPEdrkt 354
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCF-----ARlltpQSGTVFLGDKPISMLSSRQLARR-LALLPQ---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 355 aglilQMSVLHNITlpsvVMKLI-------VRKFGLIdSQLEKEIVRSFIEKLNIKTPSPyQIVENLSGGNQQKVVLAKW 427
Cdd:PRK11231 84 -----HHLTPEGIT----VRELVaygrspwLSLWGRL-SAEDNARVNQAMEQTRINHLAD-RRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 428 LAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLK 507
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLR 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-237 |
1.39e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.50 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 11 VLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLeGKEVRfrnpreaqengIA 90
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELD-LVPNLSSAENIFLSREPVNEFGVIEYQKMFeqaskLFSklgvNIDPKTKVEDLSTSQQQMVAIAKALSLDAK 169
Cdd:COG0488 382 YFDQHQEeLDPDKTVLDELRDGAPGGTEQEVRGYLGRF-----LFS----GDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 170 IIIMDEPTsaigkreteqlfN---------IIRSLKN-EGkSVIYISH-R--LEEIfeiADRVVVMRDGRkvgegpIEEF 236
Cdd:COG0488 453 VLLLDEPT------------NhldietleaLEEALDDfPG-TVLLVSHdRyfLDRV---ATRILEFEDGG------VREY 510
|
.
gi 490181991 237 D 237
Cdd:COG0488 511 P 511
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-235 |
1.58e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.78 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVI-AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNpREAQENGIA 90
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 91 LIPQELDLVpNLSSAENIFLSREPVNEFGVIEYQKMfEQASKLFSK--LGVNIDPKTKVEDLSTSQQQMVAIAKALSLDA 168
Cdd:PRK13657 413 VVFQDAGLF-NRSIEDNIRVGRPDATDEEMRAAAER-AQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 169 KIIIMDEPTSAIgKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEiADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK13657 491 PILILDEATSAL-DVETEAKVKAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-235 |
1.64e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.55 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 32 TLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPreAQENgIALIPQELDLVPNLSSAENIFLS 111
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP--SRRP-VSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 112 REP---VNEFGVIEYQKMFEQAS--KLFSKLgvnidPKtkveDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIG---KR 183
Cdd:PRK10771 96 LNPglkLNAAQREKLHAIARQMGieDLLARL-----PG----QLSGGQRQRVALARCLVREQPILLLDEPFSALDpalRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 184 ETEQLFNII---RSLknegkSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK10771 167 EMLTLVSQVcqeRQL-----TLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
29-226 |
2.15e-17 |
|
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: 80.59 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 29 NNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGkevrfrnpreaqenGIALIPQEldlvPNLSSA--- 105
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQE----PWIQNGtir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 106 ENIFlsrepvneFGVIEYQKMFEQASKL------FSKL-----------GVNidpktkvedLSTSQQQMVAIAKALSLDA 168
Cdd:cd03250 84 ENIL--------FGKPFDEERYEKVIKAcalepdLEILpdgdlteigekGIN---------LSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 169 KIIIMDEPTSAIGKRETEQLF-NIIRSLKNEGKSVIYISHRLeEIFEIADRVVVMRDGR 226
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-235 |
3.41e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRF-----RNPREAQENGIALIPQELDLVPNL 102
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 103 SSAENIFLsrePVNEFGVIEYQKMFEQASKLFSKLG----VNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTS 178
Cdd:PRK14246 106 SIYDNIAY---PLKSHGIKEKREIKKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 179 AIGKRETEQLFNIIRSLKNEgKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
283-489 |
3.59e-17 |
|
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: 80.59 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSP-RDAVKNGIGLVPedrktaglilQ 360
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQP--TSGGVILEGKQITEPGPdRMVVFQNYSLLP----------W 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 MSVLHNITLpsvVMKLIVRKFglidSQLEKE-IVRSFIEKLNIKTPSPYQIVEnLSGGNQQKVVLAKWLAIKPKVLLLDE 439
Cdd:TIGR01184 69 LTVRENIAL---AVDRVLPDL----SKSERRaIVEEHIALVGLTEAADKRPGQ-LSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181991 440 PTRGIDVNAKSEIY-KLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEG 489
Cdd:TIGR01184 141 PFGALDALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-235 |
3.76e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.54 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 26 IAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEG---KEVRFRNPREAQENGIALIPQELDLVPNL 102
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 103 SSAENIFLSRepvnEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGK 182
Cdd:PRK10070 122 TVLDNTAFGM----ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 183 R-ETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK10070 198 LiRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
12-226 |
3.90e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTF-PGVI---AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGK---EVRFRNPREA 84
Cdd:PRK11629 5 LLQCDNLCKRYqEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 85 QENGIALIPQELDLVPNLSSAENIFLsrePVnEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKAL 164
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAM---PL-LIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 165 SLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLeeifEIADRV---VVMRDGR 226
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL----QLAKRMsrqLEMRDGR 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
282-490 |
5.26e-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: 80.42 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 282 LVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIfgahpGR----TEGKVFIGGKEIKIHSPRDAVKNgIGLVPEDrktAGL 357
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-----NRliepTSGEIFIDGEDIREQDPVELRRK-IGYVIQQ---IGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQMSVLHNITLpsvVMKLIvrkfglidSQLEKEIVRSFIEKLNIKTPSPYQIVE----NLSGGNQQKVVLAKWLAIKPK 433
Cdd:cd03295 87 FPHMTVEENIAL---VPKLL--------KWPKEKIRERADELLALVGLDPAEFADryphELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 434 VLLLDEPTRGID----VNAKSEIYKLISEMavsGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03295 156 LLLMDEPFGALDpitrDQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGE 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
286-490 |
6.58e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.92 E-value: 6.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 286 VSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSPRDA--VKNGIGLVPEDRKtagLILQMS 362
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERP--SAGKIWFSGHDITRLKNREVpfLRRQIGMIFQDHH---LLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNITLPSVV-----------MKLIVRKFGLIDSqlekeiVRSFieklniktpsPYQivenLSGGNQQKVVLAKWLAIK 431
Cdd:PRK10908 96 VYDNVAIPLIIagasgddirrrVSAALDKVGLLDK------AKNF----------PIQ----LSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 432 PKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
284-490 |
7.43e-17 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 80.04 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 284 DDVSFYVRKGEVLGIYGLVGAGRTEL------LEAIfgahpgrTEGKVFIGGKEIkIHSPRDavkngiglVPEDRKTAGL 357
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLlrcinlLEEP-------DSGTITVDGEDL-TDSKKD--------INKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQ-------MSVLHNITLPSVVmkliVRKfglIDSQLEKEIVRSFIEKLNI-----KTPSpyqiveNLSGGNQQKVVLA 425
Cdd:COG1126 82 VFQqfnlfphLTVLENVTLAPIK----VKK---MSKAEAEERAMELLERVGLadkadAYPA------QLSGGQQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 426 KWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-485 |
7.75e-17 |
|
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: 83.30 E-value: 7.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 37 KGEVCALVGENGAGKSTLMKILAGVY-P---DYEGQifLEGKEV--RFRNpREAQE------NG---IALIPQELDLVPN 101
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkPnlgDYDEE--PSWDEVlkRFRG-TELQDyfkklaNGeikVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 102 LSSAE-NIFLSRepVNEFGVIEyqkmfEQASKLfsklgvNIDP--KTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTS 178
Cdd:COG1245 175 VFKGTvRELLEK--VDERGKLD-----ELAEKL------GLENilDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 179 AIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRdGRKVGEGPIEefdHDKLVRlmVGrsIDQF---FI 255
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILY-GEPGVYGVVS---KPKSVR--VG--INQYldgYL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 256 KE-------------RATITDEIFRVEGIKlW-----SLDRKKLLVDdvSFYVRKGEVLGIYGLVGAGRTELLEAIFGA- 316
Cdd:COG1245 314 PEenvrirdepiefeVHAPRREKEEETLVE-YpdltkSYGGFSLEVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVl 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 317 HPgrTEGKVFiggKEIKIhsprdAVKngiglvPEdrktaglilQMSVLHNITLPSVVMKLIVRKFGliDSQLEKEIVRSF 396
Cdd:COG1245 391 KP--DEGEVD---EDLKI-----SYK------PQ---------YISPDYDGTVEEFLRSANTDDFG--SSYYKTEIIKPL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 397 -IEKLniktpspY-QIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSElp 474
Cdd:COG1245 444 gLEKL-------LdKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH-- 514
|
490
....*....|....
gi 490181991 475 EILAM---SDRILV 485
Cdd:COG1245 515 DIYLIdyiSDRLMV 528
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-225 |
7.90e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.13 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfRNPreAQENGIAL 91
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV--EGP--GAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 ipQELDLVPNLSSAENIflsrepvnEFGV----IEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLD 167
Cdd:PRK11248 77 --QNEGLLPWRNVQDNV--------AFGLqlagVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 168 AKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDG 225
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
283-490 |
9.84e-17 |
|
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: 78.99 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKiHSPRDAVKNGIGLVPEDrktaglilqms 362
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA-EEGKIEIDGIDIS-TIPLEDLRSSLTIIPQD----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 vlhnitlPSVVMKLIVRKFGLIDSQLEKEIvrsfIEKLNIKTPSpyqivENLSGGNQQKVVLAKWLAIKPKVLLLDEPTR 442
Cdd:cd03369 91 -------PTLFSGTIRSNLDPFDEYSDEEI----YGALRVSEGG-----LNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490181991 443 GIDVNAKSEIYKLISEmAVSGMGVVMVSSELPEIlAMSDRILVMSEGR 490
Cdd:cd03369 155 SIDYATDALIQKTIRE-EFTNSTILTIAHRLRTI-IDYDKILVMDAGE 200
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
286-494 |
1.06e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.54 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 286 VSFYVRKGEVLGIYGLVGAGRTELLEAIFGAhPGRTEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDRKtagLILQMSVLH 365
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 366 NITLPSVV------MKLIVRKFGLIDSQLEKEIVRSfieklniktpspyqivENLSGGNQQKVVLAKWLAIKPKVLLLDE 439
Cdd:PRK11614 100 NLAMGGFFaerdqfQERIKWVYELFPRLHERRIQRA----------------GTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 440 PTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
283-490 |
1.18e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.26 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAiFGAHPGRTEGKVFIGGKEIKIHSPRDAVKngiglvpEDRKTAGLILQMS 362
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQH-FNALLKPSSGTITIAGYHITPETGNKNLK-------KLRKKVSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 ---VLHNITLPSVvmKLIVRKFGLIDsQLEKEIVRSFIEKLNIKT----PSPYQivenLSGGNQQKVVLAKWLAIKPKVL 435
Cdd:PRK13641 95 eaqLFENTVLKDV--EFGPKNFGFSE-DEAKEKALKWLKKVGLSEdlisKSPFE----LSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 436 LLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
30-231 |
1.40e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.84 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 30 NVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPReAQENGIALIPQElDLVPNLSSAENIF 109
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-VLRQGVAMVQQD-PVVLADTFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 110 LSREPVNE--FGVIEYQKMFEQASK----LFSKLGvnidpkTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIgKR 183
Cdd:PRK10790 437 LGRDISEEqvWQALETVQLAELARSlpdgLYTPLG------EQGNNLSVGQKQLLALARVLVQTPQILILDEATANI-DS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490181991 184 ETEQlfNIIRSLK--NEGKSVIYISHRLEEIFEiADRVVVMRDGRKVGEG 231
Cdd:PRK10790 510 GTEQ--AIQQALAavREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
284-490 |
1.60e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.98 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 284 DDVSFYVRKGEVLGIYGLVGAGRTELLEAIfGAHPGRTEGKVFIGGkeIKIHSPRDAVKngiglvpEDRKTAGLILQ--- 360
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSGDLIVDG--LKVNDPKVDER-------LIRQEAGMVFQqfy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 ----MSVLHNitlpsvVMKLIVRKFGLIDSQLEKeIVRSFIEKLNIKTPSPYQIVEnLSGGNQQKVVLAKWLAIKPKVLL 436
Cdd:PRK09493 88 lfphLTALEN------VMFGPLRVRGASKEEAEK-QARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 437 LDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
31-226 |
1.80e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.67 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 31 VTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQE---NGIALIPQELDLVPNLSSAEN 107
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 108 IFLsrePVNEFGVIEYQKMfEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQ 187
Cdd:PRK10584 109 VEL---PALLRGESSRQSR-NGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490181991 188 LFNIIRSLKNE-GKSVIYISHRlEEIFEIADRVVVMRDGR 226
Cdd:PRK10584 185 IADLLFSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
283-512 |
1.97e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGKeikihsPRDAVKNGIglvPEDRKTAGLILQm 361
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGIlKP--SSGRILFDGK------PIDYSRKGL---MKLRESVGMVFQ- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNITLPSVVMKLivrKFGLIDSQLEKEIVRSFIEKLNIKT---PSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLD 438
Cdd:PRK13636 90 DPDNQLFSASVYQDV---SFGAVNLKLPEDEVRKRVDNALKRTgieHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 439 EPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGRKTAE-FLREEVTEEDLLKAA---IPR 512
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQgNPKEVFAEKEMLRKVnlrLPR 245
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-247 |
2.13e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.26 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIALI 92
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFLSREPvnefgvieYQKMF--------EQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKAL 164
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRYP--------HQPLFtrwrkedeEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 165 SLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVR 243
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIE 238
|
....
gi 490181991 244 LMVG 247
Cdd:PRK10253 239 RIYG 242
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-226 |
3.02e-16 |
|
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: 75.56 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLegkevrfrnpreAQENGIALI 92
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------------GSTVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQeldlvpnLSSAEniflsrepvnefgvieyqkmfeqasklfsklgvnidpKTKvedlstsqqqmVAIAKALSLDAKIII 172
Cdd:cd03221 69 EQ-------LSGGE-------------------------------------KMR-----------LALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 173 MDEPTS-----AIgkretEQLfniIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:cd03221 94 LDEPTNhldleSI-----EAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
277-508 |
3.14e-16 |
|
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: 81.34 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKiHSPRDAVKNGIGLVPEDrktaG 356
Cdd:COG4988 348 GGRPAL-DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-YSGSILINGVDLS-DLDPASWRRQIAWVPQN----P 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSVLHNITL--PSVVmklivrkfgliDSQLEKEI----VRSFIEKLN--IKTPspyqIVE---NLSGGNQQKVVLA 425
Cdd:COG4988 421 YLFAGTIRENLRLgrPDAS-----------DEELEAALeaagLDEFVAALPdgLDTP----LGEggrGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 426 KWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELpEILAMSDRILVMSEGRktaefLREEVTEEDL 505
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRL-ALLAQADRILVLDDGR-----IVEQGTHEEL 558
|
...
gi 490181991 506 LKA 508
Cdd:COG4988 559 LAK 561
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-238 |
3.22e-16 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 77.45 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQENGIALIPQEldlvPNLSSAe 106
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRSSLTIIPQD----PTLFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 107 NIFLSREPVNEFGVIEyqkmfeqaskLFSKLGVnidpKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETE 186
Cdd:cd03369 97 TIRSNLDPFDEYSDEE----------IYGALRV----SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490181991 187 QLFNIIRSLKNeGKSVIYISHRLEEIFEIaDRVVVMRDGRkvgegpIEEFDH 238
Cdd:cd03369 163 LIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGE------VKEYDH 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
262-516 |
3.27e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.90 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 262 TDEIFRVEGIKLWSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDaV 341
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL-PEAGTITVGGMVLSEETVWD-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 342 KNGIGLVPE--DRKTAGLILQMSV---LHNITLPSVVMkliVRKfglIDSQLEKEIVRSFIEKlnikTPSpyqiveNLSG 416
Cdd:PRK13635 80 RRQVGMVFQnpDNQFVGATVQDDVafgLENIGVPREEM---VER---VDQALRQVGMEDFLNR----EPH------RLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 417 GNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEIlAMSDRILVMSEGRKTAEF 495
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEG 222
|
250 260
....*....|....*....|....*
gi 490181991 496 LREEVTE--EDLLKAA--IPRSVKV 516
Cdd:PRK13635 223 TPEEIFKsgHMLQEIGldVPFSVKL 247
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
283-490 |
3.85e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 80.26 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIkihsprdavkngiGLVPEDRKTAGLILQ- 360
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQP--TAGQIMLDGVDL-------------SHVPPYQRPINMMFQs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 ------MSVLHNITlpsvvmklivrkFGLIDSQLEKEIVRSFIEKL-------NIKTPSPYQivenLSGGNQQKVVLAKW 427
Cdd:PRK11607 100 yalfphMTVEQNIA------------FGLKQDKLPKAEIASRVNEMlglvhmqEFAKRKPHQ----LSGGQRQRVALARS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 428 LAIKPKVLLLDEPTRGIDVNAKSEI-YKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-247 |
4.47e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 24 GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfrnpREAQENGIALIPQ--ELDLVPN 101
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYVPQseEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 102 LSSAENIFLSRepVNEFGVIEYQKMFEQA--SKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSA 179
Cdd:PRK15056 95 VLVEDVVMMGR--YGHMGWLRRAKKRDRQivTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 180 IGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADrVVVMRDGRKVGEGPIE-EFDHDKLVRLMVG 247
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTEtTFTAENLELAFSG 240
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-235 |
4.73e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.46 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDyegQIFLEGKEVRFRN------- 80
Cdd:PRK15093 3 LLDIRNLTIEFKTsdgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKD---NWRVTADRMRFDDidllrls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 81 PREAQE---NGIALIPQEldlvPN--LSSAENIflSREPVNEFGVIEYQKMFEQ--------ASKLFSKLGVNiDPKTKV 147
Cdd:PRK15093 80 PRERRKlvgHNVSMIFQE----PQscLDPSERV--GRQLMQNIPGWTYKGRWWQrfgwrkrrAIELLHRVGIK-DHKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 148 E----DLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVM 222
Cdd:PRK15093 153 RsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVL 232
|
250
....*....|...
gi 490181991 223 RDGRKVGEGPIEE 235
Cdd:PRK15093 233 YCGQTVETAPSKE 245
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-485 |
4.89e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.01 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 37 KGEVCALVGENGAGKSTLMKILAG-VYP---DYEGQifLEGKEV--RFRNP------REAQENGI--ALIPQELDLVPNL 102
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGeLIPnlgDYEEE--PSWDEVlkRFRGTelqnyfKKLYNGEIkvVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 103 SSAENIFLSREpVNEFGVIEyqkmfEQASKLfsklgvNIDP--KTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAI 180
Cdd:PRK13409 176 FKGKVRELLKK-VDERGKLD-----EVVERL------GLENilDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 181 GKRETEQLFNIIRSLkNEGKSVIYISHRLEEIFEIADRVVVMrdgrkVGE-GPIEEFDHDKLVRlmVGrsIDQF---FIK 256
Cdd:PRK13409 244 DIRQRLNVARLIREL-AEGKYVLVVEHDLAVLDYLADNVHIA-----YGEpGAYGVVSKPKGVR--VG--INEYlkgYLP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 257 E---RatitdeiFRVEGIKL----------------WSLDRKKLlvDDVSF-----YVRKGEVLGIYGLVGAGRTELLEA 312
Cdd:PRK13409 314 EenmR-------IRPEPIEFeerpprdeseretlveYPDLTKKL--GDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 313 IFGA-HPgrTEGKVFiggKEIKIhsprdAVKngiglvPEDRKTAgliLQMSVlhnitlpSVVMKLIVRKFGliDSQLEKE 391
Cdd:PRK13409 385 LAGVlKP--DEGEVD---PELKI-----SYK------PQYIKPD---YDGTV-------EDLLRSITDDLG--SSYYKSE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 392 IVRSF-IEKLNIKTpspyqiVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMA-VSGMGVVMV 469
Cdd:PRK13409 437 IIKPLqLERLLDKN------VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVV 510
|
490
....*....|....*.
gi 490181991 470 SSELPEILAMSDRILV 485
Cdd:PRK13409 511 DHDIYMIDYISDRLMV 526
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-235 |
6.48e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 26 IAVNN----VTLQIYKGEVCALVGENGAGKSTLMKILAGVYPdYEGQIFLEGKEV---------RFRnpreaqengiALI 92
Cdd:COG4138 6 VAVAGrlgpISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLsdwsaaelaRHR----------AYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFLSREPVNEFGVIEyQKMFEQASKLfsklgvNIDPK--TKVEDLSTSQQQMVAIAKAL------ 164
Cdd:COG4138 75 SQQQSPPFAMPVFQYLALHQPAGASSEAVE-QLLAQLAEAL------GLEDKlsRPLTQLSGGEWQRVRLAAVLlqvwpt 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 165 -SLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:COG4138 148 iNPEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
263-517 |
6.53e-16 |
|
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: 77.43 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 263 DEIFRVEGIKlWSLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTEGKVFIGGKEIKIHSPRDaVK 342
Cdd:COG1119 1 DPLLELRNVT-VRRGGKTIL-DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRGGEDVWE-LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 343 NGIGLV-PEdrktagliLQMSVLHNITLPSVVMKlivrkfGLIDS--------QLEKEIVRSFIEKLNI--KTPSPYQiv 411
Cdd:COG1119 78 KRIGLVsPA--------LQLRFPRDETVLDVVLS------GFFDSiglyreptDEQRERARELLELLGLahLADRPFG-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 412 eNLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSG-MGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG1119 142 -TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
250 260
....*....|....*....|....*..
gi 490181991 491 KTAEFLREEVTEEDLLKAAIPRSVKVE 517
Cdd:COG1119 221 VVAAGPKEEVLTSENLSEAFGLPVEVE 247
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-226 |
6.75e-16 |
|
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: 80.23 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGV-----IAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfrnpreaqen 87
Cdd:COG4615 328 LELRGVTYRYPGEdgdegFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 gialiPQELDLVPNLSSAenIF----LSREPVNEFGVIEYqkmfEQASKLFSKLgvNIDPKTKVED-------LSTSQQQ 156
Cdd:COG4615 398 -----ADNREAYRQLFSA--VFsdfhLFDRLLGLDGEADP----ARARELLERL--ELDHKVSVEDgrfsttdLSQGQRK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 157 MVAIAKALSLDAKIIIMDE------PTSaigKRE--TEqlfnIIRSLKNEGKSVIYISH--RLeeiFEIADRVVVMRDGR 226
Cdd:COG4615 465 RLALLVALLEDRPILVFDEwaadqdPEF---RRVfyTE----LLPELKARGKTVIAISHddRY---FDLADRVLKMDYGK 534
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
286-517 |
6.90e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.70 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 286 VSFYVRKGEVLGIYGLVGAGRTELLEAI-FGAHPgrTEGKVFIGGKEIKIHSPRD-----AVKNGIGLVpedRKTAGLIL 359
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCInFLEKP--SEGSIVVNGQTINLVRDKDgqlkvADKNQLRLL---RTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 360 Q-------MSVLHNitlpsvVMKLIVRKFGLIDSQLEKEIVRsFIEKLNIKTPSPYQIVENLSGGNQQKVVLAKWLAIKP 432
Cdd:PRK10619 99 QhfnlwshMTVLEN------VMEAPIQVLGLSKQEARERAVK-YLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 433 KVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRktaefLREEVTEEDLLkaAIPR 512
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK-----IEEEGAPEQLF--GNPQ 244
|
....*
gi 490181991 513 SVKVE 517
Cdd:PRK10619 245 SPRLQ 249
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-236 |
7.47e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.38 E-value: 7.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 2 MLNTEKEREVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAG---VYPD--YEGQIFLEGK-- 74
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGarVEGEILLDGEdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 75 --------EVRFRnpreaqengIALIPQEldlvPN---LSSAENIflsrepvnEFGVieyqKMFEQASKlfSKLgvnidp 143
Cdd:COG1117 81 ydpdvdvvELRRR---------VGMVFQK----PNpfpKSIYDNV--------AYGL----RLHGIKSK--SEL------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 144 KTKVED---------------------LSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEgKSV 202
Cdd:COG1117 128 DEIVEEslrkaalwdevkdrlkksalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTI 206
|
250 260 270
....*....|....*....|....*....|....
gi 490181991 203 IYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEF 236
Cdd:COG1117 207 VIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-447 |
8.85e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 79.98 E-value: 8.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 17 NITKTFPGVIAV-NNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLegkevrfrnpreAQENGIALIPQE 95
Cdd:TIGR03719 9 RVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP------------QPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 96 LDLVPNLSSAENIFLS----REPVNEFGVI---------EYQKMFEQASKLFSKL----GVNIDPK-------------- 144
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGvaeiKDALDRFNEIsakyaepdaDFDKLAAEQAELQEIIdaadAWDLDSQleiamdalrcppwd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 145 TKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIgkrETEQLFNIIRSLKNEGKSVIYISH----------------- 207
Cdd:TIGR03719 157 ADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHL---DAESVAWLERHLQEYPGTVVAVTHdryfldnvagwileldr 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 208 -------------------RL--EEIFEIADRVVVMRDGRKVGEGP----------IEEFdhDKLVRLMVGRSID--QFF 254
Cdd:TIGR03719 234 grgipwegnysswleqkqkRLeqEEKEESARQKTLKRELEWVRQSPkgrqakskarLARY--EELLSQEFQKRNEtaEIY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 255 IKERATITDEIFRVEGI-KLWSldrKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGgkei 332
Cdd:TIGR03719 312 IPPGPRLGDKVIEAENLtKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGqEQP--DSGTIEIG---- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 333 kihsprDAVKngIGLVPEDRKtaGLILQMSVLHNITLPSVVMKLIVRKfglIDSqlekeivRSFIEKLNIKTPSPYQIVE 412
Cdd:TIGR03719 383 ------ETVK--LAYVDQSRD--ALDPNKTVWEEISGGLDIIKLGKRE---IPS-------RAYVGRFNFKGSDQQKKVG 442
|
490 500 510
....*....|....*....|....*....|....*
gi 490181991 413 NLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVN 447
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
28-208 |
9.00e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.76 E-value: 9.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfRNPREAQENGIALIPQELDLVPNLSSAEN 107
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 108 IFLS-REPVNEFGVIEYQKMFeqasklfsKLGVNIDPKTKVedLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETE 186
Cdd:PRK13540 95 CLYDiHFSPGAVGITELCRLF--------SLEHLIDYPCGL--LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 490181991 187 QLFNIIRSLKNEGKSVIYISHR 208
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
13-207 |
9.17e-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: 75.99 E-value: 9.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQenGIALI 92
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR--GLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENI-----FLSREPVnefgvieyqkmfEQAsklFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLD 167
Cdd:cd03231 79 GHAPGIKTTLSVLENLrfwhaDHSDEQV------------EEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490181991 168 AKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISH 207
Cdd:cd03231 144 RPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
286-512 |
9.71e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.43 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 286 VSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIhsprdavkNGIGLVpEDRKTAGLILQMSVlH 365
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILK-PTSGEVLIKGEPIKY--------DKKSLL-EVRKTVGIVFQNPD-D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 366 NITLPSVVMKLivrKFGLIDSQLEKEIVRSFI-EKLNIKTPSPYQ--IVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTR 442
Cdd:PRK13639 90 QLFAPTVEEDV---AFGPLNLGLSKEEVEKRVkEALKAVGMEGFEnkPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 443 GIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEV-TEEDLLKAA---IPR 512
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVfSDIETIRKAnlrLPR 240
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
277-506 |
1.08e-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: 76.50 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFgahpgR----TEGKVFIGG---KEIKIHSPRDAvkngIGLVP 349
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-----RfydvSSGSILIDGqdiREVTLDSLRRA----IGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 350 EDrktaglilqmSVLHNITlpsvVMKLIvrKFGLIDSQlEKEIVRS--------FIEKLniktPSPYQIV--EN---LSG 416
Cdd:cd03253 82 QD----------TVLFNDT----IGYNI--RYGRPDAT-DEEVIEAakaaqihdKIMRF----PDGYDTIvgERglkLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 417 GNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPEIlAMSDRILVMSEGRktaefL 496
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTI-VNADKIIVLKDGR-----I 213
|
250
....*....|
gi 490181991 497 REEVTEEDLL 506
Cdd:cd03253 214 VERGTHEELL 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-235 |
1.09e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.38 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 30 NVTLQIYKGEVCALVGENGAGKSTLMKILAG-VYPDyEGQIFLEGKeVRFRnpreaQENGIALIP---------QELDLV 99
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGlTRPQ-KGRIVLNGR-VLFD-----AEKGICLPPekrrigyvfQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 100 PNLSSAENIflsrepvnEFGVIEyqKMFEQASKLFSKLGvnIDP--KTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPT 177
Cdd:PRK11144 89 PHYKVRGNL--------RYGMAK--SMVAQFDKIVALLG--IEPllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 178 SAIG---KREteqLFNIIRSLKNEGK-SVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK11144 157 ASLDlprKRE---LLPYLERLAREINiPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-221 |
1.13e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 5 TEKEREVLLEARNITKTFpgviavNNVTL-----QIYKGEVCALVGENGAGKSTLMKILAGVY-PDyEGQIFLEGKevrf 78
Cdd:PRK13409 333 DESERETLVEYPDLTKKL------GDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLkPD-EGEVDPELK---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 79 rnpreaqengIALIPQELDLVPNLSSAEniFLSREPVNeFGVIEYQkmfeqaSKLFSKLGVNIDPKTKVEDLSTSQQQMV 158
Cdd:PRK13409 402 ----------ISYKPQYIKPDYDGTVED--LLRSITDD-LGSSYYK------SEIIKPLQLERLLDKNVKDLSGGELQRV 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 159 AIAKALSLDAKIIIMDEPTSAIgkrETEQLFN---IIRSL-KNEGKSVIYISHRLEEIFEIADRVVV 221
Cdd:PRK13409 463 AIAACLSRDADLYLLDEPSAHL---DVEQRLAvakAIRRIaEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-207 |
1.18e-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: 75.47 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQEngIALI 92
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN--ILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENI-FLsrepvNEFGVIEyQKMFEQAsklFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKII 171
Cdd:TIGR01189 79 GHLPGLKPELSALENLhFW-----AAIHGGA-QRTIEDA---LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 490181991 172 IMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISH 207
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
281-490 |
1.81e-15 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 75.99 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 281 LLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHSPrDAVKNGIGLVPEDrktaGLILQ 360
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP-ENGRVLVDGHDLALADP-AWLRRQVGVVLQE----NVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 MSVLHNITL--PSVVMKLIVRKFGLIDSQlekeivrSFIEKLniktPSPY-QIV-EN---LSGGNQQKVVLAKWLAIKPK 433
Cdd:cd03252 90 RSIRDNIALadPGMSMERVIEAAKLAGAH-------DFISEL----PEGYdTIVgEQgagLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 434 VLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPEILAmSDRILVMSEGR 490
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGR 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
283-509 |
1.96e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 76.77 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGKEIKIHSPRdavkngiglvpEDRKTAGLILQM 361
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIlKP--TSGSVLIRGEPITKENIR-----------EVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVlHNITLPSVVMKLivrKFGLIDSQLEKEIVRSFIEKL-------NIKTPSPYqiveNLSGGNQQKVVLAKWLAIKPKV 434
Cdd:PRK13652 87 PD-DQIFSPTVEQDI---AFGPINLGLDEETVAHRVSSAlhmlgleELRDRVPH----HLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 435 LLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEV-TEEDLLKAA 509
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLARV 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
279-519 |
2.42e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.18 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRT---ELLEAIFGAhpgrTEGKVFIGGKEIKIHSPRDAVKN-GIGLVPEDRKT 354
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKStisKILTGLLKP----QSGEIKIDGITISKENLKEIRKKiGIIFQNPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 355 AGLILQMSV---LHNITLPSVVMKLIVRKFGL---IDSQLEKEivrsfieklniktpsPyqivENLSGGNQQKVVLAKWL 428
Cdd:PRK13632 97 IGATVEDDIafgLENKKVPPKKMKDIIDDLAKkvgMEDYLDKE---------------P----QNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 429 AIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVM-VSSELPEILaMSDRILVMSEGR-----KTAEFLREevtE 502
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAI-LADKVIVFSEGKliaqgKPKEILNN---K 233
|
250
....*....|....*....
gi 490181991 503 EDLLKAAI--PRSVKVETT 519
Cdd:PRK13632 234 EILEKAKIdsPFIYKLSKK 252
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-221 |
2.96e-15 |
|
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: 78.67 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 6 EKEREVLLEARNITKTFPGViavnnvTL-----QIYKGEVCALVGENGAGKSTLMKILAGVY-PDyEGQIFLEGKevrfr 79
Cdd:COG1245 335 EKEEETLVEYPDLTKSYGGF------SLeveggEIREGEVLGIVGPNGIGKTTFAKILAGVLkPD-EGEVDEDLK----- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 80 npreaqengIALIPQEldLVPNLSSAENIFLSREPVNEFGVIEYQkmfeqaSKLFSKLGVNIDPKTKVEDLSTSQQQMVA 159
Cdd:COG1245 403 ---------ISYKPQY--ISPDYDGTVEEFLRSANTDDFGSSYYK------TEIIKPLGLEKLLDKNVKDLSGGELQRVA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 160 IAKALSLDAKIIIMDEPTSAIgkrETEQLFNIIRSLK----NEGKSVIYISHRLEEIFEIADRVVV 221
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHL---DVEQRLAVAKAIRrfaeNRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
275-488 |
3.16e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.54 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 275 SLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVfiggkeikIHSPrdavKNGIGLVPEDrk 353
Cdd:PRK09544 13 SFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGlVAP--DEGVI--------KRNG----KLRIGYVPQK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 354 taglilqmsvLH-NITLPSVVMKLIVRKFGLIDSQLEKEIVRSFIEKLnIKTPspyqiVENLSGGNQQKVVLAKWLAIKP 432
Cdd:PRK09544 76 ----------LYlDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHL-IDAP-----MQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 433 KVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSE 488
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
285-513 |
3.34e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.31 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGKEIKIHSPRDAVKngiglvpEDRKTAGLILQMSv 363
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQP--TEGKVTVGDIVVSSTSKQKEIK-------PVRKKVGVVFQFP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 364 lHNITLPSVVMKLIV---RKFGLIDSQLEK------EIV---RSFIEKlniktpSPYQivenLSGGNQQKVVLAKWLAIK 431
Cdd:PRK13643 94 -ESQLFEETVLKDVAfgpQNFGIPKEKAEKiaaeklEMVglaDEFWEK------SPFE----LSGGQMRRVAIAGILAME 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 432 PKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEE-DLLKA-- 508
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEvDFLKAhe 242
|
....*.
gi 490181991 509 -AIPRS 513
Cdd:PRK13643 243 lGVPKA 248
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
275-489 |
4.19e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.66 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 275 SLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHpGRTEGKVFIGGKEIKIHSPRDavkNGIGLVPEDRkt 354
Cdd:PRK10851 11 SFGRTQVL-NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLE-HQTSGHIRFHGTDVSRLHARD---RKVGFVFQHY-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 355 aGLILQMSVLHNITlpsvvmklivrkFGL-------------IDSQLEK--EIVRsfIEKLNIKTPSpyqiveNLSGGNQ 419
Cdd:PRK10851 84 -ALFRHMTVFDNIA------------FGLtvlprrerpnaaaIKAKVTQllEMVQ--LAHLADRYPA------QLSGGQK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 420 QKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSE----IYKLISEMAVSGmgvVMVSSELPEILAMSDRILVMSEG 489
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKElrrwLRQLHEELKFTS---VFVTHDQEEAMEVADRVVVMSQG 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
257-489 |
4.25e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.08 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 257 ERATITDEIFRVEGIKLWSLDrkKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAI-----FGAHPGRTEGKVFIGGKE 331
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYIND--KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieIYDSKIKVDGKVLYFGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 332 I-KIhsprDAVKNgiglvpedRKTAGLILQ-------MSVLHNITLPsvvmkliVRKFGLIDSQLEKEIVRSFIEKLNI- 402
Cdd:PRK14246 80 IfQI----DAIKL--------RKEVGMVFQqpnpfphLSIYDNIAYP-------LKSHGIKEKREIKKIVEECLRKVGLw 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 403 -----KTPSPyqiVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPEIL 477
Cdd:PRK14246 141 kevydRLNSP---ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQQVA 216
|
250
....*....|..
gi 490181991 478 AMSDRILVMSEG 489
Cdd:PRK14246 217 RVADYVAFLYNG 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
285-500 |
4.46e-15 |
|
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: 76.69 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKihsprDAVKnGIGLVPEDRKT------AGL 357
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGlTRP--DEGEIVLNGRTLF-----DSRK-GIFLPPEKRRIgyvfqeARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQMSVLHNItlpsvvmklivrKFGLIDSQLEKEIVR--SFIEKLNIKtPSPYQIVENLSGGNQQKVVLAKWLAIKPKVL 435
Cdd:TIGR02142 87 FPHLSVRGNL------------RYGMKRARPSERRISfeRVIELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 436 LLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEV 500
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-243 |
4.56e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.59 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNpreaQENGIALIPQELDLVPNLSSAE 106
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKT----KDKYIRPVRKRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 107 NIFLSREPVNEFGVIEYQKMFEQ----ASKLFSKLGVNIDPKTKVE-DLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIG 181
Cdd:PRK13646 98 LFEDTVEREIIFGPKNFKMNLDEvknyAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 182 KRETEQLFNIIRSLK-NEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG-PIEEFDHDKLVR 243
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTsPKELFKDKKKLA 241
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-236 |
5.80e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.04 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNIT-----KTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGV----YPD------YEGQIFLEGK 74
Cdd:PRK13631 19 DIILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskYGTiqvgdiYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 75 EVRFRNPREAQE-----NGIALIPQ--ELDLVPNLSSAENIFlsrEPVNeFGVIEYQKMfEQASKLFSKLGVNiDPKTKV 147
Cdd:PRK13631 99 LITNPYSKKIKNfkelrRRVSMVFQfpEYQLFKDTIEKDIMF---GPVA-LGVKKSEAK-KLAKFYLNKMGLD-DSYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 148 E--DLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDG 225
Cdd:PRK13631 173 SpfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
250
....*....|..
gi 490181991 226 RKVGEG-PIEEF 236
Cdd:PRK13631 253 KILKTGtPYEIF 264
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
278-490 |
6.39e-15 |
|
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: 73.77 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 278 RKKLLVDDVSFYVRKGeVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHspRDAVKNGIGLVPEDrktAGL 357
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP-SSGTIRIDGQDVLKQ--PQKLRRRIGYLPQE---FGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQMSVLHnitlpsvVMKLIVRKFGLIDSQLEKEIVRSfIEKLNIkTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLL 437
Cdd:cd03264 84 YPNFTVRE-------FLDYIAWLKGIPSKEVKARVDEV-LELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 438 DEPTRGIDVNAKSEIYKLISEMAVSgmGVVMVSSELPE-ILAMSDRILVMSEGR 490
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEdVESLCNQVAVLNKGK 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-209 |
6.57e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.40 E-value: 6.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPG-VIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIAL 91
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQEldlvPNLSSA---ENIFLSREPVNEfgvieyqkmfEQASKLFSKLGVNIDPKTKVEDLSTS-----------QQQM 157
Cdd:TIGR02868 414 CAQD----AHLFDTtvrENLRLARPDATD----------EELWAALERVGLADWLRALPDGLDTVlgeggarlsggERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490181991 158 VAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSlKNEGKSVIYISHRL 209
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-231 |
7.82e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.12 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTF----PGVI-AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIflegkEVRFRNpREAQEN 87
Cdd:PRK13651 3 IKVKNIVKIFnkklPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI-----EWIFKD-EKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 88 GIALIPQELDLVPNLSSAENIFLSREPVNEFGVI----EYQkMFEQ-----------------------ASKLFSKLGVN 140
Cdd:PRK13651 77 TKEKEKVLEKLVIQKTRFKKIKKIKEIRRRVGVVfqfaEYQ-LFEQtiekdiifgpvsmgvskeeakkrAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 141 ID--PKTKVEdLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADR 218
Cdd:PRK13651 156 ESylQRSPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKR 234
|
250
....*....|...
gi 490181991 219 VVVMRDGRKVGEG 231
Cdd:PRK13651 235 TIFFKDGKIIKDG 247
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
280-500 |
9.12e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.75 E-value: 9.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPG----RTEGKVFIGGKEIkiHSPRDavkngiglVPEDRKTA 355
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyRYSGDVLLGGRSI--FNYRD--------VLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 356 GLILQ------MSVLHNITLPSVVMKLIVRK--FGLIDSQL-EKEIVRSFIEKLnikTPSPYQivenLSGGNQQKVVLAK 426
Cdd:PRK14271 104 GMLFQrpnpfpMSIMDNVLAGVRAHKLVPRKefRGVAQARLtEVGLWDAVKDRL---SDSPFR----LSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 427 WLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEV 500
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-235 |
9.31e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.53 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 1 MMLNTEKEREVLLEARNITKTFPG----VIAVNNVTLQIYKGEVCALVGENGAGKS----TLMKILA--GVYpdyEGQIF 70
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFSTpdgdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRI---GGSAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 71 LEGKEVRfrNPREAQENG-----IALIPQE------------------LDLVPNLSSAENIflsREPVNefgVIEYQKMF 127
Cdd:PRK09473 78 FNGREIL--NLPEKELNKlraeqISMIFQDpmtslnpymrvgeqlmevLMLHKGMSKAEAF---EESVR---MLDAVKMP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 128 EQASKLfsklgvNIDPktkvEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYIS 206
Cdd:PRK09473 150 EARKRM------KMYP----HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMIT 219
|
250 260
....*....|....*....|....*....
gi 490181991 207 HRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK09473 220 HDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-226 |
1.05e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIfLEGkevrfRNPREAQENGIALI 92
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG-----TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFL---------SREPVNEFGVIEYQKMFEQAsklfsklgvnidpktkvedLSTSQQQMVAIAKA 163
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLglkgqwrdaALQALAAVGLADRANEWPAA-------------------LSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 164 LSLDAKIIIMDEPTSAIG---KRETEQLfniIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDaltRIEMQDL---IESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
257-490 |
1.11e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 75.75 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 257 ERATITDEIFRVEGIKLwSLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKih 335
Cdd:PRK09452 6 KQPSSLSPLVELRGISK-SFDGKEVI-SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETP--DSGRIMLDGQDIT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 336 sprdavkngiGLVPEDR------KTAGLILQMSVLHNITlpsvvmklivrkFGLidsQLEK----EIVRSFIEKL----- 400
Cdd:PRK09452 80 ----------HVPAENRhvntvfQSYALFPHMTVFENVA------------FGL---RMQKtpaaEITPRVMEALrmvql 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 401 -NIKTPSPYQivenLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDvnakseiYKLISEMAVS--------GMGVVMVSS 471
Cdd:PRK09452 135 eEFAQRKPHQ----LSGGQQQRVAIARAVVNKPKVLLLDESLSALD-------YKLRKQMQNElkalqrklGITFVFVTH 203
|
250
....*....|....*....
gi 490181991 472 ELPEILAMSDRILVMSEGR 490
Cdd:PRK09452 204 DQEEALTMSDRIVVMRDGR 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
13-226 |
1.23e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.55 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIAL 91
Cdd:PRK10522 323 LELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENiflsrEPVNEFGVIEYQKMFEQASKLFSKLGVNIDPKtkvedLSTSQQQMVAIAKALSLDAKII 171
Cdd:PRK10522 402 VFTDFHLFDQLLGPEG-----KPANPALVEKWLERLKMAHKLELEDGRISNLK-----LSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 172 IMDE------PTSaigKRETEQLfnIIRSLKNEGKSVIYISHRlEEIFEIADRVVVMRDGR 226
Cdd:PRK10522 472 LLDEwaadqdPHF---RREFYQV--LLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
279-509 |
1.26e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.65 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHSPRDavkngiglvpedrktagLI 358
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSP-DSGEVRLNGRPLADWSPAE-----------------LA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQMSVL---HNITLP----SVV-MKLIVRKFG------LIDSQLEKEIVRSFIEKlniktpsPYQiveNLSGGNQQKVVL 424
Cdd:PRK13548 76 RRRAVLpqhSSLSFPftveEVVaMGRAPHGLSraeddaLVAAALAQVDLAHLAGR-------DYP---QLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 425 AKWLA------IKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPeiLA--MSDRILVMSEGRKTAEF 495
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLN--LAarYADRIVLLHQGRLVADG 223
|
250
....*....|....
gi 490181991 496 LREEVTEEDLLKAA 509
Cdd:PRK13548 224 TPAEVLTPETLRRV 237
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
278-490 |
1.47e-14 |
|
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: 72.30 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 278 RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPG--RTEGKVFIGG---KEIKIHSPRDAVKNGiglvPEDr 352
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvSVEGDIHYNGipyKEFAEKYPGEIIYVS----EED- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 353 ktaglilqmsvLHNITLpsvvmklIVRKfgLIDsqlekeivrsFIEKLNiktpsPYQIVENLSGGNQQKVVLAKWLAIKP 432
Cdd:cd03233 93 -----------VHFPTL-------TVRE--TLD----------FALRCK-----GNEFVRGISGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 433 KVLLLDEPTRGIDVNAKSEIYKLISEMA-VSGMGVVM-VSSELPEILAMSDRILVMSEGR 490
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMAdVLKTTTFVsLYQASDEIYDLFDKVLVLYEGR 197
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
263-490 |
1.60e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.50 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 263 DEIFRVEGIKLwSLDRKK----LLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRtegKVFIGGKEIKIHSPR 338
Cdd:PRK13631 19 DIILRVKNLYC-VFDEKQenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK---YGTIQVGDIYIGDKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 339 DAVKNGIGLVPED-------RKTAGLILQMS--VLHNITLPSVVMklivrkFGLIDSQLEKEIVRS----FIEKLNIKTP 405
Cdd:PRK13631 95 NNHELITNPYSKKiknfkelRRRVSMVFQFPeyQLFKDTIEKDIM------FGPVALGVKKSEAKKlakfYLNKMGLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 406 ----SPYQivenLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSD 481
Cdd:PRK13631 169 ylerSPFG----LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVAD 244
|
....*....
gi 490181991 482 RILVMSEGR 490
Cdd:PRK13631 245 EVIVMDKGK 253
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
277-508 |
2.46e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 75.59 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAH-PgrTEGKVFIGGKEIKiHSPRDAVKNGIGLVPEDrkta 355
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdP--TSGRILIDGVDIR-DLTLESLRRQIGVVPQD---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 356 GLILQMSVLHNITlpsvvmklivrkFGLIDSQLEkEIVR--------SFIEKLniktPSPY--QIVE---NLSGGNQQKV 422
Cdd:COG1132 423 TFLFSGTIRENIR------------YGRPDATDE-EVEEaakaaqahEFIEAL----PDGYdtVVGErgvNLSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 423 VLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPEIlAMSDRILVMSEGRktaefLREEVTE 502
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTI-RNADRILVLDDGR-----IVEQGTH 558
|
....*.
gi 490181991 503 EDLLKA 508
Cdd:COG1132 559 EELLAR 564
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-228 |
2.48e-14 |
|
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: 71.51 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 29 NNVTLQIYKGEVCALVGENGAGKSTLMKILA-----GVypdYEGQIFLEGKEVRFRNPREaqengIALIPQELDLVPNLS 103
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGV---ITGEILINGRPLDKNFQRS-----TGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 104 saeniflsrepvnefgVIEyqkmfeqaSKLFSklgvnidpkTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKR 183
Cdd:cd03232 96 ----------------VRE--------ALRFS---------ALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490181991 184 ETEQLFNIIRSLKNEGKSVI-YISHRLEEIFEIADRVVVMRDGRKV 228
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLKRGGKT 188
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
277-490 |
3.02e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.23 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTeGKVFIGGKEIKIHSPRDaVKNGIGLVPE--DRKT 354
Cdd:PRK13650 17 DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES-GQIIIDGDLLTEENVWD-IRHKIGMVFQnpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 355 AGLILQMSV---LHNITLPSVVMKLIVrkfgliDSQLEkeivrsFIEKLNIKTPSPYQivenLSGGNQQKVVLAKWLAIK 431
Cdd:PRK13650 95 VGATVEDDVafgLENKGIPHEEMKERV------NEALE------LVGMQDFKEREPAR----LSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 432 PKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEIlAMSDRILVMSEGR 490
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-239 |
3.03e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.80 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGV---------IAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVR----- 77
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 78 ----FR--------------NPREAQEngiALIPQELDLVPNLSSAENIFLSREPVNEFGVIEyqkmfEQASKLfsklgv 139
Cdd:PRK10419 83 qrkaFRrdiqmvfqdsisavNPRKTVR---EIIREPLRHLLSLDKAERLARASEMLRAVDLDD-----SVLDKR------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 140 nidPktkvEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISH--RLEEIFeiA 216
Cdd:PRK10419 149 ---P----PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHdlRLVERF--C 219
|
250 260
....*....|....*....|....*.
gi 490181991 217 DRVVVMRDGRKVGEGPIEE---FDHD 239
Cdd:PRK10419 220 QRVMVMDNGQIVETQPVGDkltFSSP 245
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-236 |
3.20e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.20 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTF---PGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENg 88
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQELDlvpnlssAENIFLSREPVNEFGV----IEYQKMFEQASKLFskLGVN-IDPKTK-VEDLSTSQQQMVAIAK 162
Cdd:PRK13642 83 IGMVFQNPD-------NQFVGATVEDDVAFGMenqgIPREEMIKRVDEAL--LAVNmLDFKTRePARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 163 ALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGK-SVIYISHRLEEIFEiADRVVVMRDGRKVGEGPIEEF 236
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
285-493 |
3.52e-14 |
|
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: 73.98 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGK-----EIKIHSPRDavKNGIGLVPEDrktAGLI 358
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGlERP--DSGRIRLGGEvlqdsARGIFLPPH--RRRIGYVFQE---ARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQMSVLHNITLpsvVMKLIVRKFGLIDsqLEkEIVrsfiEKLNI-----KTPspyqivENLSGGNQQKVVLAKWLAIKPK 433
Cdd:COG4148 90 PHLSVRGNLLY---GRKRAPRAERRIS--FD-EVV----ELLGIghlldRRP------ATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 434 VLLLDEPTRGIDVNAKSEI--Y--KLISEMAVSgmgVVMVSSELPEILAMSDRILVMSEGRKTA 493
Cdd:COG4148 154 LLLMDEPLAALDLARKAEIlpYleRLRDELDIP---ILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
285-490 |
3.98e-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: 75.82 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYvrKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKihSPRDAVKNGIGLVPedrktaglilQMSVL 364
Cdd:TIGR01257 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLP-PTSGTVLVGGKDIE--TNLDAVRQSLGMCP----------QHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 365 -HNITLPSVVM---KLIVRKFGliDSQLEKEivrSFIEKLNIKTPSPYQiVENLSGGNQQKVVLAKWLAIKPKVLLLDEP 440
Cdd:TIGR01257 1015 fHHLTVAEHILfyaQLKGRSWE--EAQLEME---AMLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490181991 441 TRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
279-490 |
4.04e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.60 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHS--PRDavkngIGLVpedRKTA 355
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKP--TEGQIFIDGEDVTHRSiqQRD-----ICMV---FQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 356 GLILQMSVLHNItlpsvvmklivrKFGLIDSQLEKEIVRSFI-EKLNIKTPSPYQ--IVENLSGGNQQKVVLAKWLAIKP 432
Cdd:PRK11432 88 ALFPHMSLGENV------------GYGLKMLGVPKEERKQRVkEALELVDLAGFEdrYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 433 KVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
285-490 |
4.32e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.47 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAH-PgrTEGKVFIGGKEIKIHSPRDAVKNgiglvpeDRKTAGLILQMSv 363
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvP--TQGSVRVDDTLITSTSKNKDIKQ-------IRKKVGLVFQFP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 364 lHNITLPSVVMKLIV---RKFGLidSQLEKEivRSFIEKL-------NIKTPSPYQivenLSGGNQQKVVLAKWLAIKPK 433
Cdd:PRK13649 95 -ESQLFEETVLKDVAfgpQNFGV--SQEEAE--ALAREKLalvgiseSLFEKNPFE----LSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 434 VLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
280-488 |
5.13e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 70.97 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPG--RTEGKVFIGGKEIKihsprdavkngiGLVPEDRKTaGL 357
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafSASGEVLLNGRRLT------------ALPAEQRRI-GI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQ-------MSVLHNItlpsvvmklivrKFGL---IDSQLEKEIVRSFIEKLNI-----KTPSpyqiveNLSGGNQQKV 422
Cdd:COG4136 81 LFQddllfphLSVGENL------------AFALpptIGRAQRRARVEQALEEAGLagfadRDPA------TLSGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 423 VLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSdRILVMSE 488
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-217 |
5.15e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVyPDYEGQIFLEGKEVRFRNPREAQENGIALIPQELDLV---PNL-- 102
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRVEFFNQNIYERRVNLNRLRRQVSMVhpkPNLfp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 103 -SSAENIFLSREPVNEFGVIEYQKMFEQASK---LFSKLgvnidpKTKVE----DLSTSQQQMVAIAKALSLDAKIIIMD 174
Cdd:PRK14258 102 mSVYDNVAYGVKIVGWRPKLEIDDIVESALKdadLWDEI------KHKIHksalDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490181991 175 EPTSAIGKRETEQLFNIIRSLKNEGK-SVIYISHRLEEIFEIAD 217
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
280-495 |
5.43e-14 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 71.37 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKiHSPRDAVKNGIGLVPEDrktaGLIL 359
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE-LSSGSILIDGVDIS-KIGLHDLRSRISIIPQD----PVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 360 QMSVLHNITlPsvvmklivrkFGL-----IDSQLEKEIVRSFIEKLNIKTPSPYQIV-ENLSGGNQQKVVLAKWLAIKPK 433
Cdd:cd03244 91 SGTIRSNLD-P----------FGEysdeeLWQALERVGLKEFVESLPGGLDTVVEEGgENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 434 VLLLDEPTRGIDVNAKSEIYKLISEmAVSGMGVVMVSSELPEILAmSDRILVMSEGRkTAEF 495
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGR-VVEF 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-242 |
5.82e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.36 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEV-RFRnpREAQENGIALIPQeldlVPNLSS- 104
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtKLQ--LDSWRSRLAVVSQ----TPFLFSd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 105 --AENIFLSREPVNefgvieyQKMFEQASKLFSklgVNID----PK---TKVED----LSTSQQQMVAIAKALSLDAKII 171
Cdd:PRK10789 404 tvANNIALGRPDAT-------QQEIEHVARLAS---VHDDilrlPQgydTEVGErgvmLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 172 IMDEPTSAIGKReTEQlfNIIRSLKN--EGKSVIYISHRLEEIFEiADRVVVMRDGRKVGEGpieefDHDKLV 242
Cdd:PRK10789 474 ILDDALSAVDGR-TEH--QILHNLRQwgEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRG-----NHDQLA 537
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-238 |
6.21e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 73.34 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVI-AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrNPREAQENGIAL 91
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV---NELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENIF-------LSREpvnefgviEYQKMFEQASKLfsklgVNIDP--KTKVEDLSTSQQQMVAIAK 162
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAyglkirgMPKA--------EIEERVAEAARI-----LELEPllDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 163 ALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGR--KVGEgPIEEFDH 238
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVaeQIGT-PVEVYEK 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
284-490 |
7.43e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 70.51 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 284 DDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKiHSPRDAV---KNGIGLVPEDRKtagLIL 359
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKeELP--TSGTIRVNGQDVS-DLRGRAIpylRRKIGVVFQDFR---LLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 360 QMSVLHNITLPSVVMKlivrkfglIDSQLEKEIVRSFIEKLNIKTPSpYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDE 439
Cdd:cd03292 92 DRNVYENVAFALEVTG--------VPPREIRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181991 440 PTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
29-244 |
7.55e-14 |
|
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: 74.09 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 29 NNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNP---REAqengIALIPQELDLVpNLSSA 105
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQaslRAA----IGIVPQDTVLF-NDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 106 ENIFLSREPVNEFGVieyqkmfEQASKLfsklgVNIDP---------KTKVED----LSTSQQQMVAIAKALSLDAKIII 172
Cdd:COG5265 450 YNIAYGRPDASEEEV-------EAAARA-----AQIHDfieslpdgyDTRVGErglkLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 173 MDEPTSAIGKReTEQlfNIIRSLKN--EGKSVIYISHRLEEIFEiADRVVVMRDGRKVGEGpieefDHDKLVRL 244
Cdd:COG5265 518 FDEATSALDSR-TER--AIQAALREvaRGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG-----THAELLAQ 582
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-220 |
7.58e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 30 NVTLQIYKGE-VCaLVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFR----NPREAQEN-------GIALIPQEL- 96
Cdd:PRK11147 21 NAELHIEDNErVC-LVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqdPPRNVEGTvydfvaeGIEEQAEYLk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 97 ------DLVPNLSSAENifLSR-EPVNEfgVIEYQKMFEQASKLFSKLG-VNIDPKTKVEDLSTSQQQMVAIAKALSLDA 168
Cdd:PRK11147 100 ryhdisHLVETDPSEKN--LNElAKLQE--QLDHHNLWQLENRINEVLAqLGLDPDAALSSLSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490181991 169 KIIIMDEPTSAIGKRETEQLFNIirsLKNEGKSVIYISHRLEEIFEIADRVV 220
Cdd:PRK11147 176 DVLLLDEPTNHLDIETIEWLEGF---LKTFQGSIIFISHDRSFIRNMATRIV 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-225 |
7.87e-14 |
|
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: 70.82 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 23 PGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGK---EVRFRNPREAQENGIALIPQELDLV 99
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 100 pNLSSAENIFLSrEPVNEfgviEYQKMFEQASKLfsKLGVNIDP---KTKVED----LSTSQQQMVAIAKALSLDAKIII 172
Cdd:cd03290 92 -NATVEENITFG-SPFNK----QRYKAVTDACSL--QPDIDLLPfgdQTEIGErginLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 173 MDEPTSAIGKRETEQLFN--IIRSLKNEGKSVIYISHRLEEIFEiADRVVVMRDG 225
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
283-512 |
8.02e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.45 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG--AHPGRTEGKVFIGGKEIkIHSPRDAVK----NGIGLVPEDRKTAg 356
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllAANGRIGGSATFNGREI-LNLPEKELNklraEQISMIFQDPMTS- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSVLHNItlpsvvMKLIVRKFGLIDSQLEKEIVRsfieKLN-IKTPS--------PYQivenLSGGNQQKVVLAKW 427
Cdd:PRK09473 110 LNPYMRVGEQL------MEVLMLHKGMSKAEAFEESVR----MLDaVKMPEarkrmkmyPHE----FSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 428 LAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGRkTAEFLR-EEV----- 500
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR-TMEYGNaRDVfyqps 254
|
250
....*....|....
gi 490181991 501 --TEEDLLKaAIPR 512
Cdd:PRK09473 255 hpYSIGLLN-AVPR 267
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
275-502 |
8.88e-14 |
|
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: 70.72 E-value: 8.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 275 SLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKiHSPRDAVKNGIGLVPEDRkt 354
Cdd:cd03254 11 SYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD-PQKGQILIDGIDIR-DISRKSLRSMIGVVLQDT-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 355 agLILQMSVLHNItlpsvvmklivrKFGLIDSQLEKEIVRS-------FIEKLniktPSPYQIV-----ENLSGGNQQKV 422
Cdd:cd03254 87 --FLFSGTIMENI------------RLGRPNATDEEVIEAAkeagahdFIMKL----PNGYDTVlgengGNLSQGERQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 423 VLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVsGMGVVMVSSELPEILAmSDRILVMSEGRKTAEFLREEVTE 502
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-238 |
1.02e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 71.70 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVR------------------FRNPR-----E 83
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkdikqirkkvglvFQFPEsqlfeE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 84 AQENGIALIPQELdlvpNLSSAENIFLSREPVNEFGVIEyqkmfeqasKLFSKlgvniDPKtkveDLSTSQQQMVAIAKA 163
Cdd:PRK13649 102 TVLKDVAFGPQNF----GVSQEEAEALAREKLALVGISE---------SLFEK-----NPF----ELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 164 LSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG-PIEEFDH 238
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGkPKDIFQD 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
284-490 |
1.18e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.11 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 284 DDVSFYVRKGEVLGIYGLVGAGRTELLEAIfGAHPGRTEGKVFIGGKEIKIHS--------PRDAVKNGIGLV---PEDr 352
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNAL-SARLAPDAGEVHYRMRDGQLRDlyalseaeRRRLLRTEWGFVhqhPRD- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 353 ktaGLILQMSVLHNITLPsvVMKLIVRKFGLIDSQ----LEK-EIVRSFIEKLniktPSPYqivenlSGGNQQKVVLAKW 427
Cdd:PRK11701 101 ---GLRMQVSAGGNIGER--LMAVGARHYGDIRATagdwLERvEIDAARIDDL----PTTF------SGGMQQRLQIARN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 428 LAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
273-520 |
1.28e-13 |
|
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: 70.99 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 273 LWSLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSP--RDAVKNGIGLVP 349
Cdd:TIGR02769 18 FGAKQRAPVL-TNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlEKP--AQGTVSFRGQDLYQLDRkqRRAFRRDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 350 EDRKTAgLILQMSVLHNITLPsvvmkliVRKFGLIDSQLEKEIVRSFIEKLNIKTPSPYQIVENLSGGNQQKVVLAKWLA 429
Cdd:TIGR02769 95 QDSPSA-VNPRMTVRQIIGEP-------LRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 430 IKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGR-----KTAEFLREEVTEE 503
Cdd:TIGR02769 167 VKPKLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQiveecDVAQLLSFKHPAG 246
|
250
....*....|....*....
gi 490181991 504 DLLKAAI--PRSVKVETTQ 520
Cdd:TIGR02769 247 RNLQSAVlpEHPVRRSITT 265
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-238 |
1.32e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.88 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIaVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYP----DYEGQIFLEGKEVrfrNPREAQENG 88
Cdd:PRK10418 5 IELRNIALQAAQPL-VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPV---APCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQeldlvpNLSSAENiflsrePVnefgvieyQKMFEQASKLFSKLGVNIDPKTKVE-------------------D 149
Cdd:PRK10418 81 IATIMQ------NPRSAFN------PL--------HTMHTHARETCLALGKPADDATLTAaleavglenaarvlklypfE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 150 LSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKV 228
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
250
....*....|
gi 490181991 229 GEGPIEEFDH 238
Cdd:PRK10418 221 EQGDVETLFN 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-235 |
1.63e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.16 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 29 NNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYP---DYEGQIFLEGKevrfrnPREAQE-NGIALIPQELDL-VPNLS 103
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGM------PIDAKEmRAISAYVQQDDLfIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 104 SAENIFLS---REPVNefgVIEYQKMfEQASKLFSKLGVNIDPKTK------VEDLSTSQQQMVAIAKALSLDAKIIIMD 174
Cdd:TIGR00955 116 VREHLMFQahlRMPRR---VTKKEKR-ERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 175 EPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHR-LEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-207 |
1.84e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.52 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAqengIALI 92
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA----CHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENI-----FLSREPVNEFGVIEyqkmfeqasklfsklGVNIDPKT--KVEDLSTSQQQMVAIAKALS 165
Cdd:PRK13539 79 GHRNAMKPALTVAENLefwaaFLGGEELDIAAALE---------------AVGLAPLAhlPFGYLSAGQKRRVALARLLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490181991 166 LDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISH 207
Cdd:PRK13539 144 SNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
283-486 |
2.11e-13 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 72.32 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIkIHSPRDAVKNGIGLVPEdrktAGLILQM 361
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGfVDP--TEGSIAVNGVPL-ADADADSWRDQIAWVPQ----HPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNITLpsvvmklivRKFGLIDSQLEKEIVR----SFIEKLniktPSPYQIV-----ENLSGGNQQKVVLAKWLAIKP 432
Cdd:TIGR02857 411 TIAENIRL---------ARPDASDAEIREALERagldEFVAAL----PQGLDTPigeggAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 433 KVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSElPEILAMSDRILVM 486
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHR-LALAALADRIVVL 529
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-232 |
2.32e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPD--------YEGQIFLEGKEV-RFRNPREAQENgiALIPQELDL 98
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarVTGDVTLNGEPLaAIDAPRLARLR--AVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 99 VPNLSSAENIFLSREPVNEFGVIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALS---------LDAK 169
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 170 IIIMDEPTSAIGKRETEQLFNIIRSLKNEGK-SVIYISHRLEEIFEIADRVVVMRDGRKVGEGP 232
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-242 |
2.60e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKI---LAGVYPDY--EGQIFLEGK---------- 74
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFrvEGKVTFHGKnlyapdvdpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 75 EVRFRnpreaqengIALIPQELDLVPNlSSAENIflsrepvnEFG--VIEYQ-KMFEQASKLFSKLGVNIDPKTKVED-- 149
Cdd:PRK14243 88 EVRRR---------IGMVFQKPNPFPK-SIYDNI--------AYGarINGYKgDMDELVERSLRQAALWDEVKDKLKQsg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 150 --LSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKnEGKSVIYISHRLEEIFEIAD-----RVVVM 222
Cdd:PRK14243 150 lsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSDmtaffNVELT 228
|
250 260
....*....|....*....|
gi 490181991 223 RDGRKVGEgpIEEFDHDKLV 242
Cdd:PRK14243 229 EGGGRYGY--LVEFDRTEKI 246
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-236 |
2.72e-13 |
|
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: 73.06 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKevrfrnpreaqengIALIPQELdLVPNLSSAEN 107
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQA-WIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 108 IFLSRePVNEfgviEYQKMFEQASKLFSKL-----GVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGK 182
Cdd:TIGR00957 719 ILFGK-ALNE----KYYQQVLEACALLPDLeilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 183 RETEQLFNIIRSLKN--EGKSVIYISHRLEEIFEIaDRVVVMRDGRKVGEGPIEEF 236
Cdd:TIGR00957 794 HVGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
266-490 |
2.84e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 266 FRVEGIKLWSLDRKKLL--VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHSPRD--AV 341
Cdd:PRK15079 18 FDIKDGKQWFWQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA-TDGEVAWLGKDLLGMKDDEwrAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 342 KNGIGLVPEDrKTAGLILQMSVLHNITLPsvvmkLIVRKFGLIDSQLeKEIVRSFIEKL----NIKTPSPYQivenLSGG 417
Cdd:PRK15079 97 RSDIQMIFQD-PLASLNPRMTIGEIIAEP-----LRTYHPKLSRQEV-KDRVKAMMLKVgllpNLINRYPHE----FSGG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 418 NQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
283-486 |
3.11e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 70.70 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGR---TEGKVFIGGKEIKIHSPRdavkngiglvpEDRKTAG--- 356
Cdd:COG4170 23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvTADRFRWNGIDLLKLSPR-----------ERRKIIGrei 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 -LILQ--MSVLHnitlPSV-VMKLIvrKFGLIDSQLE----------KEIVRSFIEKLNIKTPS------PYQIVEnlsg 416
Cdd:COG4170 92 aMIFQepSSCLD----PSAkIGDQL--IEAIPSWTFKgkwwqrfkwrKKRAIELLHRVGIKDHKdimnsyPHELTE---- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 417 GNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMA-VSGMGVVMVSSELPEILAMSDRILVM 486
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHDLESISQWADTITVL 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-221 |
3.47e-13 |
|
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: 69.36 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 35 IYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRnpreaqengialiPQELDlvPNLSSAENIFLSrEP 114
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-------------PQYIK--ADYEGTVRDLLS-SI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 115 VNEFGVIEYQKmfeqaSKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIgkrETEQLFNIIRS 194
Cdd:cd03237 86 TKDFYTHPYFK-----TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL---DVEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|.
gi 490181991 195 LK----NEGKSVIYISHRLEEIFEIADRVVV 221
Cdd:cd03237 158 IRrfaeNNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
290-490 |
3.56e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.39 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 290 VRKGEVLGIYGLVGAGRTELLEAI-FGAHPgrTEGKVFIGGKEIKIHSPRDAVKngiGLVPEDRKTAGLILQ-------M 361
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCInLLEQP--EAGTIRVGDITIDTARSLSQQK---GLIRQLRQHVGFVFQnfnlfphR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNITLPSVVMKLIVRkfglidsQLEKEIVRSFIEKLNI---KTPSPyqivENLSGGNQQKVVLAKWLAIKPKVLLLD 438
Cdd:PRK11264 101 TVLENIIEGPVIVKGEPK-------EEATARARELLAKVGLagkETSYP----RRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490181991 439 EPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-225 |
4.53e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 72.35 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVI--AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfrnpreaqeNGI 89
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---------TNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELDLVPNLSSAENIFLSREPVNEFGV---IEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSL 166
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHLYLYARlrgVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 167 DAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDG 225
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
27-230 |
4.99e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.36 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEV-RFRNpREAQ--ENGIALIPQELDLVPNLS 103
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItRLKN-REVPflRRQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 104 SAENIFLsrePVNEFGVIEyQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKR 183
Cdd:PRK10908 96 VYDNVAI---PLIIAGASG-DDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490181991 184 ETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGE 230
Cdd:PRK10908 172 LSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
277-500 |
5.31e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 69.35 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAiFGAHPGRTEGKVFIGGKEIKihsprdavknGIGLVPEDRKTAG 356
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKH-MNALLIPSEGKVYVDGLDTS----------DEENLWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSvlHNITLPSVVMKLIVrkFGLIDSQLEKEIVRSFIE----KLNI---KTPSPYQivenLSGGNQQKVVLAKWLA 429
Cdd:PRK13633 89 MVFQNP--DNQIVATIVEEDVA--FGPENLGIPPEEIRERVDeslkKVGMyeyRRHAPHL----LSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 430 IKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEIlAMSDRILVMSEGRKTAEFLREEV 500
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEI 231
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
27-235 |
7.87e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.39 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYpDYEGQIFLEGKEVRFRNPREAQENgialipQELDLVpnlsSAE 106
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI-DYPGRVMAEKLEFNGQDLQRISEK------ERRNLV----GAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 107 NIFLSREPVNE--------FGVIEYQKMFEQASK---------LFSKLGVNiDPKTKVE----DLSTSQQQMVAIAKALS 165
Cdd:PRK11022 91 VAMIFQDPMTSlnpcytvgFQIMEAIKVHQGGNKktrrqraidLLNQVGIP-DPASRLDvyphQLSGGMSQRVMIAMAIA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 166 LDAKIIIMDEPTSAIGKRETEQLFNIIRSL-KNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK11022 170 CRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
263-509 |
7.99e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 69.06 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 263 DEIFRVEGIKLWSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG--AHPGRTEGKVFIGGKEIKIHSPRDa 340
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGllLPDDNPNSKITVDGITLTAKTVWD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 341 VKNGIGLVPE--DRKTAGLILQMSV---LHNITLPSVVMKLIVRKfglidsqlekeiVRSFIEKLNIKTPSPyqivENLS 415
Cdd:PRK13640 82 IREKVGIVFQnpDNQFVGATVGDDVafgLENRAVPRPEMIKIVRD------------VLADVGMLDYIDSEP----ANLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 416 GGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISE-MAVSGMGVVMVSSELPEIlAMSDRILVMSEGRKTAE 494
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQ 224
|
250
....*....|....*.
gi 490181991 495 FLREEV-TEEDLLKAA 509
Cdd:PRK13640 225 GSPVEIfSKVEMLKEI 240
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
283-507 |
8.97e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.65 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKiHSPRDAVKNGIglvpedRKTAGLILQM 361
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAlLKP--TTGTVTVDDITIT-HKTKDKYIRPV------RKRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 --SVLHNITlpsvVMKLIVrkFGLIDSQLEKEIVRSFIEKL--------NIKTPSPYQivenLSGGNQQKVVLAKWLAIK 431
Cdd:PRK13646 94 peSQLFEDT----VEREII--FGPKNFKMNLDEVKNYAHRLlmdlgfsrDVMSQSPFQ----MSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 432 PKVLLLDEPTRGIDVNAKSEIYKLISEMAV-SGMGVVMVSSELPEILAMSDRILVMSEGRktaefLREEVTEEDLLK 507
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGS-----IVSQTSPKELFK 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
285-490 |
1.53e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTELLEaIFGAHPGRTEGKVFIGGKEIKIHSPRDAvKNGIGLvpedRKTAGLILQ---- 360
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEMPRSGTLNIAGNHFDFSKTPSD-KAIREL----RRNVGMVFQqynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 ---MSVLHN-ITLPsvvmkliVRKFGLIDSQLEKEiVRSFIEKLNIKTPS---PYQivenLSGGNQQKVVLAKWLAIKPK 433
Cdd:PRK11124 94 wphLTVQQNlIEAP-------CRVLGLSKDQALAR-AEKLLERLRLKPYAdrfPLH----LSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 434 VLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGH 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
281-508 |
1.54e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.71 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 281 LLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAH-PgrTEGKVFIGGKEIKIHSPRDAVKNGiglVPEDRKTAGLIL 359
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkP--TGGTILLRGQHIEGLPGHQIARMG---VVRTFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 360 QMSVLHNItLPSVVMKLIVRKF-GLIDS----QLEKEIVRS---FIEKLNIkTPSPYQIVENLSGGNQQKVVLAKWLAIK 431
Cdd:PRK11300 94 EMTVIENL-LVAQHQQLKTGLFsGLLKTpafrRAESEALDRaatWLERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 432 PKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEV-TEEDLLKA 508
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIrNNPDVIKA 250
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
263-509 |
1.55e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.84 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 263 DEIFRVEGIKLWSLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRtEGKVFIGGKEIKIHSPRDaVK 342
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ-RGRVKVMGREVNAENEKW-VR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 343 NGIGLV---PEDRktaglILQMSVLHNITLPSVVMKLIVRKfglIDSQLEKEIVRSFIEKLNIKTPspyqivENLSGGNQ 419
Cdd:PRK13647 79 SKVGLVfqdPDDQ-----VFSSTVWDDVAFGPVNMGLDKDE---VERRVEEALKAVRMWDFRDKPP------YHLSYGQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 420 QKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREE 499
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSL 224
|
250
....*....|
gi 490181991 500 VTEEDLLKAA 509
Cdd:PRK13647 225 LTDEDIVEQA 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
283-490 |
1.68e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLE---------------AIFGAHPGRTEGKVFIGGKEIKIHSPRD-AVKNgig 346
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnalllpdtgtiewIFKDEKNKKKTKEKEKVLEKLVIQKTRFkKIKK--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 347 lVPEDRKTAGLILQMSVLHniTLPSVVMKLIV---RKFGlIDSQLEKEIVRSFIEKLNIKTP----SPYqiveNLSGGNQ 419
Cdd:PRK13651 100 -IKEIRRRVGVVFQFAEYQ--LFEQTIEKDIIfgpVSMG-VSKEEAKKRAAKYIELVGLDESylqrSPF----ELSGGQK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 420 QKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
275-490 |
1.84e-12 |
|
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: 66.40 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 275 SLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGaHPGR--TEGKVFIGGKEIKIHSPRDAVKNGIGlvpedr 352
Cdd:cd03217 9 SVGGKEIL-KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYevTEGEILFKGEDITDLPPEERARLGIF------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 353 ktaglilqMSVLHNITLPSVVMKlivrkfglidsqlekeivrSFIEKLNiktpspyqivENLSGGNQQKVVLAKWLAIKP 432
Cdd:cd03217 81 --------LAFQYPPEIPGVKNA-------------------DFLRYVN----------EGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 433 KVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVsSELPEILAM--SDRILVMSEGR 490
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLII-THYQRLLDYikPDRVHVLYDGR 182
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-208 |
2.55e-12 |
|
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: 64.87 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEvrfrnpreaqenGIALIPQELDLVP-NLssae 106
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------------DLLFLPQRPYLPLgTL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 107 niflsREpvnefgVIEYqkmfeqasklfsklgvnidPKTKVedLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIgkrETE 186
Cdd:cd03223 81 -----RE------QLIY-------------------PWDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSAL---DEE 125
|
170 180
....*....|....*....|..
gi 490181991 187 QLFNIIRSLKNEGKSVIYISHR 208
Cdd:cd03223 126 SEDRLYQLLKELGITVISVGHR 147
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
272-490 |
3.25e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 272 KLWSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTE--GKVFIGGKeikihsPRDAvkngiglvP 349
Cdd:TIGR00955 30 CFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKgsGSVLLNGM------PIDA--------K 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 350 EDRKTAGLILQmsvlHNITLPSvvmkLIVRKFGLIDSQL----------EKEIVRSFIEKL------NIKTPSPYQiVEN 413
Cdd:TIGR00955 96 EMRAISAYVQQ----DDLFIPT----LTVREHLMFQAHLrmprrvtkkeKRERVDEVLQALglrkcaNTRIGVPGR-VKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 414 LSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMV----SSELPEILamsDRILVMSEG 489
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEG 243
|
.
gi 490181991 490 R 490
Cdd:TIGR00955 244 R 244
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-237 |
3.26e-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: 69.59 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 26 IAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEG--------KEVRFRnpreaqengIALIPQEld 97
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglHDLRFK---------ITIIPQD-- 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 98 lvPNLSSAeNIFLSREPVNEFGVIEYQKMFEQA--SKLFSKL--GVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIM 173
Cdd:TIGR00957 1369 --PVLFSG-SLRMNLDPFSQYSDEEVWWALELAhlKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 174 DEPTSAIgKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIAdRVVVMrdgrkvGEGPIEEFD 237
Cdd:TIGR00957 1446 DEATAAV-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVL------DKGEVAEFG 1501
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-445 |
3.54e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.50 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 33 LQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQiflegKEVRFRNP-REAQENGIALIPQEL-----DLvpnLSSAE 106
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-----RQSQFSHItRLSFEQLQKLVSDEWqrnntDM---LSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 107 NIF--LSREpvnefgVI-EYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKR 183
Cdd:PRK10938 96 DDTgrTTAE------IIqDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 184 ETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLV-RLMVGRSIDQFFIKERATIT 262
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVaQLAHSEQLEGVQLPEPDEPS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 263 DEIFRVEGIKLWSL--------DRKKLlvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHP----------GRTEGK 324
Cdd:PRK10938 250 ARHALPANEPRIVLnngvvsynDRPIL--HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgysndltlfGRRRGS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 325 vfigGK---EIKIHsprdavkngIGLVPedrktaglilqmSVLH-----NITLPSVVMKLIVRKFGLID--SQLEKEIVR 394
Cdd:PRK10938 328 ----GEtiwDIKKH---------IGYVS------------SSLHldyrvSTSVRNVILSGFFDSIGIYQavSDRQQKLAQ 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 395 SFIEKLNIKTP---SPYQiveNLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGID 445
Cdd:PRK10938 383 QWLDILGIDKRtadAPFH---SLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-481 |
3.56e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.60 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 274 WSLDRKKLlVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHP----GRTEGKVFIGGKEI---KIHSPRdaVKNGIG 346
Cdd:PRK14258 15 FYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEleseVRVEGRVEFFNQNIyerRVNLNR--LRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 347 LV-PEDRktaglILQMSVLHNITL--------PSVVMKLIVRKfGLIDSQLEKEIvRSFIEKLNIktpspyqiveNLSGG 417
Cdd:PRK14258 92 MVhPKPN-----LFPMSVYDNVAYgvkivgwrPKLEIDDIVES-ALKDADLWDEI-KHKIHKSAL----------DLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 418 NQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAV-SGMGVVMVSSELPEILAMSD 481
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLrSELTMVIVSHNLHQVSRLSD 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
320-508 |
3.69e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 320 RTEGKVFIGGKEIKIHSPRDaVKNGIGLVPEDRktagLILQMSVLHNItlpsvvmklivrKFGLIDSQLEK-------EI 392
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKD-LRNLFSIVSQEP----MLFNMSIYENI------------KFGKEDATREDvkrackfAA 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 393 VRSFIEKLNIKTPS---PYQivENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMV 469
Cdd:PTZ00265 1337 IDEFIESLPNKYDTnvgPYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
170 180 190
....*....|....*....|....*....|....*....
gi 490181991 470 SSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLKA 508
Cdd:PTZ00265 1415 IAHRIASIKRSDKIVVFNNPDRTGSFVQAHGTHEELLSV 1453
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
280-504 |
4.13e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.71 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTeGKVFIGGKEIKIHSpRDAVKngiglvpEDRKTAGLIL 359
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH-GEILFDGENIPAMS-RSRLY-------TVRKRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 360 Q-------MSVLHNITLPsvvmkliVRKfgliDSQLEKEIVRSFI----EKLNIKTPSPYQIVEnLSGGNQQKVVLAKWL 428
Cdd:PRK11831 91 QsgalftdMNVFDNVAYP-------LRE----HTQLPAPLLHSTVmmklEAVGLRGAAKLMPSE-LSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 429 AIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEED 504
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
27-225 |
4.29e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.34 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKIL---AGVYPDYE--GQIFLEGKEVRFRNPREAQ-ENGIALIPQELDLVP 100
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEVTitGSIVYNGHNIYSPRTDTVDlRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 101 nLSSAENIFLSrepVNEFGVIEYQKMFEQASKlfSKLGVNI--DPKTKVED----LSTSQQQMVAIAKALSLDAKIIIMD 174
Cdd:PRK14239 100 -MSIYENVVYG---LRLKGIKDKQVLDEAVEK--SLKGASIwdEVKDRLHDsalgLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181991 175 EPTSAIGKRETEQLFNIIRSLKNEgKSVIYISHRLEEIFEIADRVVVMRDG 225
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-247 |
4.74e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.90 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 23 PGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVY---------------------PDYE--------------- 66
Cdd:PTZ00265 1179 PNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneQDYQgdeeqnvgmknvnef 1258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 67 ------------------GQIFLEGKEVRFRNPREAQeNGIALIPQElDLVPNLSSAENIFLSREPVNEFGV---IEYQK 125
Cdd:PTZ00265 1259 sltkeggsgedstvfknsGKILLDGVDICDYNLKDLR-NLFSIVSQE-PMLFNMSIYENIKFGKEDATREDVkraCKFAA 1336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 126 MFEQASKLFSKLGVNIDPKTKveDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEG-KSVIY 204
Cdd:PTZ00265 1337 IDEFIESLPNKYDTNVGPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIIT 1414
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490181991 205 ISHRLEEIfEIADRVVVMRDGRKVGEGPIEEFDHDKLVRLMVG 247
Cdd:PTZ00265 1415 IAHRIASI-KRSDKIVVFNNPDRTGSFVQAHGTHEELLSVQDG 1456
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-235 |
8.26e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 31 VTLQIYKGEVCALVGENGAGKSTLMKILAGVYPdYEGQIFLEGKEVRFRNPRE---------AQENGIALIP--QELDLv 99
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElarhraylsQQQTPPFAMPvfQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 100 pNLSSAENIFLSREPVNEFGvieyqkmfeQASKLFSKLGvnidpkTKVEDLSTSQQQMVAIA-------KALSLDAKIII 172
Cdd:PRK03695 93 -HQPDKTRTEAVASALNEVA---------EALGLDDKLG------RSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 173 MDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
283-500 |
8.48e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.30 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA--HPGR-TEGKVFIGGKEIKIHSPRdavkngiglvpEDRKTAG--- 356
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGRvMAEKLEFNGQDLQRISEK-----------ERRNLVGaev 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 -LILQ--MSVLH-NITLPSVVMKLI-VRKFGLIDSQLEKEIvrSFIEKLNIKTPS------PYQivenLSGGNQQKVVLA 425
Cdd:PRK11022 92 aMIFQdpMTSLNpCYTVGFQIMEAIkVHQGGNKKTRRQRAI--DLLNQVGIPDPAsrldvyPHQ----LSGGMSQRVMIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 426 KWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMA-VSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEV 500
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-231 |
8.58e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.91 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrnPREAQENGIALIPQELDLVPNLSSAE 106
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVV----SSTSKQKEIKPVRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 107 nifLSREPVNE---FGVIEYQKMFEQASKLFSK------LGVNIDPKTKVEdLSTSQQQMVAIAKALSLDAKIIIMDEPT 177
Cdd:PRK13643 97 ---LFEETVLKdvaFGPQNFGIPKEKAEKIAAEklemvgLADEFWEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 178 SAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG 231
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
283-490 |
9.44e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 64.76 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHpGRTEGKVFI--GGKEIKIH--SPRDAV---KNGIGLV------- 348
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNY-LPDSGSILVrhDGGWVDLAqaSPREILalrRRTIGYVsqflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 349 PedRKTAgliLQmsvlhnitlpsVVMK-LIVRkfGlIDSQLEKEIVRSFIEKLNIKtpspyqivENL--------SGGNQ 419
Cdd:COG4778 106 P--RVSA---LD-----------VVAEpLLER--G-VDREEARARARELLARLNLP--------ERLwdlppatfSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 420 QKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
283-490 |
9.72e-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: 64.44 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFY-----------VRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKiHSPrdavkngiglvPED 351
Cdd:cd03298 3 LDKIRFSygeqpmhfdltFAQGEITAIVGPSGSGKSTLLNLIAGFETP-QSGRVLINGVDVT-AAP-----------PAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 352 RKTA------GLILQMSVLHNITL---PSVVMKLIVRKfglidsQLEKEIVRSFIEKLNIKTPspyqivENLSGGNQQKV 422
Cdd:cd03298 70 RPVSmlfqenNLFAHLTVEQNVGLglsPGLKLTAEDRQ------AIEVALARVGLAGLEKRLP------GELSGGERQRV 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 423 VLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03298 138 ALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
38-222 |
1.03e-11 |
|
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: 65.08 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 38 GEVCALVGENGAGKSTLMKILAGVY----------PDYEGQI-FLEGKEVR--FRNPREAQENgIALIPQELDLVPNlSS 104
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLkpnlgkfddpPDWDEILdEFRGSELQnyFTKLLEGDVK-VIVKPQYVDLIPK-AV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 105 AENIFLSREPVNEFGVIEYqkmfeqaskLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRE 184
Cdd:cd03236 104 KGKVGELLKKKDERGKLDE---------LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 490181991 185 TEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVM 222
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-445 |
1.09e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.46 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 14 EARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENGIALIP 93
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 94 QEL--DLVPNLSSAENI-FLSRepvnEFGvieyQKMFEQASKlfsklgvnID--------------PKTKvedLSTSQQQ 156
Cdd:NF033858 83 QGLgkNLYPTLSVFENLdFFGR----LFG----QDAAERRRR--------IDellratglapfadrPAGK---LSGGMKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 157 MVAIAKALSLDAKIIIMDEPTSAI---GKRETEQLFNIIRSlKNEGKSVI----YIshrlEEifeiADR---VVVMRDGR 226
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVdplSRRQFWELIDRIRA-ERPGMSVLvataYM----EE----AERfdwLVAMDAGR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 227 KVGEGPIEEfdhdkLVRLMVGRSIDQFFI------KERATITDEI--FRVEGIKLWSLDRKKLL--------VDDVSFYV 290
Cdd:NF033858 215 VLATGTPAE-----LLARTGADTLEAAFIallpeeKRRGHQPVVIppRPADDDDEPAIEARGLTmrfgdftaVDHVSFRI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 291 RKGEVLGIYGLVGAGR-------TELLEAifgahpgrTEGKVFIGGKEIKihsPRDAvkngiglvpEDRKTAGLILQ--- 360
Cdd:NF033858 290 RRGEIFGFLGSNGCGKsttmkmlTGLLPA--------SEGEAWLFGQPVD---AGDI---------ATRRRVGYMSQafs 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 ----MSVLHNITLPSvvmklivRKFGLIDSQLE---KEIVRSF-----IEKLniktPspyqivENLSGGNQQKVVLAkwL 428
Cdd:NF033858 350 lygeLTVRQNLELHA-------RLFHLPAAEIAarvAEMLERFdladvADAL----P------DSLPLGIRQRLSLA--V 410
|
490
....*....|....*....
gi 490181991 429 AI--KPKVLLLDEPTRGID 445
Cdd:NF033858 411 AVihKPELLILDEPTSGVD 429
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
262-490 |
1.15e-11 |
|
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: 67.02 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 262 TDEIFRVEGIKLW--SLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHP---GRTEGKVFIGGKEIKIHS 336
Cdd:COG4172 3 SMPLLSVEDLSVAfgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 337 PRD--AVK-NGIGLvpedrktaglILQ--MSVL---HNITlpSVVMKLIVRKFGLIDSQLEKEIVrSFIEKLNIKTPS-- 406
Cdd:COG4172 83 ERElrRIRgNRIAM----------IFQepMTSLnplHTIG--KQIAEVLRLHRGLSGAAARARAL-ELLERVGIPDPErr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 407 ----PYQivenLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSD 481
Cdd:COG4172 150 ldayPHQ----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFAD 225
|
....*....
gi 490181991 482 RILVMSEGR 490
Cdd:COG4172 226 RVAVMRQGE 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
282-484 |
1.22e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.79 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 282 LVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEikihsprdavknGIGLVPedrktaglilQM 361
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR-PTSGTVRRAGGA------------RVAYVP----------QR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNiTLPSVVMKLIV----RKFGLID--SQLEKEIVRSFIEKLNIKTPSPYQIVEnLSGGNQQKVVLAKWLAIKPKVL 435
Cdd:NF040873 64 SEVPD-SLPLTVRDLVAmgrwARRGLWRrlTRDDRAAVDDALERVGLADLAGRQLGE-LSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490181991 436 LLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRIL 484
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-247 |
1.26e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.43 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 26 IAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVrfrnprEAQENGIALIP--QELDLVPNLS 103
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVI------TAGKKNKKLKPlrKKVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 104 SAEnifLSRE---------PVNeFGVIEyQKMFEQASKLFSKLGVNIDPKTKVE-DLSTSQQQMVAIAKALSLDAKIIIM 173
Cdd:PRK13634 95 EHQ---LFEEtvekdicfgPMN-FGVSE-EDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 174 DEPTSAI---GKRETEQLFNIIRslKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEG-PIEEFDH-DKLVRLMVG 247
Cdd:PRK13634 170 DEPTAGLdpkGRKEMMEMFYKLH--KEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGtPREIFADpDELEAIGLD 246
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
284-507 |
1.28e-11 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 64.48 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 284 DDVSFYVRKGEVLGIYGLVGAGRT---ELLEAIFGAhpgrTEGKVFIGGKEIKIHSPRDaVKNGIGLVPEDRktagLILQ 360
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKStvvSLLERFYDP----TSGEILLDGVDIRDLNLRW-LRSQIGLVSQEP----VLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 MSVLHNITL--PSVVMKLIVR--KFGLIDSqlekeivrsFIEKLniktPSPYQIV-----ENLSGGNQQKVVLAKWLAIK 431
Cdd:cd03249 91 GTIAENIRYgkPDATDEEVEEaaKKANIHD---------FIMSL----PDGYDTLvgergSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 432 PKVLLLDEPTRGIDvnAKSEiyKLISEM---AVSGMGVVMVSSELPEILAmSDRILVMSEGRktaefLREEVTEEDLLK 507
Cdd:cd03249 158 PKILLLDEATSALD--AESE--KLVQEAldrAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQ-----VVEQGTHDELMA 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
283-507 |
1.28e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.01 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRtEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDRKT--AGLILQ 360
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ-KGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqfVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 MSVL---HNITLPSVVMKLIVRKfGLIDSQLEKEIVRSfieklniktpspyqiVENLSGGNQQKVVLAKWLAIKPKVLLL 437
Cdd:PRK13644 97 EDLAfgpENLCLPPIEIRKRVDR-ALAEIGLEKYRHRS---------------PKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 438 DEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEiLAMSDRILVMSEGRKTAEFLREEVTEEDLLK 507
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
284-490 |
1.49e-11 |
|
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: 64.38 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 284 DDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIkihSPRDavkngiglvpED------RKTAG 356
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRP--TSGTVRLAGQDL---FALD----------EDararlrARHVG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQ-------MSVLHNITLPsvvmkLIVRkfGLIDSQlekEIVRSFIEKLNIK---TPSPYQivenLSGGNQQKVVLAK 426
Cdd:COG4181 94 FVFQsfqllptLTALENVMLP-----LELA--GRRDAR---ARARALLERVGLGhrlDHYPAQ----LSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 427 WLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSElPEILAMSDRILVMSEGR 490
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHD-PALAARCDRVLRLRAGR 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-222 |
1.86e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.96 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 7 KEREVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPrEAQE 86
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 87 NGIALIPQELDLVPNLSSAENIF---LSREPVNEFGVIEYQKMFEQASKLFSKlgvnidpktKVEDLSTSQQQMVAIAKA 163
Cdd:PRK10247 81 QQVSYCAQTPTLFGDTVYDNLIFpwqIRNQQPDPAIFLDDLERFALPDTILTK---------NIAELSGGEKQRISLIRN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 164 LSLDAKIIIMDEPTSAIGKRETEQLFNII-RSLKNEGKSVIYISHRLEEIFEiADRVVVM 222
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIhRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
283-489 |
2.24e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.96 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGaHPGRTEGKVFIGGKEIKIHsprdavkngiglVPEDRKTAGLILQMS 362
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGKSILTN------------ISDVHQNMGYCPQFD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNITLPSVVMKLIVRKFGLIDSQLEKeIVRSFIEKLNIKTPSPyQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTR 442
Cdd:TIGR01257 2022 AIDDLLTGREHLYLYARLRGVPAEEIEK-VANWSIQSLGLSLYAD-RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490181991 443 GIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEG 489
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
283-491 |
2.57e-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: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGkeikiHSP---RDAVKNGIGLVpedrktAG-- 356
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIlVP--TSGEVRVLG-----YVPfkrRKEFARRIGVV------FGqr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 --LILQMSVLHNITLpsvvMKLIVRkfglIDSQLEKEIVRSFIEKLNI----KTPspyqiVENLSGGNQQKVVLAKWLAI 430
Cdd:COG4586 105 sqLWWDLPAIDSFRL----LKAIYR----IPDAEYKKRLDELVELLDLgellDTP-----VRQLSLGQRMRCELAAALLH 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 431 KPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGRK 491
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
283-490 |
2.87e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 64.71 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTEL------LEaifgaHPgrTEGKVFIGGKEIKIHSPRD--AVKNGIGLVPE---- 350
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLircinlLE-----RP--TSGSVLVDGVDLTALSERElrAARRKIGMIFQhfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 351 -DRKTaglilqmsVLHNITLPsvvMKLI-VRKfglidsqleKEI---VRSFIE------KLNiKTPSpyqiveNLSGGNQ 419
Cdd:COG1135 94 lSSRT--------VAENVALP---LEIAgVPK---------AEIrkrVAELLElvglsdKAD-AYPS------QLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 420 QKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLI----SEMAVSgmgVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLkdinRELGLT---IVLITHEMDVVRRICDRVAVLENGR 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
285-490 |
3.24e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 63.49 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTELLEaIFGAHPGRTEGKVFIGGKEIKIHSPRDAvKNGIGLvpedRKTAGLILQ---- 360
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLR-VLNLLETPDSGQLNIAGHQFDFSQKPSE-KAIRLL----RQKVGMVFQqynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 ---MSVLHN-ITLPSVVMKLivrkfglidsqlEKEIVRSFIEKL-------NIKTPSPYQivenLSGGNQQKVVLAKWLA 429
Cdd:COG4161 94 wphLTVMENlIEAPCKVLGL------------SKEQAREKAMKLlarlrltDKADRFPLH----LSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 430 IKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
280-490 |
3.35e-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: 62.49 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGkeikihsprdavknGIGLVPEdrkTAgLIL 359
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE-KLSGSVSVPG--------------SIAYVSQ---EP-WIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 360 QMSVLHNITlpsvvmklivrkFGL-IDSQLEKEIVRSF-----IEKLN--IKTpspyQIVE---NLSGGNQQKVVLAKWL 428
Cdd:cd03250 79 NGTIRENIL------------FGKpFDEERYEKVIKACalepdLEILPdgDLT----EIGEkgiNLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 429 AIKPKVLLLDEPTRGIDVNAKSEIY-KLISEMAVSGMGVVMVSSELpEILAMSDRILVMSEGR 490
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
283-510 |
4.09e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.57 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDaVKNGIGLVPE--DRKTAGLILQ 360
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-EFEGKVKIDGELLTAENVWN-LRRKIGMVFQnpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 MSVLHNITLPSVVMKLIVRKfglIDSQLEKeivrsfIEKLNIKTPSPYQivenLSGGNQQKVVLAKWLAIKPKVLLLDEP 440
Cdd:PRK13642 101 DDVAFGMENQGIPREEMIKR---VDEALLA------VNMLDFKTREPAR----LSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 441 TRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEIlAMSDRILVMSEGRKTAEFLREEV--TEEDLLKAAI 510
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELfaTSEDMVEIGL 239
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-234 |
4.32e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.21 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFP-GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLegkevrfrnPREAQengIAL 91
Cdd:COG4178 363 LALEDLTLRTPdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGAR---VLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVP-NLSSAenifLSR-EPVNEFGVIEYQKMFEQA--SKLFSKLGVNiDPKTKVedLSTSQQQMVAIAKALSLD 167
Cdd:COG4178 431 LPQRPYLPLgTLREA----LLYpATAEAFSDAELREALEAVglGHLAERLDEE-ADWDQV--LSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 168 AKIIIMDEPTSAIGkRETEQlfNIIRSLKNEGKSVIYIS--HRlEEIFEIADRVVVMRDGRKVGEGPIE 234
Cdd:COG4178 504 PDWLFLDEATSALD-EENEA--ALYQLLREELPGTTVISvgHR-STLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
277-494 |
4.33e-11 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 61.95 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRtEGKVFIGGKEIkiHSPRDAVKNGIGLVPedrktag 356
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ-QGEITLDGVPV--SDLEKALSSLISVLN------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 lilQMSVLHNITLPSvvmklivrkfglidsqlekeivrsfieklNIKTPspyqivenLSGGNQQKVVLAKWLAIKPKVLL 436
Cdd:cd03247 82 ---QRPYLFDTTLRN-----------------------------NLGRR--------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 437 LDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPEILAMsDRILVMSEGRKTAE 494
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
283-490 |
4.78e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.98 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNgiglvpedRKTAGLILQ-- 360
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE-PTSGEILFDGQDITGLSGRELRPL--------RRRMQMVFQdp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 -------MSVLHNITLPSVVmklivrkFGLIDSQLEKEIVRSFIEK--LNiktPS-----PYQivenLSGGNQQKVVLAK 426
Cdd:COG4608 105 yaslnprMTVGDIIAEPLRI-------HGLASKAERRERVAELLELvgLR---PEhadryPHE----FSGGQRQRIGIAR 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 427 WLAIKPKVLLLDEPTRGIDVNAKSEIYKLI----SEMavsGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG4608 171 ALALNPKLIVCDEPVSALDVSIQAQVLNLLedlqDEL---GLTYLFISHDLSVVRHISDRVAVMYLGK 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
283-489 |
5.08e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.23 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHSPRDaVKNGIGLV---PEDrKTAGLIL 359
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKV-KSGEIFYNNQAITDDNFEK-LRKHIGIVfqnPDN-QFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 360 QMSV---LHNITLPSVVMKLIVRKfglidsqlekeiVRSFIEKLNIKTPSPyqivENLSGGNQQKVVLAKWLAIKPKVLL 436
Cdd:PRK13648 102 KYDVafgLENHAVPYDEMHRRVSE------------ALKQVDMLERADYEP----NALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 437 LDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAmSDRILVMSEG 489
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-231 |
5.61e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 19 TKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYP--DYEGQIFLEGkevrfRNPREAQENGIALIPQEL 96
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANN-----RKPTKQILKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 97 DLVPNLSSAEN-IFLS--REPVNefgvIEYQKMFEQASKLFSKLGV-----NIDPKTKVEDLSTSQQQMVAIAKALSLDA 168
Cdd:PLN03211 150 ILYPHLTVRETlVFCSllRLPKS----LTKQEKILVAESVISELGLtkcenTIIGNSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 169 KIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHR-LEEIFEIADRVVVMRDGRKVGEG 231
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
267-490 |
7.86e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 267 RVEGIklwSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPG---RTEGKVFIGGKEIKIHSPRDavkn 343
Cdd:PRK10418 6 ELRNI---ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrQTAGRVLLDGKPVAPCALRG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 344 giglvpedrKTAGLILQ-----MSVLHNI------TLPSV-------VMKLIVRKFGLIDSQlekEIVRSFieklniktp 405
Cdd:PRK10418 79 ---------RKIATIMQnprsaFNPLHTMhthareTCLALgkpaddaTLTAALEAVGLENAA---RVLKLY--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 406 sPYQivenLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISE-MAVSGMGVVMVSSELPEILAMSDRIL 484
Cdd:PRK10418 138 -PFE----MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTHDMGVVARLADDVA 212
|
....*.
gi 490181991 485 VMSEGR 490
Cdd:PRK10418 213 VMSHGR 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
277-490 |
8.66e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 61.78 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGkeiKIHSPRDAvknGIGLVPEdrkta 355
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIyPP--DSGTVTVRG---RVSSLLGL---GGGFNPE----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 356 glilqMSVLHNITLPSVVMKLivrKFGLIDsQLEKEIVrSFIEKLN-IKTPspyqiVENLSGGNQQKVVLAKWLAIKPKV 434
Cdd:cd03220 99 -----LTGRENIYLNGRLLGL---SRKEID-EKIDEII-EFSELGDfIDLP-----VKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 435 LLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
280-490 |
9.12e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.10 E-value: 9.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRteGKVFIGGKEIKIHSPRDAVKNgIGLVPEDrktaGLIL 359
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ--GSLKINGIELRELDPESWRKH-LSWVGQN----PQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 360 QMSVLHNITLPSVVMKLIVrkfglIDSQLEKEIVRSFIEKLniktpsP----YQIVEN---LSGGNQQKVVLAKWLAIKP 432
Cdd:PRK11174 436 HGTLRDNVLLGNPDASDEQ-----LQQALENAWVSEFLPLL------PqgldTPIGDQaagLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 433 KVLLLDEPTRGIDvnAKSEiyKLISEM---AVSGMGVVMVSSELPEILAMsDRILVMSEGR 490
Cdd:PRK11174 505 QLLLLDEPTASLD--AHSE--QLVMQAlnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQ 560
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
12-219 |
9.66e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 9.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNIT------KTFpgviavNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQ 85
Cdd:PRK13538 1 MLEARNLAcerderILF------SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 86 E-------NGIAlipqeldlvPNLSSAENI-FLSR--EPVNEFGVIEY-QKM----FEQASklfsklgvnidpktkVEDL 150
Cdd:PRK13538 75 DllylghqPGIK---------TELTALENLrFYQRlhGPGDDEALWEAlAQVglagFEDVP---------------VRQL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 151 STSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRleEIFEIADRV 219
Cdd:PRK13538 131 SAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQ--DLPVASDKV 197
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
261-507 |
9.76e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.31 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 261 ITDEIFRVEGIKLWSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIfgahpGR----TEGKVFIGGKEIKIHS 336
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTL-----SRlmtpAHGHVWLDGEHIQHYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 337 PRDAVKNgIGLVPEDRKTAGLILQMSVLHNITLPSVVMKLIVRKfglidsqLEKEIVRSFIEKLNIkTPSPYQIVENLSG 416
Cdd:PRK10253 76 SKEVARR-IGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRK-------EDEEAVTKAMQATGI-THLADQSVDTLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 417 GNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAEF 495
Cdd:PRK10253 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
250
....*....|..
gi 490181991 496 LREEVTEEDLLK 507
Cdd:PRK10253 227 APKEIVTAELIE 238
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
278-490 |
1.05e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 278 RKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIfgahPGRTEGKVFIGgkeikihsprDAVKNGIGLVPEDRKTAGL 357
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL----AGRIQGNNFTG----------TILANNRKPTKQILKRTGF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQMSVL--HNITLPSVVMKLIVRKFGLIDSQLEKEIVRSFIEKLNIkTPSPYQIVEN-----LSGGNQQKVVLAKWLAI 430
Cdd:PLN03211 145 VTQDDILypHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGL-TKCENTIIGNsfirgISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 431 KPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVmVSSELP--EILAMSDRILVMSEGR 490
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIV-TSMHQPssRVYQMFDSVLVLSEGR 284
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
261-445 |
1.09e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 261 ITDEIFRVEGIKLWSLDRKKLLVDDVSFYvrKGEVLGIYGLVGAGRTELLEAIF---GAHPGRT-EGKVFIGGKEIkiHS 336
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFY--PNEITALIGPSGSGKSTLLRSINrmnDLNPEVTiTGSIVYNGHNI--YS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 337 PR-DAVkngiglvpEDRKTAGLILQ------MSVLHNitlpsVVMKLivRKFGLIDSQLEKEIVRSFIEKLNIKTPSPYQ 409
Cdd:PRK14239 77 PRtDTV--------DLRKEIGMVFQqpnpfpMSIYEN-----VVYGL--RLKGIKDKQVLDEAVEKSLKGASIWDEVKDR 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 490181991 410 IVEN---LSGGNQQKVVLAKWLAIKPKVLLLDEPTRGID 445
Cdd:PRK14239 142 LHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-226 |
1.25e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 23 PGVIAV-NNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVR---FRNPREAqengIALIPQEldl 98
Cdd:PLN03232 1246 PGLPPVlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfgLTDLRRV----LSIIPQS--- 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 99 vPNLSSAeNIFLSREPVNEFGVIEYQKMFEQA----SKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMD 174
Cdd:PLN03232 1319 -PVLFSG-TVRFNIDPFSEHNDADLWEALERAhikdVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 175 EPTSAIGKReTEQLfnIIRSLKNEGKS--VIYISHRLEEIFEiADRVVVMRDGR 226
Cdd:PLN03232 1397 EATASVDVR-TDSL--IQRTIREEFKSctMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-220 |
1.26e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIfleGKEVRFRnpreaqengIAL 91
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---KRNGKLR---------IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 92 IPQELDLVPNLSSAENIFLSREPVNEFGVIEYQKMFEQASKLFSKlgvnidPKTKvedLSTSQQQMVAIAKALSLDAKII 171
Cdd:PRK09544 72 VPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDA------PMQK---LSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490181991 172 IMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVV 220
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
277-508 |
1.27e-10 |
|
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: 61.48 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIfgahpGR----TEGKVFIGG---KEIKIHSPRdavkNGIGLVP 349
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI-----PRfydvDSGRILIDGhdvRDYTLASLR----RQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 350 EDRktagLILQMSVLHNITlpsvvmklivrkFGLIDSQLEkEIVR--------SFIEKLniktPSPYQIV-----ENLSG 416
Cdd:cd03251 83 QDV----FLFNDTVAENIA------------YGRPGATRE-EVEEaaraanahEFIMEL----PEGYDTVigergVKLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 417 GNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVmVSSELPEIlAMSDRILVMSEGRktaefL 496
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFV-IAHRLSTI-ENADRIVVLEDGK-----I 214
|
250
....*....|..
gi 490181991 497 REEVTEEDLLKA 508
Cdd:cd03251 215 VERGTHEELLAQ 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
29-221 |
1.35e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 29 NNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFrnpreaqengialiPQELDLVPNLSSAENi 108
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF--------------GREASLIDAIGRKGD- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 109 flsrepvnefgvieyqkmFEQASKLFSKLGVNiDP---KTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIgKRET 185
Cdd:COG2401 112 ------------------FKDAVELLNAVGLS-DAvlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL-DRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490181991 186 EQL--FNIIRSLKNEGKSVIYISHRlEEIFE--IADRVVV 221
Cdd:COG2401 172 AKRvaRNLQKLARRAGITLVVATHH-YDVIDdlQPDLLIF 210
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
279-495 |
1.58e-10 |
|
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: 60.33 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPGRTEGKVFIGGKEIKIHSPRdavknGIGLVPedrktagl 357
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrKTAGVITGEILINGRPLDKNFQR-----STGYVE-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ilQMSVLhnitLPSvvmkLIVRkfglidsqlekEIVRsFIEKLniktpspyqivENLSGGNQQKVVLAKWLAIKPKVLLL 437
Cdd:cd03232 86 --QQDVH----SPN----LTVR-----------EALR-FSALL-----------RGLSVEQRKRLTIGVELAAKPSILFL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 438 DEPTRGIDVNAKSEIYKLISEMAVSGMGVV-MVSSELPEILAMSDRILVMSEGRKTAEF 495
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLKRGGKTVYF 191
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
285-489 |
1.58e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKihsprdAVKNGIGLVPEdRKTAGLILQM-- 361
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGlLQP--TSGTVTIGERVIT------AGKKNKKLKPL-RKKVGIVFQFpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNITlpsvVMKLIV---RKFGLIDSQLEKEiVRSFIEKL----NIKTPSPYQivenLSGGNQQKVVLAKWLAIKPKV 434
Cdd:PRK13634 96 HQLFEET----VEKDICfgpMNFGVSEEDAKQK-AREMIELVglpeELLARSPFE----LSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 435 LLLDEPTRGIDVNAKSEI----YKLISEmavSGMGVVMVSSELPEILAMSDRILVMSEG 489
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMmemfYKLHKE---KGLTTVLVTHSMEDAARYADQIVVMHKG 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
259-458 |
1.61e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.59 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 259 ATITDEIFRVEGIKLWSldRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAH---PG-RTEGKVFIGGKEIki 334
Cdd:COG1117 5 ASTLEPKIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdliPGaRVEGEILLDGEDI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 335 HSPR-DavkngiglVPEDRKTAGLILQ------MSVLHNITLPsvvmkliVRKFGLIDSQLEKEIVRSFIEKLNI----- 402
Cdd:COG1117 81 YDPDvD--------VVELRRRVGMVFQkpnpfpKSIYDNVAYG-------LRLHGIKSKSELDEIVEESLRKAALwdevk 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 403 ---KTPspyqiVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISE 458
Cdd:COG1117 146 drlKKS-----ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
283-473 |
2.06e-10 |
|
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: 63.15 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRtEGKVFIGGkeIKIHS-PRDAVKNGIGLVPEDRKtaglILQM 361
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-QGEVTLDG--VPVSSlDQDEVRRRVSVCAQDAH----LFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNITL--PSVV---MKLIVRKFGLIDsqlekeIVRSFIEKLNIKtpspyqIVEN---LSGGNQQKVVLAKWLAIKPK 433
Cdd:TIGR02868 424 TVRENLRLarPDATdeeLWAALERVGLAD------WLRALPDGLDTV------LGEGgarLSGGERQRLALARALLADAP 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490181991 434 VLLLDEPTRGIDVNAKSEiykLISEM--AVSGMGVVMVSSEL 473
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADE---LLEDLlaALSGRTVVLITHHL 530
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
287-506 |
2.86e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 287 SFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEikiHSprdavkngigLVPEDRKTAGLILQ------ 360
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTP-ASGSLTLNGQD---HT----------TTPPSRRPVSMLFQennlfs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 -MSVLHNITL---PSV--------VMKLIVRKFGLIDsqlekeivrsFIEKLniktpsPYQivenLSGGNQQKVVLAKWL 428
Cdd:PRK10771 85 hLTVAQNIGLglnPGLklnaaqreKLHAIARQMGIED----------LLARL------PGQ----LSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 429 AIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGR-----KTAEFLREEVTE 502
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRiawdgPTDELLSGKASA 224
|
....
gi 490181991 503 EDLL 506
Cdd:PRK10771 225 SALL 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
285-494 |
2.89e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.60 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTELLEaIFGAHPGRTEGKVFIGGKEIKIHSP--RDAVKNgiglvpedrKTAGLILQMS 362
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTPTSGDVIFNGQPMSKLSSaaKAELRN---------QKLGFIYQFH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 -VLHNIT-LPSVVMKLIVrkfGLIDSQLEKEIVRSFIEKLNIKTPSPYQIVEnLSGGNQQKVVLAKWLAIKPKVLLLDEP 440
Cdd:PRK11629 97 hLLPDFTaLENVAMPLLI---GKKKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 441 TRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSdRILVMSEGRKTAE 494
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
280-495 |
3.45e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 60.65 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSPRDAVkngiglVPEDRktaGLI 358
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGfLAP--SSGEITLDGVPVTGPGADRGV------VFQKD---ALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQMSVLHNITLPsvvmkLIVRKFGLIDSQlekEIVRSFIEKLNIK---TPSPYQivenLSGGNQQKVVLAKWLAIKPKVL 435
Cdd:COG4525 89 PWLNVLDNVAFG-----LRLRGVPKAERR---ARAEELLALVGLAdfaRRRIWQ----LSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 436 LLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMS--EGRKTAEF 495
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVMSpgPGRIVERL 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
3.51e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 60.63 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKI---LAGVYPD--YEGQIFLEGKEVRFR--NPREAQ 85
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEarVEGEVRLFGRNIYSPdvDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 86 ENgIALIPQELDLVPNLSSAENIFLSrepVNEFGVIEYQKMFEQASK-LFSKLGVNIDPKTKVED----LSTSQQQMVAI 160
Cdd:PRK14267 85 RE-VGMVFQYPNPFPHLTIYDNVAIG---VKLNGLVKSKKELDERVEwALKKAALWDEVKDRLNDypsnLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490181991 161 AKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEgKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
282-503 |
4.42e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 60.24 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 282 LVDDVSFYVRKGEVLGIYGLVGAGRTELLEA----IFGAHPGRTEGKVFIGGKEIkiHSPR-DAVkngiglvpEDRKTAG 356
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlLELNEEARVEGEVRLFGRNI--YSPDvDPI--------EVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQ-------MSVLHNITLpSVVMKLIVRKFGLIDSQLEKEIVRSFI-----EKLNIKtPSpyqiveNLSGGNQQKVVL 424
Cdd:PRK14267 89 MVFQypnpfphLTIYDNVAI-GVKLNGLVKSKKELDERVEWALKKAALwdevkDRLNDY-PS------NLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 425 AKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPEILAMSDRILVMSEG--------RKTAEFL 496
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK-KEYTIVLVTHSPAQAARVSDYVAFLYLGklievgptRKVFENP 239
|
....*..
gi 490181991 497 REEVTEE 503
Cdd:PRK14267 240 EHELTEK 246
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2-235 |
4.46e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.60 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 2 MLNTEKER-EVLLEARNITKTFpgvIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKevrfrn 80
Cdd:PRK13546 16 IYRTNKERmKDALIPKHKNKTF---FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 81 preaqengIALIPQELDLVPNLSSAENIflsrepvnEFGVI-------EYQKMFEQASKlFSKLGVNIdpKTKVEDLSTS 153
Cdd:PRK13546 87 --------VSVIAISAGLSGQLTGIENI--------EFKMLcmgfkrkEIKAMTPKIIE-FSELGEFI--YQPVKKYSSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 154 QQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPI 233
Cdd:PRK13546 148 MRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
..
gi 490181991 234 EE 235
Cdd:PRK13546 228 DD 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-228 |
4.94e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.20 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNIT----KTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDY---EGQIF---LEGKEVRFR 79
Cdd:cd03233 1 ASTLSWRNISfttgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHyngIPYKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 80 NPREaqengIALIPQELDLVPNLSSAENI-FLSREPVNEFgvieyqkmfeqasklfsklgvnidpktkVEDLSTSQQQMV 158
Cdd:cd03233 81 YPGE-----IIYVSEEDVHFPTLTVRETLdFALRCKGNEF----------------------------VRGISGGERKRV 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 159 AIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYIS--HRLEEIFEIADRVVVMRDGRKV 228
Cdd:cd03233 128 SIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyQASDEIYDLFDKVLVLYEGRQI 199
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
389-503 |
5.19e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.41 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 389 EKEIVRSFIEKLNIKTPSPY--QIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGV 466
Cdd:PRK13638 110 EAEITRRVDEALTLVDAQHFrhQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHV 189
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490181991 467 VMVSSELPEILAMSDRILVMSEGRKTAE------FLREEVTEE 503
Cdd:PRK13638 190 IISSHDIDLIYEISDAVYVLRQGQILTHgapgevFACTEAMEQ 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
414-490 |
6.01e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.08 E-value: 6.01e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 414 LSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
279-448 |
6.39e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 61.62 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGgKEIKI------------HSPRDAVKNGi 345
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGeLEP--DSGEVSIP-KGLRIgylpqeppldddLTVLDTVLDG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 346 glvpeDRKTAGLILQMS-VLHNITLPSVVMKLIVRKFGLIDS----QLEKEIvRSFIEKLNIKTPSPYQIVENLSGGNQQ 420
Cdd:COG0488 86 -----DAELRALEAELEeLEAKLAEPDEDLERLAELQEEFEAlggwEAEARA-EEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180
....*....|....*....|....*...
gi 490181991 421 KVVLAKWLAIKPKVLLLDEPTRGIDVNA 448
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
283-490 |
6.83e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.02 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTeGKVFIGGKEIkihsPRDAVKngIGLVPEDRKTAGLILQMS 362
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISET-GQTIVGDYAI----PANLKK--IKEVKRLRKEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHniTLPSVVMKLIVrkFGLIDSQLEKEIVRSFIEKLNIKTPSPYQIVE----NLSGGNQQKVVLAKWLAIKPKVLLLD 438
Cdd:PRK13645 100 EYQ--LFQETIEKDIA--FGPVNLGENKQEAYKKVPELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490181991 439 EPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGK 228
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-238 |
7.80e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.79 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 16 RNITKTF-PGVIAvnnvtlqiykgevcALVGENGAGKSTLMKILAGvypdYEGQIFLEGkEVRFRNPREAQEN--GIALI 92
Cdd:PLN03140 897 REVTGAFrPGVLT--------------ALMGVSGAGKTTLMDVLAG----RKTGGYIEG-DIRISGFPKKQETfaRISGY 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDL-VPNLSSAENIFLS---REPVNefgVIEYQKM--FEQASKL--FSKLGVNIDPKTKVEDLSTSQQQMVAIAKAL 164
Cdd:PLN03140 958 CEQNDIhSPQVTVRESLIYSaflRLPKE---VSKEEKMmfVDEVMELveLDNLKDAIVGLPGVTGLSTEQRKRLTIAVEL 1034
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 165 SLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLE-EIFEIADRVVVM-RDGRKVGEGPIEEFDH 238
Cdd:PLN03140 1035 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMkRGGQVIYSGPLGRNSH 1110
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-243 |
8.77e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEV------RFRNPREAq 85
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrsRLYTVRKR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 86 engIALIPQELDLVPNLSSAENIflsrepvnEFGVIEYQKMFEQA--SKLFSKL---GVNIDPKTKVEDLSTSQQQMVAI 160
Cdd:PRK11831 86 ---MSMLFQSGALFTDMNVFDNV--------AYPLREHTQLPAPLlhSTVMMKLeavGLRGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 161 AKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNE-GKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEFDH- 238
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAn 234
|
....*.
gi 490181991 239 -DKLVR 243
Cdd:PRK11831 235 pDPRVR 240
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
255-511 |
9.79e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.42 E-value: 9.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 255 IKERATITDEIFRVEGIKLWSLDRkkLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEaIFGAHPGRTEGKVFIGGKEIKI 334
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGR--TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSEGEILLDAQPLES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 335 HSPRDAVkngiglvpedRKTAGLILQMSVLHNITLPSVVMklIVR--------KFGLIDsqleKEIVRSFIEKLNIKtPS 406
Cdd:PRK10575 78 WSSKAFA----------RKVAYLPQQLPAAEGMTVRELVA--IGRypwhgalgRFGAAD----REKVEEAISLVGLK-PL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 407 PYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMA-VSGMGVVMVSSELPEILAMSDRILV 485
Cdd:PRK10575 141 AHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVA 220
|
250 260
....*....|....*....|....*...
gi 490181991 486 MSEGRKTAEFLREEVTEEDLLKA--AIP 511
Cdd:PRK10575 221 LRGGEMIAQGTPAELMRGETLEQiyGIP 248
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
283-490 |
1.15e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.81 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIHSPRdavkngiGLVPEDRKTaGLILQ- 360
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLlERP--TSGRVLVDGQDLTALSEK-------ELRKARRQI-GMIFQh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 ------MSVLHNITLPsvvMKLIVRKFGLIDSQLEKEIVRSFIEKLNIKTPSpyqiveNLSGGNQQKVVLAKWLAIKPKV 434
Cdd:PRK11153 91 fnllssRTVFDNVALP---LELAGTPKAEIKARVTELLELVGLSDKADRYPA------QLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 435 LLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
31-237 |
1.29e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 31 VTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRNPREAQENgIALIPQeldlVPNLSSAeNIFL 110
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV-LGIIPQ----APVLFSG-TVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 111 SREPVNEFGVIEYQKMFEQA----SKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKReTE 186
Cdd:PLN03130 1332 NLDPFNEHNDADLWESLERAhlkdVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR-TD 1410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490181991 187 QLfnIIRSLKNEGKS--VIYISHRLEEIFEiADRVVVMRDGRKVgegpieEFD 237
Cdd:PLN03130 1411 AL--IQKTIREEFKSctMLIIAHRLNTIID-CDRILVLDAGRVV------EFD 1454
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
274-494 |
3.51e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 274 WSLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEaIFGAHPGRTEGKVFIGGKEIKIHSPRdavkngiglvpEDRK 353
Cdd:PRK10247 15 YLAGDAKIL-NNISFSLRAGEFKLITGPSGCGKSTLLK-IVASLISPTSGTLLFEGEDISTLKPE-----------IYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 354 TAGLILQM------SVLHNITLP------SVVMKLIVR---KFGLIDSQLEKEIvrsfieklniktpspyqivENLSGGN 418
Cdd:PRK10247 82 QVSYCAQTptlfgdTVYDNLIFPwqirnqQPDPAIFLDdleRFALPDTILTKNI-------------------AELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 419 QQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEINHADKVITLQPHAGEMQE 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-447 |
3.56e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 16 RNITKTFPG--VIaVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFL-EGKEVrfrnpreaqenGIalI 92
Cdd:PRK11819 10 NRVSKVVPPkkQI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKV-----------GY--L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQELDLVPNLSSAENIFLS----REPVNEFGVI---------EYQKMFEQASKLFSKL----GVNIDPK----------- 144
Cdd:PRK11819 76 PQEPQLDPEKTVRENVEEGvaevKAALDRFNEIyaayaepdaDFDALAAEQGELQEIIdaadAWDLDSQleiamdalrcp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 145 ---TKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTS---AigkrET----EQLfniirsLKNEGKSVIYISH-RL---- 209
Cdd:PRK11819 156 pwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNhldA----ESvawlEQF------LHDYPGTVVAVTHdRYfldn 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 210 --EEIFEIaDRvvvmrdgrkvGEG-P-----------------IEEFDHDKLVRLMV-----------GR---------- 248
Cdd:PRK11819 226 vaGWILEL-DR----------GRGiPwegnysswleqkakrlaQEEKQEAARQKALKrelewvrqspkARqakskarlar 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 249 -----SIDQffikERATITDEIF------------RVEGIklwsldRK----KLLVDDVSFYVRKGEVLGIYGLVGAGRT 307
Cdd:PRK11819 295 yeellSEEY----QKRNETNEIFippgprlgdkviEAENL------SKsfgdRLLIDDLSFSLPPGGIVGIIGPNGAGKS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 308 ELLEAIFGAHPgRTEGKVFIGgkeikihsprDAVKngIGLVPEDR------KTA------GL-ILQmsvLHNITLPSvvm 374
Cdd:PRK11819 365 TLFKMITGQEQ-PDSGTIKIG----------ETVK--LAYVDQSRdaldpnKTVweeisgGLdIIK---VGNREIPS--- 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 375 klivrkfglidsqlekeivRSFIEKLNIKTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVN 447
Cdd:PRK11819 426 -------------------RAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
280-502 |
3.99e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.05 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGR-TEGKV-----------------FIGGK----------- 330
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEpTSGRIiyhvalcekcgyverpsKVGEPcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 331 EIKIHSPRDAVKNGIglvpedRKTAGLILQMS--------VLHNI--TLPSV---VMKLIVRKFGLID-SQLEKEIVrsf 396
Cdd:TIGR03269 93 EVDFWNLSDKLRRRI------RKRIAIMLQRTfalygddtVLDNVleALEEIgyeGKEAVGRAVDLIEmVQLSHRIT--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 397 ieklniktpspyQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEmAVSGMGVVMV-SSELPE 475
Cdd:TIGR03269 164 ------------HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEE-AVKASGISMVlTSHWPE 230
|
250 260
....*....|....*....|....*...
gi 490181991 476 ILA-MSDRILVMSEGRKTAEFLREEVTE 502
Cdd:TIGR03269 231 VIEdLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
108-310 |
4.15e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 59.46 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 108 IFLSREPVNEFGVIEYQKMFEQASKLFSKLGVN-IDPKTKVEDLSTSQQQMVAIAKAL--SLDAKIIIMDEPTSAIGKRE 184
Cdd:PRK00635 434 IFLSQLPSKSLSIEEVLQGLKSRLSILIDLGLPyLTPERALATLSGGEQERTALAKHLgaELIGITYILDEPSIGLHPQD 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 185 TEQLFNIIRSLKNEGKSVIYISHRlEEIFEIADRVVVMRDGRKV--GE----GPIEEFdhdklvrLMVGRSIDQFFIKER 258
Cdd:PRK00635 514 THKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIIDIGPGAGIfgGEvlfnGSPREF-------LAKSDSLTAKYLRQE 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490181991 259 ATITDEIFRVEGIKLWSLDR-KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELL 310
Cdd:PRK00635 586 LTIPIPEKRTNSLGTLTLSKaTKHNLKDLTISLPLGRLTVVTGVSGSGKSSLI 638
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
281-489 |
4.42e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.51 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 281 LLVDDVSFYVRKGEVLGIYGLVGAGRTELLEaIFGAHPGRTEGKVFIGGKEIKIHSP---RDAVKNGIGLVpedRKTAGL 357
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVR-LLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKIAMV---FQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQMSVLHNITlpsvvmklivrkFGL----IDSQLEKEIVRSFIEKLNIKTPSpYQIVENLSGGNQQKVVLAKWLAIKPK 433
Cdd:PRK10070 118 MPHMTVLDNTA------------FGMelagINAEERREKALDALRQVGLENYA-HSYPDELSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 434 VLLLDEPTRGIDVNAKSEIY-KLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEG 489
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
284-490 |
4.49e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 284 DDVSFYVRKGEVLGIYGLVGAGRTELLEaIFGAHPGRTEGKVFIGGKEIkihsprdAVKNGIGLVPEDRKTAGLILQ--- 360
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKPTSGTYRVAGQDV-------ATLDADALAQLRREHFGFIFQryh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 ----MSVLHNITLPSVvmklivrkFGLIDSQLEKEIVRSFIEKLNIKTPSPYQIVEnLSGGNQQKVVLAKWLAIKPKVLL 436
Cdd:PRK10535 97 llshLTAAQNVEVPAV--------YAGLERKQRLLRAQELLQRLGLEDRVEYQPSQ-LSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 437 LDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSElPEILAMSDRILVMSEGR 490
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGE 220
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-230 |
4.65e-09 |
|
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: 55.79 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 21 TFPGVIA--VNNVTLQIYKGEVCALVGENGAGKSTLMKilagvypdyegQIFLEGKEVRFrnpreaqengialipqeLDL 98
Cdd:cd03238 2 TVSGANVhnLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLYASGKARL-----------------ISF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 99 VPNLSSAENIFLSRepvnefgvieyqkmfeqaSKLFSKLGVN-IDPKTKVEDLSTSQQQMVAIAKALSLDAK--IIIMDE 175
Cdd:cd03238 54 LPKFSRNKLIFIDQ------------------LQFLIDVGLGyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 176 PTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRlEEIFEIADRVVVM--RDGRKVGE 230
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWIIDFgpGSGKSGGK 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
407-490 |
5.77e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 407 PYQivenLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILV 485
Cdd:PRK15134 154 PHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAV 229
|
....*
gi 490181991 486 MSEGR 490
Cdd:PRK15134 230 MQNGR 234
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-212 |
5.89e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.36 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 27 AVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEvrfrnpreaqengiALIPQELDLVPNLSSAE 106
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA--------------ALIAISSGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 107 NIFL-------SREPVNEF--GVIEyqkmfeqasklFSKLGVNIDPKTKVedLSTSQQQMVAIAKALSLDAKIIIMDEPT 177
Cdd:PRK13545 105 NIELkglmmglTKEKIKEIipEIIE-----------FADIGKFIYQPVKT--YSSGMKSRLGFAISVHINPDILVIDEAL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 490181991 178 SAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEI 212
Cdd:PRK13545 172 SVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-212 |
1.01e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 9 REVLLEARNITKTFPGV--IAVNNV--------TLQIYK--------GEVCALVGENGAGKSTLMKILAGVYPDYEGQIF 70
Cdd:PTZ00265 364 RKPLVENNDDGKKLKDIkkIQFKNVrfhydtrkDVEIYKdlnftlteGKTYAFVGESGCGKSTILKLIERLYDPTEGDII 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 71 LEG----KEVRFRNPREAqengIALIPQELDLVPN---------LSSAENIFLSREPVNEFGVIEYQKMFEQASKLFSKL 137
Cdd:PTZ00265 444 INDshnlKDINLKWWRSK----IGVVSQDPLLFSNsiknnikysLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCA 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 138 G-----------------------------VNIDPKTKVED-------------------LSTSQQQMVAIAKALSLDAK 169
Cdd:PTZ00265 520 GdlndmsnttdsneliemrknyqtikdsevVDVSKKVLIHDfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPK 599
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490181991 170 IIIMDEPTSAIGKRETEQLFNIIRSLK-NEGKSVIYISHRLEEI 212
Cdd:PTZ00265 600 ILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTI 643
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
283-490 |
1.04e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTEL---LEAIfgAHPgrTEGKVFIGGKEIKIHsPRDAVKN---GIGLVPED----- 351
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarlLTMI--ETP--TGGELYYQGQDLLKA-DPEAQKLlrqKIQIVFQNpygsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 352 --RKTAGLILQMSVLHNITLpsvvmklivrkfgliDSQLEKEIVRSFIEKLNIKtPSPYQIVENL-SGGNQQKVVLAKWL 428
Cdd:PRK11308 106 npRKKVGQILEEPLLINTSL---------------SAAERREKALAMMAKVGLR-PEHYDRYPHMfSGGQRQRIAIARAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 429 AIKPKVLLLDEPTRGIDVNAKSEIYKLI----SEMavsGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQVLNLMmdlqQEL---GLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
282-490 |
1.22e-08 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 57.83 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 282 LVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTeGKVFIGGKEIKIHSpRDAVKNGIGLVPEDRktagLILQM 361
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS-GEILLNGFSLKDID-RHTLRQFINYLPQEP----YIFSG 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNITL---PSVVMKLIVRKFGLIDsqlekeiVRSFIEKLniktPSPYQI-----VENLSGGNQQKVVLAKWLAIKPK 433
Cdd:TIGR01193 563 SILENLLLgakENVSQDEIWAACEIAE-------IKDDIENM----PLGYQTelseeGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 434 VLLLDEPTRGIDVNAKSEIYKLIseMAVSGMGVVMVSSELpEILAMSDRILVMSEGR 490
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGK 685
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
12-231 |
1.47e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGvYPDYE---GQIFLEGKEVRFRNPREAQENG 88
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG-REDYEvtgGTVEFKGKDLLELSPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALI---PQELDLVPN---LSSAENI---FLSREPVNEFgviEYQKMFEQASKLFsKLGVNIDPKTKVEDLSTSQQQMVA 159
Cdd:PRK09580 80 IFMAfqyPVEIPGVSNqffLQTALNAvrsYRGQEPLDRF---DFQDLMEEKIALL-KMPEDLLTRSVNVGFSGGEKKRND 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 160 IAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHrLEEIFEI--ADRVVVMRDGRKVGEG 231
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
281-490 |
1.93e-08 |
|
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: 54.78 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 281 LLVDDVSFYVRKGEVLGIYGLVGAGRT---ELLEAIFGAhpgrTEGKVFIGGKEIKIHSPRdAVKNGIGLVPEDRktagL 357
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKStvvALLENFYQP----QGGQVLLDGKPISQYEHK-YLHSKVSLVGQEP----V 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQMSVLHNIT--LPSVvmklivrKFGLIDSQLEKEIVRSFIEKLniktPSPYQIV-----ENLSGGNQQKVVLAKWLAI 430
Cdd:cd03248 99 LFARSLQDNIAygLQSC-------SFECVKEAAQKAHAHSFISEL----ASGYDTEvgekgSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 431 KPKVLLLDEPTRGIDVNAKSEIYKLISEmAVSGMGVVMVSSELPEIlAMSDRILVMSEGR 490
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
282-490 |
2.01e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.30 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 282 LVDDVSFYVRKGEVLGIYGLVGAGRTELLEA---IFGAHP-GRTEGKVFIGGKEI-KIHsprdavkngiglVPEDRKTAG 356
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPeARVSGEVYLDGQDIfKMD------------VIELRRRVQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQ-------MSVLHNITLPSVVMKLIVRKFGLidsqleKEIVRSFIEKLNIktpspYQIVEN--------LSGGNQQK 421
Cdd:PRK14247 86 MVFQipnpipnLSIFENVALGLKLNRLVKSKKEL------QERVRWALEKAQL-----WDEVKDrldapagkLSGGQQQR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 422 VVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQ 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-244 |
2.51e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.48 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 10 EVLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLeGKEVRfrnpreaqengI 89
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 90 ALIPQELD-LVPNLSSAENI-------------FLSREPVNEFGvieyqkmFEQAsklfsklgvniDPKTKVEDLSTSQQ 155
Cdd:TIGR03719 388 AYVDQSRDaLDPNKTVWEEIsggldiiklgkreIPSRAYVGRFN-------FKGS-----------DQQKKVGQLSGGER 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 156 QMVAIAKALSLDAKIIIMDEPTSAIgkrETEQLFNIIRSLKNEGKSVIYISHR---LEEI------FEIADRVVVMrdgr 226
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDL---DVETLRALEEALLNFAGCAVVISHDrwfLDRIathilaFEGDSHVEWF---- 522
|
250
....*....|....*...
gi 490181991 227 kvgEGPIEEFDHDKLVRL 244
Cdd:TIGR03719 523 ---EGNFSEYEEDKKRRL 537
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
295-513 |
3.08e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.65 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 295 VLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGK-----EIKIHSPRDavKNGIGLVPEDrktAGLILQMSVLHNIt 368
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGlTRP--QKGRIVLNGRvlfdaEKGICLPPE--KRRIGYVFQD---ARLFPHYKVRGNL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 369 lpsvvmklivrKFGLIDSQLEK--EIVRSF-IEKLNIKTPSpyqiveNLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGID 445
Cdd:PRK11144 98 -----------RYGMAKSMVAQfdKIVALLgIEPLLDRYPG------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 446 VNAKSEIYKLISEMAVS-GMGVVMVSSELPEILAMSDRILVMSEGRKTAEFLREEVTEEDLLKAAIPRS 513
Cdd:PRK11144 161 LPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKE 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
283-490 |
3.24e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.70 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGA-HPgrTEGKVFIGGkeiKIHSPrdavkngIGLvpedrkTAGLILQM 361
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIlEP--TSGRVEVNG---RVSAL-------LEL------GAGFHPEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNITLPSVVMKLIVRKfglIDsQLEKEIVrSF--IEKLnIKTPspyqiVENLSGGNQQKVVLAKWLAIKPKVLLLDE 439
Cdd:COG1134 104 TGRENIYLNGRLLGLSRKE---ID-EKFDEIV-EFaeLGDF-IDQP-----VKTYSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 440 ptrGIDV-----NAKSeiYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:COG1134 173 ---VLAVgdaafQKKC--LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
285-489 |
4.35e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.50 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAhpgrtegkVFIGGKEIKI--HSPRDAVK-NGIGLVPEDRKTAgliLQM 361
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGF--------VRLASGKISIlgQPTRQALQkNLVAYVPQSEEVD---WSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLhnitLPSVVMKLIVRKFGL--IDSQLEKEIVRSFIEKLNIKTPSPYQIVEnLSGGNQQKVVLAKWLAIKPKVLLLDE 439
Cdd:PRK15056 94 PVL----VEDVVMMGRYGHMGWlrRAKKRDRQIVTAALARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490181991 440 PTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRIlVMSEG 489
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKG 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
275-490 |
4.48e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 53.92 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 275 SLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGaHPG--RTEGKVFIGGKEIKihsprdavkngiGLVPEDR 352
Cdd:COG0396 9 SVEGKEIL-KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPKyeVTSGSILLDGEDIL------------ELSPDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 353 KTAGLILQMSvlHNITLPSV-VMKLI------VRKFGLIDSQLEKEIV---------RSFIEK-LNiktpspyqivENLS 415
Cdd:COG0396 75 ARAGIFLAFQ--YPVEIPGVsVSNFLrtalnaRRGEELSAREFLKLLKekmkelgldEDFLDRyVN----------EGFS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 416 GGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVsSELPEILAM--SDRILVMSEGR 490
Cdd:COG0396 143 GGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILII-THYQRILDYikPDFVHVLVDGR 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
286-506 |
4.67e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 286 VSFYVRKGEVLGIYGLVGAGRTELLEAIFgahpgRT----EGKVFIGGKeikihsprDAVKNGIGLVpedRKTAGLILQM 361
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALF-----RIveleKGRIMIDDC--------DVAKFGLTDL---RRVLSIIPQS 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNITLpsvvmklivrKFGLI------DSQLEKEIVRSFIEKLNIKTP-----SPYQIVENLSGGNQQKVVLAKWLAI 430
Cdd:PLN03232 1319 PVLFSGTV----------RFNIDpfsehnDADLWEALERAHIKDVIDRNPfgldaEVSEGGENFSVGQRQLLSLARALLR 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 431 KPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSgMGVVMVSSELPEILAmSDRILVMSEGRktaefLREEVTEEDLL 506
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIID-CDKILVLSSGQ-----VLEYDSPQELL 1457
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-267 |
5.51e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.69 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 30 NVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKevrfrnpreaqengIALIPQELDLVPNLSSAENIF 109
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPGTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 110 -LSREPVNEFGVIEYQKMFEQASKLFSKlgvnidPKTKVED----LSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRE 184
Cdd:TIGR01271 510 gLSYDEYRYTSVIKACQLEEDIALFPEK------DKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 185 TEQLFN--IIRSLKNegKSVIYISHRLEEIfEIADRVVVMRDGRKVGEGPIEEFDH---DKLVRLMVGRSIDQFFIKERA 259
Cdd:TIGR01271 584 EKEIFEscLCKLMSN--KTRILVTSKLEHL-KKADKILLLHEGVCYFYGTFSELQAkrpDFSSLLLGLEAFDNFSAERRN 660
|
....*...
gi 490181991 260 TITDEIFR 267
Cdd:TIGR01271 661 SILTETLR 668
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
280-522 |
6.06e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.92 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKI--HSPRDAVKNGIGLVPED----- 351
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESP--SQGNVSWRGEPLAKlnRAQRKAFRRDIQMVFQDsisav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 352 --RKTAGLILQMSVLHNITLP----SVVMKLIVRKFGLIDSQLEKEivrsfieklniktpsPYQivenLSGGNQQKVVLA 425
Cdd:PRK10419 103 npRKTVREIIREPLRHLLSLDkaerLARASEMLRAVDLDDSVLDKR---------------PPQ----LSGGQLQRVCLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 426 KWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEG-----RKTAEFLREE 499
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGqivetQPVGDKLTFS 243
|
250 260
....*....|....*....|....*
gi 490181991 500 VTEEDLLKAAI--PRSVKVETTQRE 522
Cdd:PRK10419 244 SPAGRVLQNAVlpAFPVRRRTTEKV 268
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
257-504 |
7.22e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.34 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 257 ERATITD----EIFRVEGIKLWSLDRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVfiggkei 332
Cdd:TIGR00957 625 ERRTIKPgegnSITVHNATFTWARDLPPTL-NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD-KVEGHV------- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 333 kihsprdAVKNGIGLVPedrktaglilQMSVLHNITLPSVVMklivrkFGlidSQLEKEIVRSFIE------KLNIkTPS 406
Cdd:TIGR00957 696 -------HMKGSVAYVP----------QQAWIQNDSLRENIL------FG---KALNEKYYQQVLEacallpDLEI-LPS 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 407 PYQ--IVE---NLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDvnakSEIYKLISEMAVSGMGV------VMVS---SE 472
Cdd:TIGR00957 749 GDRteIGEkgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD----AHVGKHIFEHVIGPEGVlknktrILVThgiSY 824
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490181991 473 LPEIlamsDRILVMSEGRKT---------------AEFLREEVTEED 504
Cdd:TIGR00957 825 LPQV----DVIIVMSGGKISemgsyqellqrdgafAEFLRTYAPDEQ 867
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-226 |
8.08e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIflegkevrfrnpREAQENGIALI 92
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 93 PQelDLVPNLSSAENIF--LS--REPVNEfgvieyqkmfEQASK------LFSklgvNIDPKTKVEDLSTSQQQMVAIAK 162
Cdd:PRK15064 388 AQ--DHAYDFENDLTLFdwMSqwRQEGDD----------EQAVRgtlgrlLFS----QDDIKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 163 ALSLDAKIIIMDEPTSAIGKRETEQLFNiirSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGR 226
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESIESLNM---ALEKYEGTLIFVSHDREFVSSLATRIIEITPDG 512
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
285-490 |
9.03e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.27 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRdavKNGIGLVpedRKTAGLILQMSVL 364
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED-ITSGDLFIGEKRMNDVPPA---ERGVGMV---FQSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 365 HNItlpSVVMKLIVRKFGLIDSQLEK--EIVRsfIEKLNIKTPspyqivENLSGGNQQKVVLAKWLAIKPKVLLLDEPTR 442
Cdd:PRK11000 94 ENM---SFGLKLAGAKKEEINQRVNQvaEVLQ--LAHLLDRKP------KALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490181991 443 GID----VNAKSEIYKLISEMavsGMGVVMVSSELPEILAMSDRILVMSEGR 490
Cdd:PRK11000 163 NLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
262-459 |
1.08e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 53.25 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 262 TDEIFRVEGIKLWSldRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELL-------EAIFGAhpgRTEGKVFIGGKEIki 334
Cdd:PRK14243 7 TETVLRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGF---RVEGKVTFHGKNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 335 HSPR-DAVkngiglvpEDRKTAGLILQM------SVLHNITLPSVV--MKlivrkfGLIDSQLEKEIVRSFI-----EKL 400
Cdd:PRK14243 80 YAPDvDPV--------EVRRRIGMVFQKpnpfpkSIYDNIAYGARIngYK------GDMDELVERSLRQAALwdevkDKL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 401 NIKTPSpyqivenLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM 459
Cdd:PRK14243 146 KQSGLS-------LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL 197
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
390-508 |
1.32e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.65 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 390 KEIVRSFieklniktpsPYQIVEnlsgGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVM 468
Cdd:PRK15093 149 KDAMRSF----------PYELTE----GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILL 214
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 490181991 469 VSSELPEILAMSDRILVMSEGRKTaeflrEEVTEEDLLKA 508
Cdd:PRK15093 215 ISHDLQMLSQWADKINVLYCGQTV-----ETAPSKELVTT 249
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
283-494 |
1.41e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.59 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAG--RTELLEAIFGAHPGRTEGKVFIGGkeikihSPRDAVKNGIGLVPEDRKtaGLILQ 360
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWC------ANRRALRRTIG*HRPVR*--GRRES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 MSVLHNITLPSVVMKLiVRKfgliDSQLEKEivrSFIEKLNIkTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEP 440
Cdd:NF000106 101 FSGRENLYMIGR*LDL-SRK----DARARAD---ELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 441 TRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTAE 494
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-236 |
2.11e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDyegqifLEGKEVRFRNpreaqenGIALIPQeLDLVPNLSSAEN 107
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH------AETSSVVIRG-------SVAYVPQ-VSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 108 IFLSR--EPVNEFGVIEYQKMfEQASKLFS--------KLGVNIdpktkvedlSTSQQQMVAIAKALSLDAKIIIMDEPT 177
Cdd:PLN03232 699 ILFGSdfESERYWRAIDVTAL-QHDLDLLPgrdlteigERGVNI---------SGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 178 SAIGKRETEQLFNIIRSLKNEGKSVIYISHRLeEIFEIADRVVVMRDGRKVGEGPIEEF 236
Cdd:PLN03232 769 SALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
265-489 |
2.13e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.32 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 265 IFRVEgiKLWSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPG--RTEGKVFIGGKEIKIHS--PRDA 340
Cdd:PRK09984 4 IIRVE--KLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGdkSAGSHIELLGRTVQREGrlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 341 VKNgiglvpedRKTAGLILQ-------MSVLHNITLPSV----VMKLIVRKFglidSQLEKEIVRSFIEKLNIKTPSpYQ 409
Cdd:PRK09984 82 RKS--------RANTGYIFQqfnlvnrLSVLENVLIGALgstpFWRTCFSWF----TREQKQRALQALTRVGMVHFA-HQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 410 IVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSE 488
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
.
gi 490181991 489 G 489
Cdd:PRK09984 229 G 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
282-468 |
2.34e-07 |
|
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: 51.34 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 282 LVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKeiKIHSPRDAVKNGIGLVPEdrkTAGLILQM 361
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP-PLAGRVLLNGG--PLDFQRDSIARGLLYLGH---APGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 362 SVLHNITLpsvvmkliVRKFGlIDSQLEKEIVRSFIEKLNiktpspYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPT 441
Cdd:cd03231 89 SVLENLRF--------WHADH-SDEQVEEALARVGLNGFE------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180
....*....|....*....|....*..
gi 490181991 442 RGIDVNAKSEIYKLISEMAVSGMGVVM 468
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVL 180
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
13-236 |
2.39e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.82 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 13 LEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTlmkilaGVYPDYEGQIFLEGKEVRFR----NPREAQENG 88
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAHV*GPDAGRRPWRF*twcaNRRALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 89 IALIPQELDLVPNLSSAENIFLSREPVNefgvIEYQKMFEQASKLFSKLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDA 168
Cdd:NF000106 88 G*HRPVR*GRRESFSGRENLYMIGR*LD----LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 169 KIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIFEIADRVVVMRDGRKVGEGPIEEF 236
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
286-506 |
2.40e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 286 VSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPGRteGKVFIGGKEIKIHSPRDAvkngiglvpedRKTAGLILQMSVL 364
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRiVELER--GRILIDGCDISKFGLMDL-----------RKVLGIIPQAPVL 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 365 HNITLpsvvmklivrKFGL----------IDSQLE----KEIVRSFIEKLNIKTpspYQIVENLSGGNQQKVVLAKWLAI 430
Cdd:PLN03130 1325 FSGTV----------RFNLdpfnehndadLWESLErahlKDVIRRNSLGLDAEV---SEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 431 KPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSgMGVVMVSSELPEILAmSDRILVMSEGRktaefLREEVTEEDLL 506
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKS-CTMLIIAHRLNTIID-CDRILVLDAGR-----VVEFDTPENLL 1460
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
38-235 |
2.47e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 38 GEVCALVGENGAGKSTLMKILAGVYPDY----EGQIFLEG---KEVRFRNPREAQENGialipqELDL-VPNLSSAENIF 109
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGitpEEIKKHYRGDVVYNA------ETDVhFPHLTVGETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 110 LS---REPVNEF-GVIEYQKMFEQASKLFSKLGVNIDPKTKVED-----LSTSQQQMVAIAKALSLDAKIIIMDEPTSAI 180
Cdd:TIGR00956 161 FAarcKTPQNRPdGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 181 GKRETEQLFNIIRSLKNEGKSVIYIS--HRLEEIFEIADRVVVMRDGRKVGEGPIEE 235
Cdd:TIGR00956 241 DSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGPADK 297
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-267 |
2.66e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.17 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 30 NVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKevrfrnpreaqengIALIPQELDLVPNlSSAENIF 109
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 110 --LSREPVNEFGVIEYQKMFEQASKLFSKlgvniDPKTKVE---DLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRE 184
Cdd:cd03291 120 fgVSYDEYRYKSVVKACQLEEDITKFPEK-----DNTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 185 TEQLFNIIRSLKNEGKSVIYISHRLEEIfEIADRVVVMRDGRKVGEGPIEEFDH---DKLVRLMVGRSIDQFFIKERATI 261
Cdd:cd03291 195 EKEIFESCVCKLMANKTRILVTSKMEHL-KKADKILILHEGSSYFYGTFSELQSlrpDFSSKLMGYDTFDQFSAERRNSI 273
|
....*.
gi 490181991 262 TDEIFR 267
Cdd:cd03291 274 LTETLR 279
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
414-506 |
3.08e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 52.91 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 414 LSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPEILAMsDRILVMSEGRkta 493
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQ--- 550
|
90
....*....|...
gi 490181991 494 efLREEVTEEDLL 506
Cdd:PRK11160 551 --IIEQGTHQELL 561
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
412-487 |
3.16e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 50.23 E-value: 3.16e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 412 ENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMavsGMGVVMVSSElPEILAMSDRILVMS 487
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHR-PSLWKFHDRVLDLD 161
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
283-508 |
3.37e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.80 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGE-VL----------GIYGLVG---AGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRdAVKNGIGLV 348
Cdd:PRK10790 343 IDNVSFAYRDDNlVLqninlsvpsrGFVALVGhtgSGKSTLASLLMGYYP-LTEGEIRLDGRPLSSLSHS-VLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 349 PEDRktagLILQMSVLHNITLPSVVMKLIVRKfGLIDSQLeKEIVRSFIEKLNikTPSPYQiVENLSGGNQQKVVLAKWL 428
Cdd:PRK10790 421 QQDP----VVLADTFLANVTLGRDISEEQVWQ-ALETVQL-AELARSLPDGLY--TPLGEQ-GNNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 429 AIKPKVLLLDEPTRGIDVNAKSEIYK---LISEMAVsgmgVVMVSSELPEILAmSDRILVMSEGRKTaeflrEEVTEEDL 505
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQalaAVREHTT----LVVIAHRLSTIVE-ADTILVLHRGQAV-----EQGTHQQL 561
|
...
gi 490181991 506 LKA 508
Cdd:PRK10790 562 LAA 564
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
409-492 |
3.76e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 409 QIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAkseIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSE 488
Cdd:PLN03073 623 QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSE 699
|
....
gi 490181991 489 GRKT 492
Cdd:PLN03073 700 GKVT 703
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
283-508 |
3.87e-07 |
|
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: 52.80 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAI--FgAHPgrTEGKVFIGGKEIKIHSPRDaVKNGIGLVPEDrktaglilq 360
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIprF-YEP--DSGQILLDGHDLADYTLAS-LRRQVALVSQD--------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 361 mSVLHNITLPSVV----MKLIVRKfgLIDSQLEKEIVRSFIEKL--NIKTPspyqIVEN---LSGGNQQKVVLAKWLAIK 431
Cdd:TIGR02203 415 -VVLFNDTIANNIaygrTEQADRA--EIERALAAAYAQDFVDKLplGLDTP----IGENgvlLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 432 PKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVmVSSELPEIlAMSDRILVMSEGRktaefLREEVTEEDLLKA 508
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLMQGRTTLV-IAHRLSTI-EKADRIVVMDDGR-----IVERGTHNELLAR 557
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-251 |
4.72e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 30 NVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFlegkevrfrnpreaQENGIALIPQELdLVPNLSSAENI- 108
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------------AERSIAYVPQQA-WIMNATVRGNIl 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 109 -FLSREPVNEFGVIEYQKMFEQASKLFSKLGVNIDPKTKveDLSTSQQQMVAIAKALSLDAKIIIMDEPTSA----IGKR 183
Cdd:PTZ00243 743 fFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGV--NLSGGQKARVSLARAVYANRDVYLLDDPLSAldahVGER 820
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 184 ETEQLFniIRSLKneGKSVIYISHRLeEIFEIADRVVVMRDGRKVGEGPIEEFDHDKLVRLMVGRSID 251
Cdd:PTZ00243 821 VVEECF--LGALA--GKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAAELKE 883
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
274-522 |
4.82e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 274 WSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTEGKVFIGGKeikihsprdavkngIGLVPedrk 353
Cdd:PLN03232 624 WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGS--------------VAYVP---- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 354 taglilQMSVLHNITlpsvvmkliVRKFGLIDSQLEKEIVRSFIEKLNIKTP-------SPYQIVE---NLSGGNQQKVV 423
Cdd:PLN03232 686 ------QVSWIFNAT---------VRENILFGSDFESERYWRAIDVTALQHDldllpgrDLTEIGErgvNISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 424 LAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELpEILAMSDRILVMSEGrktaeFLREEVTEE 503
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEG-----MIKEEGTFA 824
|
250 260
....*....|....*....|....*
gi 490181991 504 DLLKAAI------PRSVKVETTQRE 522
Cdd:PLN03232 825 ELSKSGSlfkklmENAGKMDATQEV 849
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
279-495 |
5.44e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIfgahPGRTEGKVFIGGkeikihsprDAVKNGIGLVPEDRKTAGLI 358
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVL----AERVTTGVITGG---------DRLVNGRPLDSSFQRSIGYV 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQmsvlHNITLPSVVMK--LIVRKFGLIDSQL---EK-EIVRSFIEKLNIKTpspYQ--IV----ENLSGGNQQKVVLAK 426
Cdd:TIGR00956 842 QQ----QDLHLPTSTVResLRFSAYLRQPKSVsksEKmEYVEEVIKLLEMES---YAdaVVgvpgEGLNVEQRKRLTIGV 914
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 427 WLAIKPKVLL-LDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSElPEILAMS--DRILVMSEGRKTAEF 495
Cdd:TIGR00956 915 ELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ-PSAILFEefDRLLLLQKGGQTVYF 985
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
286-500 |
6.00e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.55 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 286 VSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKI--HSPRDAVK-NGIGLVpedRKTAGLILQMS 362
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDG-SSGEVSLVGQPLHQmdEEARAKLRaKHVGFV---FQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNITLPSVVMklivrkfGLIDSQlEKEIVRSFIEKLNIKTpSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTR 442
Cdd:PRK10584 105 ALENVELPALLR-------GESSRQ-SRNGAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 443 GIDVNAKSEIYKLISEMAVS-GMGVVMVSSElPEILAMSDRILVMSEGRktaefLREEV 500
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQ-----LQEEA 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
284-489 |
6.47e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.85 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 284 DDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTeGKVFIGGKEIKIHSPRDAVkngiglVPEDRktaGLILQMSV 363
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH-GSITLDGKPVEGPGAERGV------VFQNE---GLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 364 LHNITlpsvvmklivrkFGL----IDSQLEKEIVRSFIEKLNIKTPSPYQIVEnLSGGNQQKVVLAKWLAIKPKVLLLDE 439
Cdd:PRK11248 88 QDNVA------------FGLqlagVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ-LSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490181991 440 PTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEG 489
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-221 |
6.96e-07 |
|
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: 49.49 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 24 GVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRFRnpreaqengialiPQELDLvpnls 103
Cdd:cd03222 11 GVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYK-------------PQYIDL----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 104 saeniflsrepvnefgvieyqkmfeqasklfsklgvnidpktkvedlSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKR 183
Cdd:cd03222 73 -----------------------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
|
170 180 190
....*....|....*....|....*....|....*....
gi 490181991 184 ETEQLFNIIRSLKNEG-KSVIYISHRLEEIFEIADRVVV 221
Cdd:cd03222 106 QRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHV 144
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
414-489 |
8.00e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 51.73 E-value: 8.00e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 414 LSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMaVSGMGVVMVSSElPEILAMSDRILVMSEG 489
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE-LPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
283-496 |
8.92e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.56 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKI-----HSPRdavkngIGLVPEDRKTA-- 355
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-PTSGELLIDDHPLHFgdysyRSQR------IRMIFQDPSTSln 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 356 -----GLILQMSVLHNITLPSvvmklivrkfglidSQLEKEIVRSfIEKLNIKTPSPYQIVENLSGGNQQKVVLAKWLAI 430
Cdd:PRK15112 102 prqriSQILDFPLRLNTDLEP--------------EQREKQIIET-LRQVGLLPDHASYYPHMLAPGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 431 KPKVLLLDEPTRGIDVNAKSEIYKLISEM-AVSGMGVVMVSSELPEILAMSDRILVMSEGR-----KTAEFL 496
Cdd:PRK15112 167 RPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEvvergSTADVL 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
281-495 |
9.63e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.87 E-value: 9.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 281 LLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGG---KEIKIHSPRDAvkngIGLVPEDRKTAGL 357
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINES-AEGEIIIDGlniAKIGLHDLRFK----ITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 358 ILQMSV--LHNITLPSVVMKLIVRKFglidsqleKEIVRSFIEKLNIKTPspyQIVENLSGGNQQKVVLAKWLAIKPKVL 435
Cdd:TIGR00957 1375 SLRMNLdpFSQYSDEEVWWALELAHL--------KTFVSALPDKLDHECA---EGGENLSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 436 LLDEPTRGIDVNAKSEIYKLIsEMAVSGMGVVMVSSELPEILAMSdRILVMSEGrKTAEF 495
Cdd:TIGR00957 1444 VLDEATAAVDLETDNLIQSTI-RTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKG-EVAEF 1500
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-226 |
1.01e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.52 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 37 KGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLegkevrfrnpreaqengialipqeldlvpnLSSAENIFLSREPVN 116
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------IDGEDILEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 117 EFGVIEYQKMFEQAsklfsklgvnidpktkvedlstsQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRS-- 194
Cdd:smart00382 51 LIIVGGKKASGSGE-----------------------LRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490181991 195 ----LKNEGKSVIYISHRLEEIFE-----IADRVVVMRDGR 226
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPallrrRFDRRIVLLLIL 148
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
414-505 |
1.05e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 414 LSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVMSEGRKTA 493
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
90
....*....|..
gi 490181991 494 EFLREEVTEEDL 505
Cdd:PRK10938 216 TGEREEILQQAL 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-239 |
1.58e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 30 NVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYE-GQIFLEGKevrfrnpreaqengIALIPQeLDLVPNLSSAENI 108
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT--------------VAYVPQ-VSWIFNATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 109 FLSrepvNEFGVIEYQKMFEqASKLFSKL--------------GVNIdpktkvedlSTSQQQMVAIAKALSLDAKIIIMD 174
Cdd:PLN03130 700 LFG----SPFDPERYERAID-VTALQHDLdllpggdlteigerGVNI---------SGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 175 EPTSAIGKRETEQLFNiiRSLKNE--GKSVIYISHRLEEIFEIaDRVVVMRDGRKVGEGPIEEFDHD 239
Cdd:PLN03130 766 DPLSALDAHVGRQVFD--KCIKDElrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
45-207 |
1.80e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 45 GENGAGKSTLMKILAGVYPDYEGQIFlegkeVRFRNPREAQENGIALIPQELDLVPNLSSAENIFLSREPVNE----FGV 120
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIY-----YKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSaetlYAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 121 IEYQKMFEQASKlfsklgvnidpktKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGK 200
Cdd:PRK13541 108 IHYFKLHDLLDE-------------KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGG 174
|
....*..
gi 490181991 201 SVIYISH 207
Cdd:PRK13541 175 IVLLSSH 181
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
283-489 |
1.93e-06 |
|
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: 48.87 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPgRTEGKVFIGGKEIKIHSPRDAVKNGIGLVPEDRKTAGLiLQMS 362
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ-TLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL-LNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 VLHNITLPSVVMKLivRKFGLIDS-QLEKEI-VRSFIEKLNIKTPSPyqiveNLSGGNQQKVVLAKWLAIKPKVLLLDEP 440
Cdd:cd03290 95 VEENITFGSPFNKQ--RYKAVTDAcSLQPDIdLLPFGDQTEIGERGI-----NLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490181991 441 TRGIDVN-----AKSEIYKLISEmavSGMGVVMVSSELpEILAMSDRILVMSEG 489
Cdd:cd03290 168 FSALDIHlsdhlMQEGILKFLQD---DKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
279-508 |
2.28e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.93 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIfgahpGR----TEGKVFIGGKEIKihsprdavkngiglvpeDRKT 354
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMI-----SRllppDSGEVLVDGLDVA-----------------TTPS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 355 AGLILQMSVL--HNitlpSVVMKLIVRK---FG----------LIDsqleKEIVRSFIEKLNIkTPSPYQIVENLSGGNQ 419
Cdd:COG4604 71 RELAKRLAILrqEN----HINSRLTVRElvaFGrfpyskgrltAED----REIIDEAIAYLDL-EDLADRYLDELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 420 QKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMA-VSGMGVVMVsseLPEI---LAMSDRILVMSEGRKTAEF 495
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIV---LHDInfaSCYADHIVAMKDGRVVAQG 218
|
250
....*....|...
gi 490181991 496 LREEVTEEDLLKA 508
Cdd:COG4604 219 TPEEIITPEVLSD 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-235 |
2.52e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 29 NNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPdyEGQIFLEGKEVRFRNPREAQENGIALIPQElDL-VPNLSSAEN 107
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDRLVNGRPLDSSFQRSIGYVQQQ-DLhLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 108 IFLS---REPV-------NEF--GVIEYQKMFEQASKLFSKLGvnidpktkvEDLSTSQQQMVAIAKALSLDAKIII-MD 174
Cdd:TIGR00956 857 LRFSaylRQPKsvsksekMEYveEVIKLLEMESYADAVVGVPG---------EGLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490181991 175 EPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLE-EIFEIADRVVVM-RDGRKVGEGPIEE 235
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaILFEEFDRLLLLqKGGQTVYFGDLGE 990
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
38-176 |
3.38e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 38 GEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfrnpREAQENGIALIPQELDLVPNLSSAENIFLsrepVNE 117
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT----RGDRSRFMAYLGHLPGLKADLSTLENLHF----LCG 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 118 FGVIEYQKMFEQASKLfskLGVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEP 176
Cdd:PRK13543 109 LHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
285-490 |
3.39e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 49.72 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTE---LLEAIFgaHPgrTEGKVFIGGKEIK------IHSPrdavkngIGLVPEDRkta 355
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLY--QP--TGGQVLLDGVPLVqydhhyLHRQ-------VALVGQEP--- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 356 gLILQMSVLHNITlpsvvmklivrkFGLIDSqlEKEIVRS---------FIEKLniktPSPYQIV-----ENLSGGNQQK 421
Cdd:TIGR00958 565 -VLFSGSVRENIA------------YGLTDT--PDEEIMAaakaanahdFIMEF----PNGYDTEvgekgSQLSGGQKQR 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 422 VVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLiseMAVSGMGVVMVSSELPeILAMSDRILVMSEGR 490
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLS-TVERADQILVLKKGS 690
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
275-490 |
5.63e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.19 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 275 SLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAH-PgrTEGKVFIGGKEIKIHSpRDAVKNGIGLVPEDrk 353
Cdd:PRK13657 343 SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdP--QSGRILIDGTDIRTVT-RASLRRNIAVVFQD-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 354 tAGLiLQMSVLHNITlpsvvmkliVRKFGLIDSQLEKEIVRS----FIEklniKTPSPYQIV-----ENLSGGNQQKVVL 424
Cdd:PRK13657 418 -AGL-FNRSIEDNIR---------VGRPDATDEEMRAAAERAqahdFIE----RKPDGYDTVvgergRQLSGGERQRLAI 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 425 AKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMaVSGMGVVMVSSELPEIlAMSDRILVMSEGR 490
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTV-RNADRILVFDNGR 546
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
282-517 |
6.00e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.14 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 282 LVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFgaHPGRTEGKVFIGG---KEIKIHSPRDAvkngIGLVPEDRKTAGLI 358
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL--RLLSTEGEIQIDGvswNSVTLQTWRKA----FGVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQMSVLHNITLPSVVMKLIVRKFGLidsqleKEIVRSFIEKLNiktpspYQIVEN---LSGGNQQKVVLAKWLAIKPKVL 435
Cdd:TIGR01271 1308 FRKNLDPYEQWSDEEIWKVAEEVGL------KSVIEQFPDKLD------FVLVDGgyvLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 436 LLDEPTRGIDVNAKSEIYKLISEmAVSGMGVVMVSSELPEILAMSDriLVMSEGRKTAEF--LREEVTEEDLLKAAIPRS 513
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEALLECQQ--FLVIEGSSVKQYdsIQKLLNETSLFKQAMSAA 1452
|
....
gi 490181991 514 VKVE 517
Cdd:TIGR01271 1453 DRLK 1456
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
395-489 |
8.91e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 395 SFIEKLNIKTPSPYQIVENLSGGNQQKVVLAKWLA--IKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSE 472
Cdd:cd03238 69 QFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
90
....*....|....*..
gi 490181991 473 lPEILAMSDRILVMSEG 489
Cdd:cd03238 149 -LDVLSSADWIIDFGPG 164
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
277-490 |
1.49e-05 |
|
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: 47.51 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLlvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFgahpgR----TEGKVFIGG---KEIKIHSPRDAvkngIGLVP 349
Cdd:COG5265 370 ERPIL--KGVSFEVPAGKTVAIVGPSGAGKSTLARLLF-----RfydvTSGRILIDGqdiRDVTQASLRAA----IGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 350 EDrktaglilqmSVLHNITLpsvvmklivR---KFGLIDSQlEKEIVR--------SFIEKLniktPSPYQIV--E---N 413
Cdd:COG5265 439 QD----------TVLFNDTI---------AyniAYGRPDAS-EEEVEAaaraaqihDFIESL----PDGYDTRvgErglK 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490181991 414 LSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVMVSSELPEIlAMSDRILVMSEGR 490
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTI-VDADEILVLEAGR 569
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
150-223 |
1.52e-05 |
|
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: 45.43 E-value: 1.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 150 LSTSQQQMVAIAKALSL----DAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRlEEIFEIADRVVVMR 223
Cdd:cd03227 78 LSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL-PELAELADKLIHIK 154
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
279-449 |
1.96e-05 |
|
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: 44.36 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 279 KKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGahpgrtegkvfiggkeikihsprdavkngiglvpEDRKTAGLI 358
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG----------------------------------ELEPDEGIV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQMSVLhnitlpsvvmklivrKFGLidsqlekeivrsfieklniktpspyqiVENLSGGNQQKVVLAKWLAIKPKVLLLD 438
Cdd:cd03221 58 TWGSTV---------------KIGY---------------------------FEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170
....*....|.
gi 490181991 439 EPTRGIDVNAK 449
Cdd:cd03221 96 EPTNHLDLESI 106
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
387-448 |
2.68e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 2.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 387 QLEKEIvRSFIEKLNIktpSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNA 448
Cdd:PRK11147 134 QLENRI-NEVLAQLGL---DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
28-225 |
2.71e-05 |
|
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: 45.67 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLEGKEVRfRNPREAQENGIALIPQEldlvPNLSSAeN 107
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS-KLPLHTLRSRLSIILQD----PILFSG-S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 108 IFLSREPVNEFGVIEYQKMFEQAS-KLFSKL---GVNIDPKTKVEDLSTSQQQMVAIAKALSLDAKIIIMDEPTSAIgKR 183
Cdd:cd03288 111 IRFNLDPECKCTDDRLWEALEIAQlKNMVKSlpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI-DM 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490181991 184 ETEQLFNIIRSLKNEGKSVIYISHRLEEIFEiADRVVVMRDG 225
Cdd:cd03288 190 ATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRG 230
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
277-445 |
3.57e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.95 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGR-TEGKVFIGGKEIkihSPRDAVKNGIGLVpEDRKTA 355
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTpVAGCVDVPDNQF---GREASLIDAIGRK-GDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 356 glilqMSVLHNITLPSVVmkLIVRKFglidsqlekeivrsfieklniktpspyqivENLSGGNQQKVVLAKWLAIKPKVL 435
Cdd:COG2401 116 -----VELLNAVGLSDAV--LWLRRF------------------------------KELSTGQKFRFRLALLLAERPKLL 158
|
170
....*....|
gi 490181991 436 LLDEPTRGID 445
Cdd:COG2401 159 VIDEFCSHLD 168
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
282-521 |
4.06e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 45.62 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 282 LVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHpgRTEGKVFIGG---KEIKIHSPRDAvkngIGLVPEDRKTAGLI 358
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL--NTEGDIQIDGvswNSVPLQKWRKA----FGVIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 359 LQMSVLHNITLPSVVMKLIVRKFGLidsqleKEIVRSFIEKLNiktpspYQIVEN---LSGGNQQKVVLAKWLAIKPKVL 435
Cdd:cd03289 93 FRKNLDPYGKWSDEEIWKVAEEVGL------KSVIEQFPGQLD------FVLVDGgcvLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 436 LLDEPTRGIDvNAKSEIYKLISEMAVSGMGVVMVSSELPEILAmSDRILVMSEGR-KTAEFLREEVTEEDLLKAAIPRSV 514
Cdd:cd03289 161 LLDEPSAHLD-PITYQVIRKTLKQAFADCTVILSEHRIEAMLE-CQRFLVIEENKvRQYDSIQKLLNEKSHFKQAISPSD 238
|
....*..
gi 490181991 515 KVETTQR 521
Cdd:cd03289 239 RLKLFPR 245
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
280-474 |
5.35e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.48 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGrTEGKVFIGGKEIKIHSP---------RDAVKNgiglvpe 350
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVaeachylghRNAMKP------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 351 drktaglilQMSVLHNITL--------PSVVMKLIVRkFGLIDsqlekeivrsfIEKLniktpsPYQiveNLSGGNQQKV 422
Cdd:PRK13539 87 ---------ALTVAENLEFwaaflggeELDIAAALEA-VGLAP-----------LAHL------PFG---YLSAGQKRRV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490181991 423 VLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGmGVVMVSSELP 474
Cdd:PRK13539 137 ALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQG-GIVIAATHIP 187
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-60 |
6.53e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 6.53e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490181991 14 EARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAG 60
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG 367
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
261-490 |
6.95e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 261 ITDEIFRveGIKLWSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIfgahPGRTEGkvFIGGKEIKI----HS 336
Cdd:TIGR00956 57 ILTRGFR--KLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTI----ASNTDG--FHIGVEGVItydgIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 337 PRDAVKNGIGLVPEDRKTAGLILQMSVLHniTLP-SVVMKLIVRKFGLIDSQLEKEIVRSFIEKL-------NIKTPSpy 408
Cdd:TIGR00956 129 PEEIKKHYRGDVVYNAETDVHFPHLTVGE--TLDfAARCKTPQNRPDGVSREEYAKHIADVYMATyglshtrNTKVGN-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 409 QIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVS--SELPEILAMSDRILVM 486
Cdd:TIGR00956 205 DFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVL 284
|
....
gi 490181991 487 SEGR 490
Cdd:TIGR00956 285 YEGY 288
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
150-236 |
8.41e-05 |
|
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: 45.39 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 150 LSTSQQQMVAIAKAL--SLDAKIIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRlEEIFEIADRVVVM----- 222
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYVIDIgpgag 567
|
90
....*....|....*
gi 490181991 223 -RDGRKVGEGPIEEF 236
Cdd:TIGR00630 568 eHGGEVVASGTPEEI 582
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
274-507 |
9.38e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 274 WSLDRKKLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPGRTEGKVFIGGKeikihsprdavkngIGLVPedrk 353
Cdd:PLN03130 624 WDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGT--------------VAYVP---- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 354 taglilQMSVLHNITLPSVVMklivrkFGLI--DSQLEKEI-VRSFIEKLNIKTPSPY-QIVE---NLSGGNQQKVVLAK 426
Cdd:PLN03130 686 ------QVSWIFNATVRDNIL------FGSPfdPERYERAIdVTALQHDLDLLPGGDLtEIGErgvNISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 427 WLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELpEILAMSDRILVMSEGRktaefLREEVTEEDLL 506
Cdd:PLN03130 754 AVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQL-HFLSQVDRIILVHEGM-----IKEEGTYEELS 827
|
.
gi 490181991 507 K 507
Cdd:PLN03130 828 N 828
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
389-486 |
1.02e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.16 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 389 EKEIVRSFIEKLNIKtPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVM 468
Cdd:COG1245 189 ERGKLDELAEKLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLV 267
|
90
....*....|....*....
gi 490181991 469 VSSELpEIL-AMSDRILVM 486
Cdd:COG1245 268 VEHDL-AILdYLADYVHIL 285
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
283-439 |
1.02e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 283 VDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIKIhsprdavknGIGlvpedrktAGLILQM 361
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGvTMP--NKGTVDIKGSAALI---------AIS--------SGLNGQL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490181991 362 SVLHNITLPSVVMKLIVRKFglidsqleKEIVRSFIEKLNIKTpSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDE 439
Cdd:PRK13545 101 TGIENIELKGLMMGLTKEKI--------KEIIPEIIEFADIGK-FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
280-471 |
2.56e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.48 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFG-AHPgrTEGKVFIGGKEIkiHSPRDAV---------KNGIglvp 349
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlARP--DAGEVLWQGEPI--RRQRDEYhqdllylghQPGI---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 350 edrKTAglilqMSVLHNitlpsvvmkliVRKFGLIDSQLEKEIVRSFIEKLNIK----TPspyqiVENLSGGNQQKVVLA 425
Cdd:PRK13538 86 ---KTE-----LTALEN-----------LRFYQRLHGPGDDEALWEALAQVGLAgfedVP-----VRQLSAGQQRRVALA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490181991 426 K-WLAiKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGmGVVMVSS 471
Cdd:PRK13538 142 RlWLT-RAPLWILDEPFTAIDKQGVARLEALLAQHAEQG-GMVILTT 186
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-60 |
2.57e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 2.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 490181991 11 VLLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAG 60
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG 372
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
411-486 |
6.90e-04 |
|
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: 41.58 E-value: 6.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490181991 411 VENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVSSELPEILAMSDRILVM 486
Cdd:cd03236 137 IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
285-490 |
8.54e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.17 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 285 DVSFYVRKGEVLGIYGLVGAGRTELLEAIFGaHPGR--TEGKVFIGGKEIkihsprdavkngIGLVPEDRKTAGLILQMS 362
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAYkiLEGDILFKGESI------------LDLEPEERAHLGIFLAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 363 vlHNITLPSV----VMKLI---VRKFgLIDSQLEKEIVRSFI-EKLNIKTPSPYQIVENL----SGGNQQKVVLAKWLAI 430
Cdd:CHL00131 92 --YPIEIPGVsnadFLRLAynsKRKF-QGLPELDPLEFLEIInEKLKLVGMDPSFLSRNVnegfSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 431 KPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVVMVsSELPEIL--AMSDRILVMSEGR 490
Cdd:CHL00131 169 DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILI-THYQRLLdyIKPDYVHVMQNGK 229
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-71 |
9.59e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 9.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFL 71
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
389-507 |
1.45e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 389 EKEIVRSFIEKLniktPSPYQIV-----ENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSG 463
Cdd:PTZ00265 554 KKVLIHDFVSAL----PDKYETLvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNE 629
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 490181991 464 MGVVMVSSELPEILAMSDRILVMSEgRKTAEFLREEVTEEDLLK 507
Cdd:PTZ00265 630 NRITIIIAHRLSTIRYANTIFVLSN-RERGSTVDVDIIGEDPTK 672
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
280-506 |
1.62e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 40.28 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 280 KLLVDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAhPGRTEGKVFIGGKEIK---IHSPRDAVKngiglvpedrktag 356
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM-VDIFDGKIVIDGIDISklpLHTLRSRLS-------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 357 LILQMSVLHNITLpsvvmklivrKFGL------IDSQLEKEIVRSFIEKLNIKTPSPYQIV-----ENLSGGNQQKVVLA 425
Cdd:cd03288 99 IILQDPILFSGSI----------RFNLdpeckcTDDRLWEALEIAQLKNMVKSLPGGLDAVvteggENFSVGQRQLFCLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 426 KWLAIKPKVLLLDEPTRGIDVnAKSEIYKLISEMAVSGMGVVMVSSELPEILAmSDRILVMSEGrktaeFLREEVTEEDL 505
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDM-ATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRG-----ILVECDTPENL 241
|
.
gi 490181991 506 L 506
Cdd:cd03288 242 L 242
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
150-235 |
1.70e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 150 LSTSQQQMVAIAKALSLDAK---IIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLEEIfEIADRVVVM---- 222
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI-KTADYIIDLgpeg 908
|
90
....*....|....*
gi 490181991 223 --RDGRKVGEGPIEE 235
Cdd:TIGR00630 909 gdGGGTVVASGTPEE 923
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
298-474 |
1.78e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 298 IYGLVGAGRTELLEAIFG-AHPgrTEGKVFIggKEIKIHSPRDAVKNGIGlvpedrKTAGLILQMSVLHNITLPSVV--- 373
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGiMQP--SSGNIYY--KNCNINNIAKPYCTYIG------HNLGLKLEMTVFENLKFWSEIyns 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 374 ---MKLIVRKFGLIDSQLEKeivrsfieklniktpspyqiVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKS 450
Cdd:PRK13541 101 aetLYAAIHYFKLHDLLDEK--------------------CYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
170 180
....*....|....*....|....
gi 490181991 451 EIYKLISEMAVSGmGVVMVSSELP 474
Cdd:PRK13541 161 LLNNLIVMKANSG-GIVLLSSHLE 183
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
277-489 |
1.90e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 277 DRKKLLvDDVSFYVRKGEVLGIYGLVGAGRTELLEAIFGAHPG-RTEGKVFIGGkeikihsprdavkngiglVPEDRKTA 355
Cdd:PLN03140 891 DRLQLL-REVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgYIEGDIRISG------------------FPKKQETF 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 356 GLILQMSVLHNITLPSVVMK--LIVRKFGLIDSQLEKEIVRSFIEKL-------NIKT-----PSpyqiVENLSGGNQQK 421
Cdd:PLN03140 952 ARISGYCEQNDIHSPQVTVResLIYSAFLRLPKEVSKEEKMMFVDEVmelveldNLKDaivglPG----VTGLSTEQRKR 1027
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490181991 422 VVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVSGMGVV-MVSSELPEILAMSDRILVMSEG 489
Cdd:PLN03140 1028 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVcTIHQPSIDIFEAFDELLLMKRG 1096
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-72 |
2.12e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 2.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490181991 12 LLEARNITKTFPGVIAVNNVTLQIYKGEVCALVGENGAGKSTLMKILAGVYPDYEGQIFLE 72
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
377-448 |
2.30e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 2.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490181991 377 IVRKFGLIDSQLEKEIVRSFIEKLNIKTPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNA 448
Cdd:PLN03073 308 IYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA 379
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
43-59 |
2.94e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 39.36 E-value: 2.94e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-220 |
3.76e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 3.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490181991 150 LSTSQQQMVAIAKALSLDAK---IIIMDEPTSAIGKRETEQLFNIIRSLKNEGKSVIYISHRLeEIFEIADRVV 220
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVL 882
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
393-485 |
5.69e-03 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 38.54 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 393 VRSFI-EKLNIKTPSPY----------------QIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKL 455
Cdd:cd03237 78 VRDLLsSITKDFYTHPYfkteiakplqieqildREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
90 100 110
....*....|....*....|....*....|.
gi 490181991 456 ISEMAVSGMGVVMV-SSELPEILAMSDRILV 485
Cdd:cd03237 158 IRRFAENNEKTAFVvEHDIIMIDYLADRLIV 188
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
28-245 |
7.62e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.83 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 28 VNNVTLQIYKGEVCaLVGENGAGKSTLMKILAGVYPDYEGQIFlegKEVRFRNPREAQENGIALipqELDLVPNLSSAEN 107
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSRKF---DEEDFYLGDDPDLPEIEI---ELTFGSLLSRLLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 108 IFLSREPVNEFGVI------EYQKMFEQASKLFSKLGVNIDPKTKV----------------------------EDLSTS 153
Cdd:COG3593 87 LLLKEEDKEELEEAleelneELKEALKALNELLSEYLKELLDGLDLelelsldeledllkslslriedgkelplDRLGSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 154 QQQMVAIA--KALSL-----DAKIIIMDEPtsaigkrET-------EQLFNIIRSLKNEGKSVIYISHRLE--EIFEIAD 217
Cdd:COG3593 167 FQRLILLAllSALAElkrapANPILLIEEP-------EAhlhpqaqRRLLKLLKELSEKPNQVIITTHSPHllSEVPLEN 239
|
250 260
....*....|....*....|....*...
gi 490181991 218 RVVVMRDGRKVGEGPIEEFDHDKLVRLM 245
Cdd:COG3593 240 IRRLRRDSGGTTSTKLIDLDDEDLRKLL 267
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
389-486 |
8.66e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 38.64 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490181991 389 EKEIVRSFIEKLNIKtPSPYQIVENLSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAvSGMGVVM 468
Cdd:PRK13409 189 ERGKLDEVVERLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLV 266
|
90
....*....|....*...
gi 490181991 469 VSSELPEILAMSDRILVM 486
Cdd:PRK13409 267 VEHDLAVLDYLADNVHIA 284
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
414-462 |
9.39e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 38.58 E-value: 9.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 490181991 414 LSGGNQQKVVLAKWLAIKPKVLLLDEPTRGIDVNAKSEIYKLISEMAVS 462
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGIT 631
|
|
| |
