|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-589 |
0e+00 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 999.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 1 MDKSRQSELVRWLKLQAAPARRWLRLSMLLGVLSGLLIIGQAWCLAVLLQSLIMEHVPREQLLTPFTVLVILFIARAVVA 80
Cdd:PRK11174 1 MDKSRQKELTRWLKQQSKPAKRWLNLSILLGFLSGLLLIAQAWLLATILQALIIENIPREALLPPFILLILLFVLRALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 81 AIRERVGFICGQVVRRDIRRTVLDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFP 160
Cdd:PRK11174 81 WLRERVGFKAGQHIRQQIRQQVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 161 INWAAALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTM 240
Cdd:PRK11174 161 INWAAGLILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 241 EVLRMAFLSSAVLEFFAAISIAVVAVYFGFSYLGELNFGSYGMGVTLFAGFIALILAPEFFQPLRDLGTYYHAKAQAVGA 320
Cdd:PRK11174 241 EVLRMAFLSSAVLEFFASISIALVAVYFGFSYLGELNFGHYGTGVTLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 321 AESLFTLLSAENNDDElPGTEPLTPAEQIAVTATDLVIFAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLLGF 400
Cdd:PRK11174 321 AESLVTFLETPLAHPQ-QGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 401 LPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSRPDASAEEITAVMEKAYVTDFIDSLPDGVNTVV 480
Cdd:PRK11174 400 LPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 481 GDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTHLLEETRDYDEVWVMDKG 560
Cdd:PRK11174 480 GDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
570 580
....*....|....*....|....*....
gi 802097265 561 LIIEQGSYAALQQQQGAFAQLLSHRTGDL 589
Cdd:PRK11174 560 QIVQQGDYAELSQAGGLFATLLAHRQEEI 588
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-576 |
0e+00 |
|
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: 740.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 6 QSELVRWLKLQAAPARRWLRLSMLLGVLSGLLIIGQAWCLAVLLQSLIMEHVPREQLLTPFTVLVILFIARAVVAAIRER 85
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 86 VGFICGQVVRRDIRRTVLDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAA 165
Cdd:COG4988 81 AAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 166 ALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRM 245
Cdd:COG4988 161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 246 AFLSSAVLEFFAAISIAVVAVYFGFSYLGElnfgsygmGVTLFAGFIALILAPEFFQPLRDLGTYYHAKAQAVGAAESLF 325
Cdd:COG4988 241 AFLSSAVLEFFASLSIALVAVYIGFRLLGG--------SLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 326 TLLSAENNDDElPGTEPLTPAEQIAVTATDLVIFAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYE 404
Cdd:COG4988 313 ALLDAPEPAAP-AGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLgFLPPYS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 405 GSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSRPDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNA 484
Cdd:COG4988 392 GSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 485 ARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIE 564
Cdd:COG4988 472 RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVE 551
|
570
....*....|..
gi 802097265 565 QGSYAALQQQQG 576
Cdd:COG4988 552 QGTHEELLAKNG 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-557 |
0e+00 |
|
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: 561.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 20 ARRWLRLSMLLGVLSGLLIIGQAWCLAVLLQSLIMEHVPREQLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIR 99
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 100 RTVLDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVF 179
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 180 MALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFFAAI 259
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 260 SIAVVAVYFGFSYLGElnfgsygmGVTLFAGFIALILAPEFFQPLRDLGTYYHAKAQAVGAAESLFTLLSAenNDDELPG 339
Cdd:TIGR02857 241 SVALVAVYIGFRLLAG--------DLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDA--APRPLAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 340 TEPLTPAEQIAVTATDLVIFAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIR 418
Cdd:TIGR02857 311 KAPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLgFVDPTEGSIAVNGVPLADAD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 419 PESWRTQLSWVGQNPHLPEQTILDNIRLSRPDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVA 498
Cdd:TIGR02857 391 ADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALA 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 499 RALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTHLLEETRDYDEVWVM 557
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
27-324 |
6.07e-130 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 382.14 E-value: 6.07e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 27 SMLLGVLSGLLIIGQAWCLAVLLQSLIMEHVPREQLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTVLDKL 106
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 107 EQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVFMALVGLG 186
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 187 AADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFFAAISIAVVAV 266
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 267 YFGFSYLGElnfgsygmGVTLFAGFIALILAPEFFQPLRDLGTYYHAKAQAVGAAESL 324
Cdd:cd18584 241 YIGFRLLGG--------SLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-588 |
2.57e-108 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 336.75 E-value: 2.57e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 1 MDKSRQSeLVRWLKLQAAPARRWLRLSMLLGVLSGLLIIGQAWCLAVLLQSLImEHVPREQLLTPFTVLVILFIARAVVA 80
Cdd:COG1132 1 MSKSPRK-LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-AGGDLSALLLLLLLLLGLALLRALLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 81 AIRERVGFICGQVVRRDIRRTVLDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFP 160
Cdd:COG1132 79 YLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 161 INWAAALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTM 240
Cdd:COG1132 159 IDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 241 EVLRMAFLSSAVLEFFAAISIAVVAVYFGFSYL-GELNFGSygmgvtlFAGFIALILApeFFQPLRDLGTYYHAKAQAVG 319
Cdd:COG1132 239 RAARLSALFFPLMELLGNLGLALVLLVGGLLVLsGSLTVGD-------LVAFILYLLR--LFGPLRQLANVLNQLQRALA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 320 AAESLFTLLSAENNDDELPGTEPLTPAEQiAVTATDlVIFAPSGEK--LAGpLNFTLNAGQRIALVGQSGAGKSSllnll 397
Cdd:COG1132 310 SAERIFELLDEPPEIPDPPGAVPLPPVRG-EIEFEN-VSFSYPGDRpvLKD-ISLTIPPGETVALVGPSGSGKSTlvnll 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 398 -lgflPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSRPDASAEEITAVMEKAYVTDFIDSLPDGV 476
Cdd:COG1132 387 lrfydPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 477 NTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTHLLEETRDYDEVWV 556
Cdd:COG1132 467 DTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILV 546
|
570 580 590
....*....|....*....|....*....|..
gi 802097265 557 MDKGLIIEQGSYAALQQQQGAFAQLLSHRTGD 588
Cdd:COG1132 547 LDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
27-324 |
2.65e-94 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 290.72 E-value: 2.65e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 27 SMLLGVLSGLLIIGQAWCLAVLLQSLIMeHVPREQLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTVLDKL 106
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFA-GGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 107 EQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVFMALVGLG 186
Cdd:cd18561 80 LKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 187 AADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFFAAISIAVVAV 266
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 267 YFGFSYLgelnfgsyGMGVTLFAGFIALILAPEFFQPLRDLGTYYHAKAQAVGAAESL 324
Cdd:cd18561 240 VGALRVL--------GGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-584 |
9.69e-83 |
|
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: 269.71 E-value: 9.69e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 7 SELVRWLKLqAAPARRWLRLSMLLGVLSGLLIIG----QAWCL-AVLLQSLIMEhvpreqLLTPfTVLVILF-IARAVV- 79
Cdd:COG4987 1 RDLLRLLRL-LRPHRGRLLLGVLLGLLTLLAGIGllalSGWLIaAAALAPPILN------LFVP-IVGVRAFaIGRTVFr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 80 ---------AAIRervgficgqvVRRDIRRTVLDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSR-YLPQMTLSAT 149
Cdd:COG4987 73 ylerlvshdATLR----------LLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRvLLPLLVALLV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 150 IPMMILITLF---PINWAAALILLVTAPLIPVFMALVGLGAADANRRnflALSRLSGDFLDRLRGLETIRFFHRGREEVK 226
Cdd:COG4987 143 ILAAVAFLAFfspALALVLALGLLLAGLLLPLLAARLGRRAGRRLAA---ARAALRARLTDLLQGAAELAAYGALDRALA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 227 QIDDATEDFRSRTMEVLRMAFLSSAVLEFFAAISIAVVAVyfgfsyLGELNFGSYGMGVTLFAGFIALILA-PEFFQPLR 305
Cdd:COG4987 220 RLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLW------LAAPLVAAGALSGPLLALLVLAALAlFEALAPLP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 306 DLGTYYhakAQAVGAAESLFTLLSAENNDDElpGTEPLTPAEQIAVTATDLVI-FAPSGEKLAGPLNFTLNAGQRIALVG 384
Cdd:COG4987 294 AAAQHL---GRVRAAARRLNELLDAPPAVTE--PAEPAPAPGGPSLELEDVSFrYPGAGRPVLDGLSLTLPPGERVAIVG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 385 QSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSRPDASAEEITAVMEKA 463
Cdd:COG4987 369 PSGSGKSTLLALLLrFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 464 YVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTH 543
Cdd:COG4987 449 GLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITH 528
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 802097265 544 LLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLLSH 584
Cdd:COG4987 529 RLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-583 |
7.71e-73 |
|
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: 247.05 E-value: 7.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 11 RWLKLQAAPARRWLRLSMLLGVLSGLLiigqAWCLAVLLQSLIMEHVPRE--QLLTPFTV-LVILFIARAVVAAIRERVG 87
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLL----ALATPLFTQVVIDRVLPNQdlSTLWVLAIgLLLALLFEGLLRLLRSYLL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 88 FICGQVVRRDIRRTVLDKLEQLgPVRV-KGKPAGSWATIILEqIDDMQDYYSRYLpqMTLSATIPMMI--LITLFPINWA 164
Cdd:COG2274 221 LRLGQRIDLRLSSRFFRHLLRL-PLSFfESRSVGDLASRFRD-VESIREFLTGSL--LTALLDLLFVLifLIVLFFYSPP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 165 AALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLR 244
Cdd:COG2274 297 LALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 245 MAFLSSAVLEFFAAISIAVVaVYFGfSYL---GELNFGsygmgvTLFAgFIALILApeFFQPLRDLGTYYHAKAQAVGAA 321
Cdd:COG2274 377 LSNLLSTLSGLLQQLATVAL-LWLG-AYLvidGQLTLG------QLIA-FNILSGR--FLAPVAQLIGLLQRFQDAKIAL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 322 ESLFTLLSAEnnDDELPGTEPLTPAE-QIAVTATDLVI-FAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLL- 398
Cdd:COG2274 446 ERLDDILDLP--PEREEGRSKLSLPRlKGDIELENVSFrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLg 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 399 GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSRPDASAEEITAVMEKAYVTDFIDSLPDGVNT 478
Cdd:COG2274 524 LYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDT 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 479 VVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTHLLEETRDYDEVWVMD 558
Cdd:COG2274 604 VVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLD 683
|
570 580
....*....|....*....|....*
gi 802097265 559 KGLIIEQGSYAALQQQQGAFAQLLS 583
Cdd:COG2274 684 KGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
370-581 |
1.33e-57 |
|
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: 193.14 E-value: 1.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGF-LPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFyDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:cd03249 102 PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQL 581
Cdd:cd03249 182 LDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
154-585 |
1.55e-53 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 191.77 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 154 ILITLFPINWAAALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATE 233
Cdd:PRK11176 156 LFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 234 DFRSRTMEVLRMAFLSSAVLEFFAAISIAVVAVYFGF-SYLGELNFGSYgmgVTLFAGFIALIlapeffQPLRDLgTYYH 312
Cdd:PRK11176 236 RMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVMDTLTAGTI---TVVFSSMIALM------RPLKSL-TNVN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 313 AKAQ-AVGAAESLFTLLSAENNDDElpGTEPLTPAeQIAVTATDLVIFAPSGEKLA-GPLNFTLNAGQRIALVGQSGAGK 390
Cdd:PRK11176 306 AQFQrGMAACQTLFAILDLEQEKDE--GKRVIERA-KGDIEFRNVTFTYPGKEVPAlRNINFKIPAGKTVALVGRSGSGK 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 391 SSLLNLLLGFLP-YEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSRPDA-SAEEITAVMEKAYVTDF 468
Cdd:PRK11176 383 STIANLLTRFYDiDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDF 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 469 IDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTHLLEET 548
Cdd:PRK11176 463 INKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTI 542
|
410 420 430
....*....|....*....|....*....|....*..
gi 802097265 549 RDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLlsHR 585
Cdd:PRK11176 543 EKADEILVVEDGEIVERGTHAELLAQNGVYAQL--HK 577
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-545 |
5.52e-52 |
|
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: 186.41 E-value: 5.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 11 RWLKLQAAPARRWLRLSMLLGVLSGLLIIGQAWCLAVLLqSLIMEHVPREQLLTPFTVLVILFIARAVVAAIRERVGFIC 90
Cdd:TIGR02868 2 LRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLI-SRAAEMPPVLYLSVAAVAVRAFGIGRAVFRYLERLVGHDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 91 GQVVRRDIRRTVLDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILL 170
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 171 VTAPLIPVFMALV-GLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLS 249
Cdd:TIGR02868 161 AGLLLAGFVAPLVsLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 250 SAVLEFFAAISIAVVAVYFGFSYLGElnfgsyGMGVTLFAGFIALILApeFFQPLRDLGTYYHAKAQAVGAAESLFTLLS 329
Cdd:TIGR02868 241 AALTLLAAGLAVLGALWAGGPAVADG------RLAPVTLAVLVLLPLA--AFEAFAALPAAAQQLTRVRAAAERIVEVLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 330 AENNDDE--LPGTEPLtPAEQIAVTATDLVIFAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGS 406
Cdd:TIGR02868 313 AAGPVAEgsAPAAGAV-GLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAgLLDPLQGE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 407 IRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSRPDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAAR 486
Cdd:TIGR02868 392 VTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGAR 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 487 LSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTHLL 545
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
370-581 |
2.55e-51 |
|
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: 176.27 E-value: 2.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLG-FLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRfYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:cd03251 101 PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQL 581
Cdd:cd03251 181 LERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
370-581 |
5.15e-51 |
|
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: 175.50 E-value: 5.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFL-PYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYdVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:cd03253 100 PDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQL 581
Cdd:cd03253 180 LRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
370-576 |
4.48e-49 |
|
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: 170.10 E-value: 4.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGF-LPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:cd03254 102 PNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQG 576
Cdd:cd03254 182 LEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
301-581 |
3.54e-46 |
|
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: 171.93 E-value: 3.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 301 FQPLRDLGTYYHAKAQAVGAAESLFTLLSAENNDDELPGTEPLTPAEqiAVTATDLVIFAPSGEK--LAGpLNFTLNAGQ 378
Cdd:COG5265 309 YIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGG--GEVRFENVSFGYDPERpiLKG-VSFEVPAGK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 379 RIALVGQSGAGKSSLLNLLLGF-LPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSRPDASAEEIT 457
Cdd:COG5265 386 TVAIVGPSGAGKSTLARLLFRFyDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 458 AVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQT 537
Cdd:COG5265 466 AAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRT 545
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 802097265 538 TLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQL 581
Cdd:COG5265 546 TLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
146-582 |
3.10e-44 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 165.90 E-value: 3.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 146 LSATIPMMILI-TLFPINWAAALILLVtapLIPVFMALVGL-------GAADANRRNflalSRLSGDFLDRLRGLETIRF 217
Cdd:PRK13657 138 LATLVALVVLLpLALFMNWRLSLVLVV---LGIVYTLITTLvmrktkdGQAAVEEHY----HDLFAHVSDAIGNVSVVQS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 218 FHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEffAAISIAVVAVYFGFSYL---GELNFGSygmgVTLFAGFIAL 294
Cdd:PRK13657 211 YNRIEAETQALRDIADNLLAAQMPVLSWWALASVLNR--AASTITMLAILVLGAALvqkGQLRVGE----VVAFVGFATL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 295 ILapeffQPLRDLGTYYHAKAQAVGAAESLFTLLSAENNDDELPGTEPLTPAEQiAVTATDLVI-FAPSGEKLAGpLNFT 373
Cdd:PRK13657 285 LI-----GRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKG-AVEFDDVSFsYDNSRQGVED-VSFE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 374 LNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSRPDAS 452
Cdd:PRK13657 358 AKPGQTVAIVGPTGAGKSTLINLLQrVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDAT 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 453 AEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEA 532
Cdd:PRK13657 438 DEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 802097265 533 AHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLL 582
Cdd:PRK13657 518 MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
370-566 |
5.51e-40 |
|
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: 145.04 E-value: 5.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAgLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:cd03245 103 PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKER 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQG 566
Cdd:cd03245 183 LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
370-560 |
7.20e-40 |
|
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: 143.29 E-value: 7.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIrlsr 448
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLrLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENI---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 pdasaeeitavmekayvtdfidslpdgvntvvgdnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:cd03228 97 --------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
|
170 180 190
....*....|....*....|....*....|..
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKG 560
Cdd:cd03228 139 LRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
155-582 |
2.85e-37 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 147.18 E-value: 2.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 155 LITLFPINWAAALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATED 234
Cdd:TIGR00958 293 LGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 235 FRS--RTMEVLRMAFLssAVLEFFAAISIAVVAVYFGFSYL-GELNFGsygmGVTLFagfiaLILAPEFFQPLRDLGTYY 311
Cdd:TIGR00958 373 TLQlnKRKALAYAGYL--WTTSVLGMLIQVLVLYYGGQLVLtGKVSSG----NLVSF-----LLYQEQLGEAVRVLSYVY 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 312 HAKAQAVGAAESLFTLLSAENNDdELPGTepLTPAEQIAVTATDLVIFA----PSGEKLAGpLNFTLNAGQRIALVGQSG 387
Cdd:TIGR00958 442 SGMMQAVGASEKVFEYLDRKPNI-PLTGT--LAPLNLEGLIEFQDVSFSypnrPDVPVLKG-LTFTLHPGEVVALVGPSG 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 388 AGKSSLLNLLLGF-LPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSRPDASAEEITAVMEKAYVT 466
Cdd:TIGR00958 518 SGKSTVAALLQNLyQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAH 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 467 DFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEervmHALNEAAHQQ--TTLLVTHL 544
Cdd:TIGR00958 598 DFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRAsrTVLLIAHR 673
|
410 420 430
....*....|....*....|....*....|....*...
gi 802097265 545 LEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLL 582
Cdd:TIGR00958 674 LSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
29-312 |
1.17e-36 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 138.05 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 29 LLGVLSGLLIIGQAWCLAVLLQSLIMEHVPREQLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTVLDKLEQ 108
Cdd:cd18781 3 LLQWISLLANIAFVFSIANLLQKLLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 109 LGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVFMALVGLGAA 188
Cdd:cd18781 83 LGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKIAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 189 DANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFFA------AISIA 262
Cdd:cd18781 163 KLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVAyggaalGIILA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 802097265 263 VVAVYFGfsylgelnfgsygmGVTLFAGFIALILAPEFFQPLRDLGTYYH 312
Cdd:cd18781 243 LLQFANG--------------SISLAGALFIILLSAEFFLPLRLLGSFFH 278
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
370-581 |
4.23e-36 |
|
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: 134.92 E-value: 4.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGF-LPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIALAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:cd03252 101 PGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQL 581
Cdd:cd03252 181 MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
370-567 |
4.50e-36 |
|
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: 134.54 E-value: 4.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIrlsr 448
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFrLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 pD----ASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEER 524
Cdd:cd03244 99 -DpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDAL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 802097265 525 VMHALNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGS 567
Cdd:cd03244 178 IQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
133-581 |
5.42e-36 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 142.55 E-value: 5.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 133 MQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGL 212
Cdd:PRK10790 135 IRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGM 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 213 ETIR-FFHRGREEVKQIDDATEDFRSRtMEVLRM-AFLSSAVLEFFAAISIAVVAVYFGFSylgelNFGSYGMGVtLFAg 290
Cdd:PRK10790 215 SVIQqFRQQARFGERMGEASRSHYMAR-MQTLRLdGFLLRPLLSLFSALILCGLLMLFGFS-----ASGTIEVGV-LYA- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 291 FIALIlaPEFFQPLRDLGTYYHAKAQAVGAAESLFTLLSAEN----NDDElpgtePLTPAeQIAVtatDLVIFAPSGEKL 366
Cdd:PRK10790 287 FISYL--GRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRqqygNDDR-----PLQSG-RIDI---DNVSFAYRDDNL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 367 AGPlNFTLNAGQR--IALVGQSGAGKSSLLNLLLGFLPY-EGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDN 443
Cdd:PRK10790 356 VLQ-NINLSVPSRgfVALVGHTGSGKSTLASLLMGYYPLtEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLAN 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 444 IRLSRpDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEE 523
Cdd:PRK10790 435 VTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 524 RVMHALnEAAHQQTTLLV-THLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQL 581
Cdd:PRK10790 514 AIQQAL-AAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
370-587 |
4.59e-35 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 140.65 E-value: 4.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGF-LPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:TIGR01846 476 LNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLyTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCN 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:TIGR01846 556 PGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRN 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLLSHRTG 587
Cdd:TIGR01846 636 MREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
24-292 |
8.64e-35 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 132.38 E-value: 8.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 24 LRLSMLLGVLSGLLIIGQAWCLAVLLQSLIMEHVPREQLLTPF-TVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTV 102
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYsLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 103 LDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVFMAL 182
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 183 VGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFFAAISIA 262
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|..
gi 802097265 263 VVAvYFGFSYL--GELNFGSYGMGVTLFAGFI 292
Cdd:pfam00664 241 LAL-WFGAYLVisGELSVGDLVAFLSLFAQLF 271
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
152-577 |
1.83e-34 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 138.85 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 152 MMILITLFPINWAAALILLVTAPLipvfMALVGLGA----ADANRRNFLALSRLSGDFLDRLRGLETI-------RFFHR 220
Cdd:TIGR03375 274 LLFLLVIAIIGGPLVWVPLVAIPL----ILLPGLLLqrplSRLAEESMRESAQRNAVLVESLSGLETIkalnaegRFQRR 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 221 GREEVKQIddATEDFRSRTMEVLRMAFlsSAVLEFFAAISIAVVAVYfgfsylgELNFGSYGMGvtlfaGFIA-LILAPE 299
Cdd:TIGR03375 350 WEQTVAAL--ARSGLKSRFLSNLATNF--AQFIQQLVSVAIVVVGVY-------LISDGELTMG-----GLIAcVMLSGR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 300 FFQPLRD----LGTYYHAKAqavgAAESLFTLLSAENNDDElpGTEPLT-PAEQIAVTATDLVIFAPSGEKLA-GPLNFT 373
Cdd:TIGR03375 414 ALAPLGQlaglLTRYQQAKT----ALQSLDELMQLPVERPE--GTRFLHrPRLQGEIEFRNVSFAYPGQETPAlDNVSLT 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 374 LNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSRPDAS 452
Cdd:TIGR03375 488 IRPGEKVAIIGRIGSGKSTLLKLLLgLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYAD 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 453 AEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEA 532
Cdd:TIGR03375 568 DEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW 647
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 802097265 533 AHQQTTLLVTH---LLEETrdyDEVWVMDKGLIIEQGSYAA-LQQQQGA 577
Cdd:TIGR03375 648 LAGKTLVLVTHrtsLLDLV---DRIIVMDNGRIVADGPKDQvLEALRKG 693
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
26-322 |
2.34e-34 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 131.90 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 26 LSMLLGVLSGLLIIGQAWCLAVLLQSLIMEHvPREQLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTVLDK 105
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLLIDDVIPAG-DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 106 LEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVFMALVGL 185
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 186 GAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFFAAISIAVVA 265
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 266 VYFGFSYL-GELNFGSYgmgvTLFAGFIALilapeFFQPLRDLGTYYHAKAQAVGAAE 322
Cdd:cd07346 242 LYGGYLVLqGSLTIGEL----VAFLAYLGM-----LFGPIQRLANLYNQLQQALASLE 290
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
370-584 |
2.38e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 134.57 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGF-LPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAwDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFIDSlPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:PRK11160 439 PNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILEL 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLLSH 584
Cdd:PRK11160 518 LAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQR 573
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
370-576 |
3.78e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 133.68 E-value: 3.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPY-EGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVsEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:PRK10789 414 PDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQG 576
Cdd:PRK10789 494 LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
370-562 |
1.54e-31 |
|
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: 122.19 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGF-LPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFyQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:cd03248 113 QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQA 192
|
170 180 190
....*....|....*....|....*....|....
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLI 562
Cdd:cd03248 193 LYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
146-584 |
1.35e-28 |
|
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: 121.00 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 146 LSATIPMMILITLFPINWAAALILLVTaplIPVFMALVGLGAADANRRNFLAL---SRLSGDFLDRLRGLETIRFFHRGR 222
Cdd:TIGR01193 278 LDMWILVIVGLFLVRQNMLLFLLSLLS---IPVYAVIIILFKRTFNKLNHDAMqanAVLNSSIIEDLNGIETIKSLTSEA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 223 EEVKQIDDATEDFRSRTMEVLRMAFLSSAvLEFFAAISIAVVAVYFGfSYLGELNFGSYGMGVTlFAGFIALILAPefFQ 302
Cdd:TIGR01193 355 ERYSKIDSEFGDYLNKSFKYQKADQGQQA-IKAVTKLILNVVILWTG-AYLVMRGKLTLGQLIT-FNALLSYFLTP--LE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 303 PLRDLGTYYHAKAQAVGAAESLFTLLSAENNDDELpgTEPLTPAEQIAVTatDLVIFAPSGEKLAGPLNFTLNAGQRIAL 382
Cdd:TIGR01193 430 NIINLQPKLQAARVANNRLNEVYLVDSEFINKKKR--TELNNLNGDIVIN--DVSYSYGYGSNILSDISLTIKMNSKTTI 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 383 VGQSGAGKSSLLNLLLG-FLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRL-SRPDASAEEITAVM 460
Cdd:TIGR01193 506 VGMSGSGKSTLAKLLVGfFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAAC 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 461 EKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHqQTTLL 540
Cdd:TIGR01193 586 EIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIF 664
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 802097265 541 VTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLLSH 584
Cdd:TIGR01193 665 VAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
316-577 |
1.89e-27 |
|
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: 116.77 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 316 QAVGAAESLFTLLSAENNDDElpgTEPLtPAEQIAVTATDLVIFAPSGEK--LAGpLNFTLNAGQRIALVGQSGAGKSSL 393
Cdd:COG4618 300 SARQAYRRLNELLAAVPAEPE---RMPL-PRPKGRLSVENLTVVPPGSKRpiLRG-VSFSLEPGEVLGVIGPSGSGKSTL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 394 LNLLL-GFLPYEGSIRINQQELRDIRPEswrtQL-SWVG---QNPHLPEQTILDNI-RLsrPDASAEEITAVMEKAYVTD 467
Cdd:COG4618 375 ARLLVgVWPPTAGSVRLDGADLSQWDRE----ELgRHIGylpQDVELFDGTIAENIaRF--GDADPEKVVAAAKLAGVHE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 468 FIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEA-AHQQTTLLVTH--- 543
Cdd:COG4618 449 MILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHrps 528
|
250 260 270
....*....|....*....|....*....|....*...
gi 802097265 544 LLEETrdyDEVWVMDKGLIIEQGS----YAALQQQQGA 577
Cdd:COG4618 529 LLAAV---DKLLVLRDGRVQAFGPrdevLARLARPAAA 563
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
369-515 |
5.72e-26 |
|
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: 103.88 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKSSLLNL-LLGFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHL-PEQTILDNIRL 446
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLiAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLfPRLTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802097265 447 SRP------DASAEEITAVMEKAyvtdfidSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSA 515
Cdd:pfam00005 83 GLLlkglskREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
357-570 |
5.88e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 112.06 E-value: 5.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 357 VIFAPSGEK---LAGpLNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYE-GSIRINQQELRDIRPESWRTQLSWVGQN 432
Cdd:TIGR01842 322 VTIVPPGGKkptLRG-ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTsGSVRLDGADLKQWDRETFGKHIGYLPQD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 433 PHLPEQTILDNIRLSRPDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDE 512
Cdd:TIGR01842 401 VELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802097265 513 PSASLDAHSEERVMHALNEA-AHQQTTLLVTH---LLEetrdydevwVMDKGLIIEQGSYAA 570
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALkARGITVVVITHrpsLLG---------CVDKILVLQDGRIAR 533
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
370-578 |
1.89e-24 |
|
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: 108.88 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLN-LLLGFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRlSR 448
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLgLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PF 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:TIGR00957 1384 SQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 1463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAF 578
Cdd:TIGR00957 1464 IRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
348-579 |
1.17e-22 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 101.52 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 348 QIAVTATDLVIFAPSGEKLA-GPLNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLP----YEGSIRINQQELRDIRPESW 422
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAvDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 423 RTQLSWVGQNP--HLPEQTILDNI-------RLSRPDAsAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQ 493
Cdd:COG1123 82 GRRIGMVFQDPmtQLNPVTVGDQIaealenlGLSRAEA-RARVLELLEAVGLERRLDRYP-----------HQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 494 RIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNE--AAHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAA 570
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEE 229
|
....*....
gi 802097265 571 LQQQQGAFA 579
Cdd:COG1123 230 ILAAPQALA 238
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
370-557 |
2.82e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 102.03 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFL-PYEGSIRIN-QQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLS 447
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 448 --------------RPDASA-------------------------------------------EEITAVMEKAYVTDFID 470
Cdd:PTZ00265 484 lyslkdlealsnyyNEDGNDsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdSEVVDVSKKVLIHDFVS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 471 SLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALN--EAAHQQTTLLVTHLLEET 548
Cdd:PTZ00265 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
....*....
gi 802097265 549 RDYDEVWVM 557
Cdd:PTZ00265 644 RYANTIFVL 652
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
371-562 |
3.98e-22 |
|
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: 94.86 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSL-LNLLLGFLPYEGSIRINQQELRDIRPESW----RTQLSWVGQNPHL-PEQTILDNI 444
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLlNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFNLlPDLTALENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 RL------SRPDASAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASLD 518
Cdd:cd03255 104 ELplllagVPKKERRERAEELLERVGLGDRLNHYP-----------SELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 802097265 519 AHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDYDEVWVMDKGLI 562
Cdd:cd03255 173 SETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
370-565 |
1.57e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 93.57 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKS----------SllnlllgflPYEGSIRINQQ--------ELRDIRpeswRTQLSWVGQ 431
Cdd:COG1136 27 VSLSIEAGEFVAIVGPSGSGKStllnilggldR---------PTSGEVLIDGQdisslserELARLR----RRHIGFVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 432 NPHL-PEQTILDNIRL------SRPDASAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNP 504
Cdd:COG1136 94 FFNLlPELTALENVALplllagVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802097265 505 CHLLLLDEPSASLDAHSEERVMHALNEAAHQ--QTTLLVTHLLEETRDYDEVWVMDKGLIIEQ 565
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
369-558 |
3.51e-21 |
|
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: 91.77 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDiRPESWRTQLSWVGQNPHL-PEQTILDNI-- 444
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAgLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLkPELTVRENLrf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 --RLSRPDASAEEITAVMEKAYVTDFIDSLpdgvntvvgdnAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSE 522
Cdd:COG4133 99 waALYGLRADREAIDEALEAVGLAGLADLP-----------VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 802097265 523 ERVMHALNE-AAHQQTTLLVTHLLEETRDYDEVWVMD 558
Cdd:COG4133 168 ALLAELIAAhLARGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
370-566 |
9.25e-21 |
|
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: 89.68 E-value: 9.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRpESWRTQLSWVGQNPHLPEQTILDNIrlsr 448
Cdd:cd03247 21 LSLELKQGEKIALLGRSGSGKSTLLQLLTgDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFDTTLRNNL---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 pdasaeeitavmekayvtdfidslpdgvntvvgdnAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:cd03247 96 -----------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQG 566
Cdd:cd03247 141 IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
381-567 |
2.56e-20 |
|
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: 89.93 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 381 ALVGQSGAGKSS------LLNLLLGFLPYEGSIRINQQELR--DIRPESWRTQLSWVGQNPHLPEQTILDNIRL------ 446
Cdd:cd03260 30 ALIGPSGCGKSTllrllnRLNDLIPGAPDEGEVLLDGKDIYdlDVDVLELRRRVGMVFQKPNPFPGSIYDNVAYglrlhg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 447 SRPDASAEEITA-VMEKAYvtdfidsLPDGVNTVVgdNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERV 525
Cdd:cd03260 110 IKLKEELDERVEeALRKAA-------LWDEVKDRL--HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 802097265 526 MHALNEAAHQQTTLLVTHLLEE-TRDYDEVWVMDKGLIIEQGS 567
Cdd:cd03260 181 EELIAELKKEYTIVIVTHNMQQaARVADRTAFLLNGRLVEFGP 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
369-576 |
2.76e-20 |
|
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: 90.30 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKSSLL-NLLLGFLPYEGSIRINQQELRdIRPESWRTQLSWVGQNPHLPE-QTILDNIRL 446
Cdd:COG4555 19 DVSFTAKDGEITGLLGPNGAGKTTLLrMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGVLPDERGLYDrLTVRENIRY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 447 ------SRPDASAEEITAVMEKAYVTDFIDSlpdgvntvvgdNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAH 520
Cdd:COG4555 98 faelygLFDEELKKRIEELIELLGLEEFLDR-----------RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 521 SEERVMHALNEAAHQQTTLLV-THLLEE-TRDYDEVWVMDKGLIIEQGSYAALQQQQG 576
Cdd:COG4555 167 ARRLLREILRALKKEGKTVLFsSHIMQEvEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
370-560 |
7.99e-20 |
|
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: 87.91 E-value: 7.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSS-LLNLLLGFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPH--LPEQTILD---- 442
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTlLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDdqFFGPTVEEevaf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 443 ---NIRLSRPDAsAEEITAVMEKAYVTDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLLDEPSASLDA 519
Cdd:cd03225 100 gleNLGLPEEEI-EERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 802097265 520 HSEERVMHALNEAAHQQTTLL-VTHLLEETRDY-DEVWVMDKG 560
Cdd:cd03225 168 AGRRELLELLKKLKAEGKTIIiVTHDLDLLLELaDRVIVLEDG 210
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
26-322 |
1.42e-19 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 89.52 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 26 LSMLLGVLSGLLIIGQAWCLAVLLQSLIMEHVPREQLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTVLDK 105
Cdd:cd18778 3 LTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 106 LEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVFMALVGL 185
Cdd:cd18778 83 LQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 186 GAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFFAAISIAVVa 265
Cdd:cd18778 163 KVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLV- 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 266 VYFG--FSYLGELNFGsygmgvTLFAGFIALILapeFFQPLRDLGTYYHAKAQAVGAAE 322
Cdd:cd18778 242 LGFGgrLVLAGELTIG------DLVAFLLYLGL---FYEPITSLHGLNEMLQRALAGAE 291
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
370-560 |
1.68e-19 |
|
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: 87.14 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINqqelrdirpeswrTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVSVP-------------GSIAYVSQEPWIQNGTIRENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 P-DAsaEEITAVMEK-AYVTDfIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVM 526
Cdd:cd03250 91 PfDE--ERYEKVIKAcALEPD-LEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIF 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 802097265 527 -HALNEA-AHQQTTLLVTHLLEETRDYDEVWVMDKG 560
Cdd:cd03250 168 eNCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
359-567 |
3.03e-19 |
|
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: 86.31 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 359 FAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPE 437
Cdd:cd03369 16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 438 QTILDNirLSRPDA-SAEEITAVMekayvtdfidSLPDGvntvvGDNaarLSVGQAQRIAVARALLNPCHLLLLDEPSAS 516
Cdd:cd03369 96 GTIRSN--LDPFDEySDEEIYGAL----------RVSEG-----GLN---LSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 802097265 517 LDAHSEERVMHALNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGS 567
Cdd:cd03369 156 IDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
369-566 |
3.14e-19 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 86.79 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPE---SWRTQLSWVGQNPHL---PEQTIL 441
Cdd:cd03257 23 DVSFSIKKGETLGLVGESGSGKSTLARAILgLLKPTSGSIIFDGKDLLKLSRRlrkIRRKEIQMVFQDPMSslnPRMTIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 442 DNI----RLSRPDASAEEITAVMEKAYV-----TDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDE 512
Cdd:cd03257 103 EQIaeplRIHGKLSKKEARKEAVLLLLVgvglpEEVLNRYP-----------HELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 513 PSASLDAHSEERVMHALNE--AAHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQG 566
Cdd:cd03257 172 PTSALDVSVQAQILDLLKKlqEELGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
369-560 |
3.47e-19 |
|
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: 84.60 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKSS-LLNLLLGFLPYEGSIRINQQELRDIRPESWRTQLSWVGQnphlpeqtildnirls 447
Cdd:cd00267 17 NVSLTLKAGEIVALVGPNGSGKSTlLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 448 rpdasaeeitavmekayvtdfidslpdgvntvvgdnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMH 527
Cdd:cd00267 81 ---------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....*
gi 802097265 528 ALNE-AAHQQTTLLVTHLLEETRDY-DEVWVMDKG 560
Cdd:cd00267 122 LLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
145-543 |
8.15e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.87 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 145 TLSATIPMMILITLFPINWAAALILLVTAPLIPVFMALVG--LgaadaNRRNFLALsRLSGDF---LDRLR-GLETIRFF 218
Cdd:COG4178 164 SLSGSLTFTLGGYSITIPGYMVWAALIYAIIGTLLTHLIGrpL-----IRLNFEQQ-RREADFrfaLVRVReNAESIALY 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 219 HRGREEVKQI----DDATEDFRSRTMEVLRMAFLSSAVLEFFAAISIAVVAVYFgFSylGELNFGSYGMGVTLFAGFI-A 293
Cdd:COG4178 238 RGEAAERRRLrrrfDAVIANWRRLIRRQRNLTFFTTGYGQLAVIFPILVAAPRY-FA--GEITLGGLMQAASAFGQVQgA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 294 LILAPEFFQPLRDLgtyyhakaQAVgaAESLFTLLSA-ENNDDELPGTEPLTPAEQIAVTATDLVIFAPSGEKLAGPLNF 372
Cdd:COG4178 315 LSWFVDNYQSLAEW--------RAT--VDRLAGFEEAlEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 373 TLNAGQRIALVGQSGAGKSSLLNLLLGFLPY-EGSIRinqqelrdiRPESWRtqLSWVGQNPHLPEQTILDNirLSRPDA 451
Cdd:COG4178 385 SLKPGERLLITGPSGSGKSTLLRAIAGLWPYgSGRIA---------RPAGAR--VLFLPQRPYLPLGTLREA--LLYPAT 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 452 ----SAEEITAVMEKAYVTDFIDSLpdgvnTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMH 527
Cdd:COG4178 452 aeafSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
410
....*....|....*.
gi 802097265 528 ALNEAAHQQTTLLVTH 543
Cdd:COG4178 527 LLREELPGTTVISVGH 542
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
28-322 |
9.47e-19 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 87.06 E-value: 9.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 28 MLLGVLSGLLIIGQAWCLAVLLQSLIMEH-VPREQLLTPFTVLVILFIARAVVAAIrerVGFI-------CGQVVRRDIR 99
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYiVPGQGDLQGLLLLALLYLGLLLLSFL---LQYLqtyllqkLGQRIIYDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 100 RTVLDKLEQLgPVRVKGK-PAGSWATII---LEQIDDMqdyYSRYLPQMtLSATIPM-MILITLFPINWAAALILLVTAP 174
Cdd:cd18544 78 RDLFSHIQRL-PLSFFDRtPVGRLVTRVtndTEALNEL---FTSGLVTL-IGDLLLLiGILIAMFLLNWRLALISLLVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 175 LIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLE 254
Cdd:cd18544 153 LLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 255 FFAAISIAVVAVYFGFSYL-GELNFGsygmgvTLFAgFIALILapEFFQPLRDLGTYYHAKAQAVGAAE 322
Cdd:cd18544 233 LLSSLALALVLWYGGGQVLsGAVTLG------VLYA-FIQYIQ--RFFRPIRDLAEKFNILQSAMASAE 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
311-567 |
1.47e-18 |
|
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: 88.81 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 311 YHAKAQAVGAAESLFT----LLSAENNDDELPGTEPLTPAEQIAVTATDLVIFAPSGEKLAGP----LNFTLNAGQRIAL 382
Cdd:COG1123 217 DDGRIVEDGPPEEILAapqaLAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRavddVSLTLRRGETLGL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 383 VGQSGAGKSSLL-NLLLGFLPYEGSIRINQQELRDIRPESWRTQLSWVG---QNPHL---PEQTILDNI-------RLSR 448
Cdd:COG1123 297 VGESGSGKSTLArLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQmvfQDPYSslnPRMTVGDIIaeplrlhGLLS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKayV---TDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERV 525
Cdd:COG1123 377 RAERRERVAELLER--VglpPDLADRYP-----------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 802097265 526 MHALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:COG1123 444 LNLLRDLQRELglTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGP 488
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
370-562 |
1.58e-18 |
|
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: 84.50 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLL-NLLLGFLPYEGSIRINQQELRDIRPE--SWRTQLSWVGQNPHL-PEQTILDNIR 445
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLrCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMVFQQFNLfPHLTVLENIT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 446 LS------RPDASAEEIT-AVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASLD 518
Cdd:cd03262 99 LApikvkgMSKAEAEERAlELLEKVGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 802097265 519 AHSEERVMHALNEAAHQQTT-LLVTHLLEETRDY-DEVWVMDKGLI 562
Cdd:cd03262 168 PELVGEVLDVMKDLAEEGMTmVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
371-582 |
3.21e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.04 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPEswRTQLSWVGQN----PHLpeqTILDNI- 444
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAgFLPPDSGRILWNGQDLTALPPA--ERPVSMLFQEnnlfPHL---TVAQNIg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 -------RLSRPDASAeeITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASL 517
Cdd:COG3840 94 lglrpglKLTAEQRAQ--VEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802097265 518 D-AHSEErvMHAL-NE--AAHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAALQQQQG--AFAQLL 582
Cdd:COG3840 161 DpALRQE--MLDLvDElcRERGLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLDGEPppALAAYL 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
371-587 |
2.26e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.24 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYEGsIRINQQELRDIRpeswrTQLSWVGQNPHLPEQTILDNIRLSRPD 450
Cdd:PTZ00265 1249 NVGMKNVNEFSLTKEGGSGEDSTVFKNSGKILLDG-VDICDYNLKDLR-----NLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 451 ASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSE---ERVMH 527
Cdd:PTZ00265 1323 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEkliEKTIV 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 528 ALNEAAhQQTTLLVTHLLEETRDYDEVWVMDKGliIEQGSYAalqQQQGAFAQLLSHRTG 587
Cdd:PTZ00265 1403 DIKDKA-DKTIITIAHRIASIKRSDKIVVFNNP--DRTGSFV---QAHGTHEELLSVQDG 1456
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
370-584 |
5.43e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.83 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSIRINQQEL--------RDIRpeSWRTQLSWVGQNPHL-PEQT 439
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPRSGTLNIAGNHFdfsktpsdKAIR--ELRRNVGMVFQQYNLwPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 440 ILDNI--------RLSRPDASAEEItAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLD 511
Cdd:PRK11124 99 VQQNLieapcrvlGLSKDQALARAE-KLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 512 EPSASLDAHSEERVMHALNEAAHQQ-TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAALQQ-QQGAFAQLLSH 584
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKTaSRVVYMENGHIVEQGDASCFTQpQTEAFKNYLSH 242
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
371-574 |
7.58e-17 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 80.30 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPE---SWRTQLSWVGQNPHL-PEQTILDNI- 444
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNgLVEPTSGSVLIDGTDINKLKGKalrQLRRQIGMIFQQFNLiERLSVLENVl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 --RLSR-----------PDASAEEITAVMEKAYVTDFIDSlpdgvntvvgdNAARLSVGQAQRIAVARALLNPCHLLLLD 511
Cdd:cd03256 101 sgRLGRrstwrslfglfPKEEKQRALAALERVGLLDKAYQ-----------RADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 512 EPSASLDAHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAALQQQ 574
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYaDRIVGLKDGRIVFDGPPAELTDE 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
230-582 |
1.24e-16 |
|
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: 83.84 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 230 DATEDFRSRTMEVLRMAFLSSAVLEFFAAISIAVVAV--YFGFSYLGELNFgsygmgVTLFAGFIALILAPEFFQPLRDL 307
Cdd:TIGR00957 520 DKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALitFAVYVTVDENNI------LDAEKAFVSLALFNILRFPLNIL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 308 GTYYHAKAQAVGAAESLFTLLSAENNDDELPGTEPLTPAEQIAVTATDLVI-FAPSGEKLAGPLNFTLNAGQRIALVGQS 386
Cdd:TIGR00957 594 PMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSITVHNATFtWARDLPPTLNGITFSIPEGALVAVVGQV 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 387 GAGKSSLLNLLLGFL-PYEGSIRInqqelrdirpeswRTQLSWVGQNPHLPEQTILDNIRLSRPdASAEEITAVMEKAYV 465
Cdd:TIGR00957 674 GCGKSSLLSALLAEMdKVEGHVHM-------------KGSVAYVPQQAWIQNDSLRENILFGKA-LNEKYYQQVLEACAL 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 466 TDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVM-HALNEAA--HQQTTLLVT 542
Cdd:TIGR00957 740 LPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGvlKNKTRILVT 819
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 802097265 543 HLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLL 582
Cdd:TIGR00957 820 HGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
370-582 |
1.31e-16 |
|
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: 79.95 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLP-YEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRLSR 448
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 pDASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:cd03288 120 -KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKV 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 802097265 529 LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAAL-QQQQGAFAQLL 582
Cdd:cd03288 199 VMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLlAQEDGVFASLV 253
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
357-560 |
1.69e-16 |
|
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: 77.26 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 357 VIFAPSGEK---LAGpLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQN 432
Cdd:cd03246 6 VSFRYPGAEppvLRN-VSFSIEPGESLAIIGPSGSGKSTLARLILgLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 433 PHLPEQTILDNIrlsrpdasaeeitavmekayvtdfidslpdgvntvvgdnaarLSVGQAQRIAVARALLNPCHLLLLDE 512
Cdd:cd03246 85 DELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 802097265 513 PSASLDAHSEERVMHALNEA-AHQQTTLLVTHLLEETRDYDEVWVMDKG 560
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
370-547 |
2.69e-16 |
|
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: 78.28 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPeswrtQLSWVGQNPHL-PEQTILDNIRLS 447
Cdd:cd03293 23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAgLERPTSGEVLVDGEPVTGPGP-----DRGYVFQQDALlPWLTVLDNVALG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 448 -----RPDASAEEIT-AVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHS 521
Cdd:cd03293 98 lelqgVPKAEARERAeELLELVGLSGFENAYP-----------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALT 166
|
170 180
....*....|....*....|....*....
gi 802097265 522 EERvMHALNEAA---HQQTTLLVTHLLEE 547
Cdd:cd03293 167 REQ-LQEELLDIwreTGKTVLLVTHDIDE 194
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
351-584 |
2.84e-16 |
|
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: 79.13 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 351 VTATDLVI-FAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYEGSIRINQQELRDIRPESWRTQLSWV 429
Cdd:cd03289 3 MTVKDLTAkYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 430 GQNPHLPEQTILDNIRlsrPDA--SAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHL 507
Cdd:cd03289 83 PQKVFIFSGTFRKNLD---PYGkwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 508 LLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLLSH 584
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISP 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
370-567 |
3.25e-16 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 78.01 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSIRINQQELRDIRPESWRTQLSWVG---QNPHLPEQ-TILDNI 444
Cdd:cd03258 24 VSLSVPKGEIFGIIGRSGAGKSTLIRCInGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGmifQHFNLLSSrTVFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 rlsrpdASAEEItAVMEKAYVTDFIDSLPDGVNtvVGDNA----ARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAH 520
Cdd:cd03258 104 ------ALPLEI-AGVPKAEIEERVLELLELVG--LEDKAdaypAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 802097265 521 SEERVMHALNEaAHQQ---TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:cd03258 175 TTQSILALLRD-INRElglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGT 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
370-587 |
3.96e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 82.33 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYE-GSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIrlsr 448
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---- 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 pDASAEEITA----VMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEER 524
Cdd:PLN03232 1331 -DPFSEHNDAdlweALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802097265 525 VMHALNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLLSHRTG 587
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTG 1472
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
369-566 |
4.76e-16 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 77.17 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPEswRTQLSWVGQNPHL-PEQTILDNIRL 446
Cdd:cd03259 18 DLSLTVEPGEFLALLGPSGCGKTTLLRLIAgLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALfPHLTVAENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 447 ---SRPDASAEEITAVMEKAYVTDFIDSLPDGVNTvvgdnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEE 523
Cdd:cd03259 96 glkLRGVPKAEIRARVRELLELVGLEGLLNRYPHE--------LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLRE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 802097265 524 RVMHALNE--AAHQQTTLLVTHLLEET-RDYDEVWVMDKGLIIEQG 566
Cdd:cd03259 168 ELREELKElqRELGITTIYVTHDQEEAlALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
369-547 |
1.24e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 77.05 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKSS--------LLnlllgflPYEGSIRINQQELRDIRPEswrtqLSWVGQNPHL-PEQT 439
Cdd:COG1116 29 DVSLTVAAGEFVALVGPSGCGKSTllrliaglEK-------PTSGEVLVDGKPVTGPGPD-----RGVVFQEPALlPWLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 440 ILDNIRLS------RPDASAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEP 513
Cdd:COG1116 97 VLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEP 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 802097265 514 SASLDAHSEERVMHALNE--AAHQQTTLLVTHLLEE 547
Cdd:COG1116 166 FGALDALTRERLQDELLRlwQETGKTVLFVTHDVDE 201
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
26-324 |
1.37e-15 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 77.46 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 26 LSMLLGVLSGLLIIGQAWCLAVLLQSLIMEHVPREQLLTPFtVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTVLDK 105
Cdd:cd18552 3 LAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPL-AIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 106 LEQLGPVRVKGKPAGSWATIILEQIDDMQDyysrylpqmTLSATIPMMI---------LITLFPINWAAALILLVTAPLI 176
Cdd:cd18552 82 LLRLPLSFFDRNSSGDLISRITNDVNQVQN---------ALTSALTVLVrdpltviglLGVLFYLDWKLTLIALVVLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 177 PVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFF 256
Cdd:cd18552 153 ALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 257 AAISIAVVAVYFGFSYL-GELNFGSygmgvtlFAGFIALILApeFFQPLRDLGTYYHAKAQAVGAAESL 324
Cdd:cd18552 233 GAIAIALVLWYGGYQVIsGELTPGE-------FISFITALLL--LYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
370-562 |
3.20e-15 |
|
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: 73.59 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDiRPESWRTQLSWVGQNPHLPEQ-TILDNIRLS 447
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILgLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTVRENLKLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 448 RpdasaeeitavmekayvtdfidslpdgvntvvgdnaarlsvGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMH 527
Cdd:cd03230 98 G-----------------------------------------GMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 802097265 528 ALNEAAHQQTT-LLVTHLLEETRDY-DEVWVMDKGLI 562
Cdd:cd03230 137 LLRELKKEGKTiLLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
370-560 |
3.40e-15 |
|
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: 75.06 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESW----RTQLSWVGQNPHLPEQTILDNI 444
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 RLSRPdASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEER 524
Cdd:cd03290 100 TFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 802097265 525 VMHA-----LNEaaHQQTTLLVTHLLEETRDYDEVWVMDKG 560
Cdd:cd03290 179 LMQEgilkfLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
370-566 |
5.66e-15 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 73.24 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQnphlpeqtildnirlsr 448
Cdd:cd03214 18 LSLSIEAGEIVGILGPNGAGKSTLLKTLAgLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 pdasaeeitaVMEKAYVTDFIDSlpdGVNTvvgdnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:cd03214 81 ----------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLEL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 802097265 529 LNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQG 566
Cdd:cd03214 140 LRRLARERgkTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
370-566 |
8.23e-15 |
|
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: 74.29 E-value: 8.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPEswRTQLSWVGQNPHL-PEQTILDNI--- 444
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAgFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALfPHMTVYKNIayg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 ----RLSRPDASAE--EITAVMekayvtdfidslpdGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLD 518
Cdd:cd03299 96 lkkrKVDKKEIERKvlEIAEML--------------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 802097265 519 AHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQG 566
Cdd:cd03299 162 VRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALaDKVAIMLNGKLIQVG 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
361-567 |
8.24e-15 |
|
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: 74.26 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 361 PSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHL-PEQ 438
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLfPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 439 TILDNIRL---------SRPDASAEEITAVMekayvtdfidSLPDGvnTVVGDNAARLSVGQAQRIAVARALLNPCHLLL 509
Cdd:cd03295 91 TVEENIALvpkllkwpkEKIRERADELLALV----------GLDPA--EFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802097265 510 LDEPSASLDAHSEERV---MHALNEAAHqQTTLLVTHLLEET-RDYDEVWVMDKGLIIEQGS 567
Cdd:cd03295 159 MDEPFGALDPITRDQLqeeFKRLQQELG-KTIVFVTHDIDEAfRLADRIAIMKNGEIVQVGT 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
226-582 |
1.16e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.71 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 226 KQIDDATEDFRSRTMEVLRMAFLSSAVLEFFA-AISIAVVAVYFGFsylgelnFGSYGMGVTLFAGFIALILapefFQPL 304
Cdd:PLN03232 499 KSFESRIQGIRNEELSWFRKAQLLSAFNSFILnSIPVVVTLVSFGV-------FVLLGGDLTPARAFTSLSL----FAVL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 305 R-DLGTYYHAKAQAVGAAESLFT----LLSAENNDDELPGTEPLTPAEQI--AVTATDLVIFAPSgeklAGPLNFTLNAG 377
Cdd:PLN03232 568 RsPLNMLPNLLSQVVNANVSLQRieelLLSEERILAQNPPLQPGAPAISIknGYFSWDSKTSKPT----LSDINLEIPVG 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 378 QRIALVGQSGAGKSSLLNLLLGFLPY--EGSIRInqqelrdirpeswRTQLSWVGQNPHLPEQTILDNIRLSRPDASAEE 455
Cdd:PLN03232 644 SLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVI-------------RGSVAYVPQVSWIFNATVRENILFGSDFESERY 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 456 ITAVMEKAYVTDfIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA-LNEAAH 534
Cdd:PLN03232 711 WRAIDVTALQHD-LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELK 789
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 802097265 535 QQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLL 582
Cdd:PLN03232 790 GKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
370-543 |
1.22e-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: 73.21 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLL-NLLLGFLPYEGSIRINQQELRDIRPES---WRTQLSWVGQ-NPHLPEQTILDNI 444
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLkLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQdFRLLPDRNVYENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 RLS------RPDASAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASLD 518
Cdd:cd03292 100 AFAlevtgvPPREIRKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180
....*....|....*....|....*.
gi 802097265 519 AHSEERVMHALNEAAHQQTTLLV-TH 543
Cdd:cd03292 169 PDTTWEIMNLLKKINKAGTTVVVaTH 194
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
370-584 |
1.24e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 77.64 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRlsrP 449
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD---P 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 450 DA--SAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMH 527
Cdd:TIGR01271 1315 YEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRK 1394
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 528 ALNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLLSH 584
Cdd:TIGR01271 1395 TLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSA 1451
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
370-564 |
1.41e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 73.16 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLL-NLLLGFLPYEGSIRINQQELRDIRPES---WRTQLSWVGQNPHL-PEQTILDNI 444
Cdd:COG2884 21 VSLEIEKGEFVFLTGPSGAGKSTLLkLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRIGVVFQDFRLlPDRTVYENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 RLS------RPDASAEEITAVMEKAYVTDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLLDEPSASLD 518
Cdd:COG2884 101 ALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIARALVNRPELLLADEPTGNLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 802097265 519 AHSEERVMHALNEAAHQQTTLLV-TH---LLEETRDYdeVWVMDKGLIIE 564
Cdd:COG2884 170 PETSWEIMELLEEINRRGTTVLIaTHdleLVDRMPKR--VLELEDGRLVR 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
370-571 |
1.58e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.63 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSIRINQQELRDIRPES--------WRTQLSWVGQNPHL-PEQT 439
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQPEAGTIRVGDITIDTARSLSqqkglirqLRQHVGFVFQNFNLfPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 440 ILDNI------RLSRPDASAEEIT-AVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDE 512
Cdd:PRK11264 102 VLENIiegpviVKGEPKEEATARArELLAKVGLAGKETSYP-----------RRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802097265 513 PSASLDAHSEERVMHALNEAAHQQTTL-LVTHLLEETRDY-DEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQEKRTMvIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
363-544 |
1.92e-14 |
|
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: 72.14 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 363 GEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPeSWRTQLSWVGQNPHLPEQ-TI 440
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAgLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAPGIKTTlSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNIRLSRPDASAEEITAVMEKAYVTDFIDsLPdgvntvvgdnAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAH 520
Cdd:cd03231 91 LENLRFWHADHSDEQVEEALARVGLNGFED-RP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....*..
gi 802097265 521 SEERVMHALneAAHQQ---TTLLVTHL 544
Cdd:cd03231 160 GVARFAEAM--AGHCArggMVVLTTHQ 184
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
370-566 |
2.60e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.51 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELrdiRPES-W--RTQLSWVGQNPHlpEQTI----- 440
Cdd:PRK13635 26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNgLLLPEAGTITVGGMVL---SEETvWdvRRQVGMVFQNPD--NQFVgatvq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 ------LDNIRLSRPDAsAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPS 514
Cdd:PRK13635 101 ddvafgLENIGVPREEM-VERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 802097265 515 ASLDAHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDYDEVWVMDKGLIIEQG 566
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
347-554 |
4.40e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 347 EQIAVTATDLVIFAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLL-NLLLGFLPYEGSIRINQQELRDIRPESWRTQ 425
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLkIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 426 LSWVGQNPHLPEQTILDN------IRLSRPDasaeeitavmEKAYVTDFID-SLPDgvnTVVGDNAARLSVGQAQRIAVA 498
Cdd:PRK10247 83 VSYCAQTPTLFGDTVYDNlifpwqIRNQQPD----------PAIFLDDLERfALPD---TILTKNIAELSGGEKQRISLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 499 RALLNPCHLLLLDEPSASLDAHSEERV---MHALNEaAHQQTTLLVTHLLEETRDYDEV 554
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVneiIHRYVR-EQNIAVLWVTHDKDEINHADKV 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
370-582 |
5.39e-14 |
|
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: 72.58 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQElrdirpeSWRTQLSWVgqnphLPeQTILDNIRLSr 448
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGRI-------SFSSQFSWI-----MP-GTIKENIIFG- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 pdASAEEI--TAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVM 526
Cdd:cd03291 122 --VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIF 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 527 HA-LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLL 582
Cdd:cd03291 200 EScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
370-582 |
5.90e-14 |
|
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: 75.33 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQElrdirpeSWRTQLSWVgqnphLPeQTILDNIRLSr 448
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKIKHSGRI-------SFSPQTSWI-----MP-GTIKDNIIFG- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 pdASAEEI--TAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVM 526
Cdd:TIGR01271 511 --LSYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 527 HA-LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLL 582
Cdd:TIGR01271 589 EScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
371-566 |
7.16e-14 |
|
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: 70.79 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNA-----GQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIR------PEswRTQLSWVGQN----PH 434
Cdd:cd03297 12 DFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAgLEKPDGGTIVLNGTVLFDSRkkinlpPQ--QRKIGLVFQQyalfPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 435 LpeqTILDNIRLSRPDASAEEItavmeKAYVTDFIDSLpdGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPS 514
Cdd:cd03297 90 L---NVRENLAFGLKRKRNRED-----RISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 802097265 515 ASLDAHSEERVMHALNE--AAHQQTTLLVTHLLEET-RDYDEVWVMDKGLIIEQG 566
Cdd:cd03297 160 SALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
370-574 |
1.54e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYEGSIRINQQELRDIRPES---WRTQLSWVGQ------NPHLP-EQT 439
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQdpnsslNPRLNvLQI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 440 ILDNIRLSRPDASAEE----ITAVMEKayvtdfidslpdgvntvVG-DNAAR------LSVGQAQRIAVARALLNPCHLL 508
Cdd:PRK15134 385 IEEGLRVHQPTLSAAQreqqVIAVMEE-----------------VGlDPETRhrypaeFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802097265 509 LLDEPSASLDAHSEERVMHALN--EAAHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS----YAALQQQ 574
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKslQQKHQLAYLFISHDLHVVRALcHQVIVLRQGEVVEQGDcervFAAPQQE 520
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
371-567 |
1.74e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.20 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLN-LLLGFLPYEGSIRINQQEL------RDIRPesWRTQLSWVGQNP--HLPEQTIL 441
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQhLNGLLQPTSGTVTIGERVItagkknKKLKP--LRKKVGIVFQFPehQLFEETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 442 DNI-----RLSRPDASAEEITAVMEKayvtdfIDSLPDGVNTvvgDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSAS 516
Cdd:PRK13634 105 KDIcfgpmNFGVSEEDAKQKAREMIE------LVGLPEELLA---RSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 802097265 517 LDAHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGT 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
360-574 |
2.07e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 360 APSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRI------NQQELRDIRPEswRTQLSWVGQN 432
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNgLLQPTEGKVTVgdivvsSTSKQKEIKPV--RKKVGVVFQF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 433 P--HLPEQTIL-------DNIRLSRPDA---SAEEITAVmekAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARA 500
Cdd:PRK13643 93 PesQLFEETVLkdvafgpQNFGIPKEKAekiAAEKLEMV---GLADEFWEKSP-----------FELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 501 LLNPCHLLLLDEPSASLDAHSEERVMHaLNEAAHQ--QTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAALQQQ 574
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQsgQTVVLVTHLMDDVADYaDYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
370-562 |
3.73e-13 |
|
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: 68.71 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRpeswrTQLSWVGQNPHLPEQ---TILDNIR 445
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILgLLKPTSGSIRVFGKPLEKER-----KRIGYVPQRRSIDRDfpiSVRDVVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 446 LSR----------PDASAEEITAVMEKAYVTDFIDSlpdgvntvvgdNAARLSVGQAQRIAVARALLNPCHLLLLDEPSA 515
Cdd:cd03235 93 MGLyghkglfrrlSKADKAKVDEALERVGLSELADR-----------QIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 802097265 516 SLDAHSEERVMHALNE-AAHQQTTLLVTHLLEETRDY-DEVWVMDKGLI 562
Cdd:cd03235 162 GVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLNRTVV 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
370-585 |
4.02e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.16 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQEL------RDIRPesWRTQLSWVGQNP--HLPEQTI 440
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNgLHVPTQGSVRVDDTLItstsknKDIKQ--IRKKVGLVFQFPesQLFEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNIRLSRPD--ASAEEITAV-MEKAYVTDFIDSLPDgvntvvgDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASL 517
Cdd:PRK13649 104 LKDVAFGPQNfgVSQEEAEALaREKLALVGISESLFE-------KNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 518 DAHSEERVMhALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAALQQ--------QQG-----AFAQL 581
Cdd:PRK13649 177 DPKGRKELM-TLFKKLHQSgmTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKPKDIFQdvdfleekQLGvpkitKFAQR 255
|
....
gi 802097265 582 LSHR 585
Cdd:PRK13649 256 LADR 259
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
375-583 |
5.36e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 69.23 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 375 NAGQRIALVGQSGAGKSSLLN-LLLGFLPYEGSIRINQQELRDIRP-------------ESWRTQLSWVGQNPHL-PEQT 439
Cdd:PRK10619 29 NAGDVISIIGSSGSGKSTFLRcINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqlRLLRTRLTMVFQHFNLwSHMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 440 ILDNIR--------LSRPDASaEEITAVMEKAYVTDfidslpdgvnTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLD 511
Cdd:PRK10619 109 VLENVMeapiqvlgLSKQEAR-ERAVKYLAKVGIDE----------RAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 512 EPSASLDAHSEERVMHALNEAAHQ-QTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAAL--QQQQGAFAQLLS 583
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLfgNPQSPRLQQFLK 253
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
370-565 |
6.47e-13 |
|
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: 68.05 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPEswRTQLSWVGQNPHL-PEQTILDNI--- 444
Cdd:cd03301 19 LNLDIADGEFVVLLGPSGCGKTTTLRMIAgLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQNYALyPHMTVYDNIafg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 ---RLSRPDASAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAH- 520
Cdd:cd03301 97 lklRKVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKl 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 521 -----SEERVMHalneAAHQQTTLLVTHlleetrDYDE-------VWVMDKGlIIEQ 565
Cdd:cd03301 166 rvqmrAELKRLQ----QRLGTTTIYVTH------DQVEamtmadrIAVMNDG-QIQQ 211
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
376-567 |
9.64e-13 |
|
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: 68.09 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 376 AGQRIALVGQSGAGKSS------LLNLLLGFLPYEGSIRINQQELRD--IRPESWRTQLSWVGQNPHLPEQTILDNIRLS 447
Cdd:TIGR00972 26 KNQVTALIGPSGCGKSTllrslnRMNDLVPGVRIEGKVLFDGQDIYDkkIDVVELRRRVGMVFQKPNPFPMSIYDNIAYG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 448 ------RPDASAEEIT-AVMEKAyvtdfidSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAH 520
Cdd:TIGR00972 106 prlhgiKDKKELDEIVeESLKKA-------ALWDEVKDRLHDSALGLSGGQQQRLCIARALAVEPEVLLLDEPTSALDPI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 802097265 521 SEERVMHALNEAAHQQTTLLVTHLLEET-RDYDEVWVMDKGLIIEQGS 567
Cdd:TIGR00972 179 ATGKIEELIQELKKKYTIVIVTHNMQQAaRISDRTAFFYDGELVEYGP 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
370-562 |
1.30e-12 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 67.81 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSllnll-lgflPYEGSIRINQQELRDIRPeswrtQLSWVGQNPHLPEQ---TILDNI- 444
Cdd:COG1121 25 VSLTIPPGEFVAIVGPNGAGKSTllkailgllpPTSGTVRLFGKPPRRARR-----RIGYVPQRAEVDWDfpiTVRDVVl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 -----------RLSRPDAsaEEITAVMEKAYVTDFIDSLpdgvntvVGDnaarLSVGQAQRIAVARALLNPCHLLLLDEP 513
Cdd:COG1121 100 mgrygrrglfrRPSRADR--EAVDEALERVGLEDLADRP-------IGE----LSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 802097265 514 SASLDAHSEERVMHALNEAAHQQTT-LLVTHLLEETRDY-DEVWVMDKGLI 562
Cdd:COG1121 167 FAGVDAATEEALYELLRELRREGKTiLVVTHDLGAVREYfDRVLLLNRGLV 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
370-567 |
1.43e-12 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 67.75 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPEswRTQLSWVGQN----PHLpeqTILDNI 444
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAgLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHyalfRHM---TVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 --------RLSRPDAS--AEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPS 514
Cdd:cd03296 96 afglrvkpRSERPPEAeiRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 515 ASLDAHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGT 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
369-582 |
1.94e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.91 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTL--NAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPEswRTQLSWVGQN----PHLpeqTIL 441
Cdd:PRK10771 15 PMRFDLtvERGERVAILGPSGAGKSTLLNLIAgFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQEnnlfSHL---TVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 442 DNI--------RLSrpDASAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEP 513
Cdd:PRK10771 90 QNIglglnpglKLN--AAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802097265 514 SASLDAHSEERVMHALNEAAHQQ--TTLLVTHLLEET-RDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLL 582
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAaRIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
26-322 |
2.29e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 67.92 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 26 LSMLLGVLSGLLIigqawclaVLLQSLIMEHVPREQLLTPFTVLVILFI--------ARAVVAAIRERVGFICGQVVRRD 97
Cdd:cd18563 6 LLMLLGTALGLVP--------PYLTKILIDDVLIQLGPGGNTSLLLLLVlglagayvLSALLGILRGRLLARLGERITAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 98 IRRTVLDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIP 177
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 178 VFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFFA 257
Cdd:cd18563 158 WGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLT 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 258 AISIAVVaVYFGFSYL--GELNFGSygmgVTLFAGFIALilapeFFQPLRDLGTYYHAKAQAVGAAE 322
Cdd:cd18563 238 SLGTLIV-WYFGGRQVlsGTMTLGT----LVAFLSYLGM-----FYGPLQWLSRLNNWITRALTSAE 294
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
362-567 |
2.62e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 68.25 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 362 SGEKLAGPLNFTLNAGQRIALVGQSGAGKSS---------LlnlllgflPYEGSIRINQQELRdirpeswrTQLS----- 427
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTllriiagleT--------PDSGRIVLNGRDLF--------TNLPprerr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 428 --WVGQN----PHLpeqTILDNIR--LSRPDASAEEITA-VME--KAY-VTDFIDSLPdgvntvvgdnaARLSVGQAQRI 495
Cdd:COG1118 77 vgFVFQHyalfPHM---TVAENIAfgLRVRPPSKAEIRArVEEllELVqLEGLADRYP-----------SQLSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 496 AVARALLNPCHLLLLDEPSASLDAH--SE-ERVMHALNEAAHqQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKvrKElRRWLRRLHDELG-GTTVFVTHDQEEALELaDRVVVMNQGRIEQVGT 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
370-560 |
2.75e-12 |
|
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: 65.29 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLL-NLLLGFLPYEGSIRINQQEL---RDIRPESwRTQLSWVGQNPHL-PEQTILDNI 444
Cdd:cd03229 19 VSLNIEAGEIVALLGPSGSGKSTLLrCIAGLEEPDSGSILIDGEDLtdlEDELPPL-RRRIGMVFQDFALfPHLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 RLsrpdasaeeitavmekayvtdfidslpdgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEER 524
Cdd:cd03229 98 AL---------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 802097265 525 VMHALNE--AAHQQTTLLVTHLLEETRDY-DEVWVMDKG 560
Cdd:cd03229 139 VRALLKSlqAQLGITVVLVTHDLDEAARLaDRVVVLRDG 177
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
372-566 |
3.06e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.08 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 372 FTLN-------AGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSI-----RINQQELRDIRpeswrTQLSWVGQNPHlpEQ 438
Cdd:PRK13648 23 FTLKdvsfnipKGQWTSIVGHNGSGKSTIAKLMIgIEKVKSGEIfynnqAITDDNFEKLR-----KHIGIVFQNPD--NQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 439 TI-----------LDNIRLSRpDASAEEITAVMEKAYVTDFIDSLPDGvntvvgdnaarLSVGQAQRIAVARALLNPCHL 507
Cdd:PRK13648 96 FVgsivkydvafgLENHAVPY-DEMHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802097265 508 LLLDEPSASLDAHSEERVMHALNE--AAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQG 566
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
19-435 |
5.28e-12 |
|
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: 68.29 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 19 PARRWLRLSMLLGVLSGLLIIGqawCLAVLLQSLIMEHVPREQLLTPFTVLVILFIARAVVAAIR-ERVGF-----ICGQ 92
Cdd:COG4615 10 ESRWLLLLALLLGLLSGLANAG---LIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLlTRLGQhavarLRLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 93 VVRRdIRRTVLDKLEQLGPVRVkgkpagsWATIIlEQIDDMQDYYSRyLPQMTLSATIPMMILITLFPINWAAALILLVt 172
Cdd:COG4615 87 LSRR-ILAAPLERLERIGAARL-------LAALT-EDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFLLTLV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 173 aplipvFMALVGLGAADANRR--NFLALSR-----LSGDFLDRLRGLETIRFfHRGR------EEVKQIDDATEDFRSRT 239
Cdd:COG4615 156 ------LLGLGVAGYRLLVRRarRHLRRAReaedrLFKHFRALLEGFKELKL-NRRRrraffdEDLQPTAERYRDLRIRA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 240 MEVLRMAFLSSAVLeFFAAIsiavVAVYFGFSYLGELNfgsygmgVTLFAGFIALILapeF-FQPLRDLGTYYHAKAQAV 318
Cdd:COG4615 229 DTIFALANNWGNLL-FFALI----GLILFLLPALGWAD-------PAVLSGFVLVLL---FlRGPLSQLVGALPTLSRAN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 319 GAAESLFTLLSAENNDDELPGTEPLTPA----EQIAVTAtdlVIFAPSGEKLA-----GPLNFTLNAGQRIALVGQSGAG 389
Cdd:COG4615 294 VALRKIEELELALAAAEPAAADAAAPPApadfQTLELRG---VTYRYPGEDGDegftlGPIDLTIRRGELVFIVGGNGSG 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 802097265 390 KSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHL 435
Cdd:COG4615 371 KSTLAKLLTgLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHL 417
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
370-571 |
7.99e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.27 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNP--HLPEQTILDNIRL 446
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDgLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 447 SRPDASA--EEITAVMEKAYVT----DFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAH 520
Cdd:PRK13642 106 GMENQGIprEEMIKRVDEALLAvnmlDFKTREP-----------ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 802097265 521 SEERVMHALNEA--AHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK13642 175 GRQEIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
370-575 |
1.29e-11 |
|
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: 64.83 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLL-NLLLGFLPYEGSIRINQQELRDIRPE---SWRTQLSWVGQNPHL-PEQTILDNI 444
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLrLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMGMLFQSGALfDSLTVFENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 --------RLSRpdasaEEITA-VMEK-AYV--TDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDE 512
Cdd:cd03261 99 afplrehtRLSE-----EEIREiVLEKlEAVglRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 513 PSASLD---AHSEERVMHALNEaAHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAALQQQQ 575
Cdd:cd03261 163 PTAGLDpiaSGVIDDLIRSLKK-ELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRASD 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
370-567 |
1.49e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 65.24 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNL-LLGFLPYEGSIRI---------NQQELRDIRPEswrtqLSWVGQNP--HLPE 437
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHfNALLKPSSGTITIagyhitpetGNKNLKKLRKK-----VSLVFQFPeaQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 438 QTILDNIRL-------SRPDASAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLL 510
Cdd:PRK13641 101 NTVLKDVEFgpknfgfSEDEAKEKALKWLKKVGLSEDLISKSP-----------FELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802097265 511 DEPSASLDAHSEERVMHALNE---AAHqqTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDyqkAGH--TVILVTHNMDDVAEYaDDVLVLEHGKLIKHAS 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
370-571 |
1.80e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.19 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSIRINQ---------QELRDIRPEswrtqlswVGQNPHLPE-Q 438
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNInALLKPTTGTVTVDDitithktkdKYIRPVRKR--------IGMVFQFPEsQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 439 TILDNIR---LSRPDASAEEITAVMEKAYvtDFIDSLPDGVNtVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSA 515
Cdd:PRK13646 98 LFEDTVEreiIFGPKNFKMNLDEVKNYAH--RLLMDLGFSRD-VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 516 SLDAHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDEnkTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKEL 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
370-582 |
2.84e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLP--YEGSIRInqqelrdirpeswRTQLSWVGQNPHLPEQTILDNIRLS 447
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPprSDASVVI-------------RGTVAYVPQVSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 448 RPDASAEEITAVMEKAYVTDfIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMH 527
Cdd:PLN03130 703 SPFDPERYERAIDVTALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD 781
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 528 A-LNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQGAFAQLL 582
Cdd:PLN03130 782 KcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLM 837
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-566 |
3.09e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.78 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 351 VTATDLVIFAPSGEKLAGpLNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPY------EGSIRINQQELRDIRPESWRT 424
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDG-VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearvSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 425 QLSWVGQNPH-LPEQTILDNI----RLSRPDASAEEITA----VMEKAyvtdfidSLPDGVNTVVGDNAARLSVGQAQRI 495
Cdd:PRK14247 83 RVQMVFQIPNpIPNLSIFENValglKLNRLVKSKKELQErvrwALEKA-------QLWDEVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802097265 496 AVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTHLLEE-TRDYDEVWVMDKGLIIEQG 566
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQaARISDYVAFLYKGQIVEWG 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
358-571 |
4.11e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.60 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 358 IFAPSGE-KLAGPLNFTLNAGQRIALVGQSGAGKSSLL-NLLLGFLPYEGSIRINQQELRDIRPESW---RTQLSWVGQN 432
Cdd:PRK11308 21 LFKPERLvKALDGVSFTLERGKTLAVVGESGCGKSTLArLLTMIETPTGGELYYQGQDLLKADPEAQkllRQKIQIVFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 433 PHL---PEQTI--------LDNIRLSRPDaSAEEITAVMEKAYV-TDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARA 500
Cdd:PRK11308 101 PYGslnPRKKVgqileeplLINTSLSAAE-RREKALAMMAKVGLrPEHYDRYPH-----------MFSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802097265 501 LLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTT--LLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQI 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
370-571 |
4.29e-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: 65.48 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYEGSIRINQQEL-----RDIRPesWRTQLSWVGQNP-------HLPE 437
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLdglsrRALRP--LRRRMQVVFQDPfgslsprMTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 438 QTILDNIRLSRPDASAEE----ITAVMEKayvtdfidslpdgvntvVG-DNAAR------LSVGQAQRIAVARALLNPCH 506
Cdd:COG4172 383 QIIAEGLRVHGPGLSAAErrarVAEALEE-----------------VGlDPAARhrypheFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 507 LLLLDEPSASLDAHSEERVMHALNE--AAHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAAL 571
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDlqREHGLAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
368-566 |
5.11e-11 |
|
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: 62.60 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 368 GPLNFTLNAGQrIALVGQSGAGKSS-LLNLLLGFLPYEGSIRINQQELRDiRPESWRTQLSWVGQN----PHLPEQTILD 442
Cdd:cd03264 17 DGVSLTLGPGM-YGLLGPNGAGKTTlMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEfgvyPNFTVREFLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 443 NIrlsrpdASAEEITAVMEKAYVTDFIDSLpdGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSE 522
Cdd:cd03264 95 YI------AWLKGIPSKEVKARVDEVLELV--NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEER 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 802097265 523 ERVMHALNEAAHQQTTLLVTHLLEETRD-YDEVWVMDKGLIIEQG 566
Cdd:cd03264 167 IRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
370-565 |
5.25e-11 |
|
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: 63.29 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPES---WRTQLSWVGQ------NPHLP-EQ 438
Cdd:TIGR02769 30 VSLSIEEGETVGLLGRSGCGKSTLARLLLgLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQdspsavNPRMTvRQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 439 TILDNIR-LSRPDASAEE--ITAVMEKAYV-TDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPS 514
Cdd:TIGR02769 110 IIGEPLRhLTSLDESEQKarIAELLDMVGLrSEDADKLP-----------RQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 802097265 515 ASLDAHSEERVMHALNEAAHQQTT--LLVTHLLEETRDY-DEVWVMDKGLIIEQ 565
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFcQRVAVMDKGQIVEE 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
370-567 |
6.11e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 64.35 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSS--------LLnlllgflPYEGSIRINQQELRDIRPEswRTQLSWVGQN----PHLpe 437
Cdd:COG3842 24 VSLSIEPGEFVALLGPSGCGKTTllrmiagfET-------PDSGRILLDGRDVTGLPPE--KRNVGMVFQDyalfPHL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 438 qTILDNIR--LSRPDASAEEITAVMEKA--YV--TDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARAllnpchllllD 511
Cdd:COG3842 93 -TVAENVAfgLRMRGVPKAEIRARVAELleLVglEGLADRYPH-----------QLSGGQQQRVALARAlapeprvlllD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802097265 512 EPSASLDAHSEERVMHALneAAHQQ----TTLLVTHLLEEtr-dyDEVWVMDKGLIIEQGS 567
Cdd:COG3842 161 EPLSALDAKLREEMREEL--RRLQRelgiTFIYVTHDQEEalalaDRIAVMNDGRIEQVGT 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
344-567 |
6.82e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.09 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 344 TPAEQIAVTATDLVIFAPSGEKLA-GPLNFTLNAGQRIALVGQSGAGKSSLL-NLLLGFLPYEGSIRI-----NQQELRD 416
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENNAlKNVSFEINEGEYVAILGHNGSGKSTISkILTGLLKPQSGEIKIdgitiSKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 417 IrpeswRTQLSWVGQNPHlpEQTI-----------LDNIRLSRPDASAeEITAVMEKAYVTDFIDSLPDgvntvvgdnaa 485
Cdd:PRK13632 81 I-----RKKIGIIFQNPD--NQFIgatveddiafgLENKKVPPKKMKD-IIDDLAKKVGMEDYLDKEPQ----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 486 RLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQT-TLL-VTHLLEETRDYDEVWVMDKGLII 563
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLIsITHDMDEAILADKVIVFSEGKLI 221
|
....
gi 802097265 564 EQGS 567
Cdd:PRK13632 222 AQGK 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-566 |
1.15e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 381 ALVGQSGAGKSSLLNL------LLGFLPYEGSIRINQQEL--RDIRPESWRTQLSWVGQNPH-LPEQTILDNI----RLS 447
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTfnrlleLNEEARVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNpFPHLTIYDNVaigvKLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 448 RPDASAEEITAVMEKAYVTDfidSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMH 527
Cdd:PRK14267 114 GLVKSKKELDERVEWALKKA---ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 802097265 528 ALNEAAHQQTTLLVTHL-LEETRDYDEVWVMDKGLIIEQG 566
Cdd:PRK14267 191 LLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
370-567 |
1.45e-10 |
|
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: 61.23 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFL-PYEGSIRINQQELRDiRPESWRTQLSWVGQNPHL-PEQTILDNI--- 444
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVdDELTGWENLyih 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 -RL-----SRPDASAEEITAVMEkayVTDFIDSLpdgvntvvgdnAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLD 518
Cdd:cd03265 98 aRLygvpgAERRERIDELLDFVG---LLEAADRL-----------VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 802097265 519 AHSEE---RVMHALNEaAHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:cd03265 164 PQTRAhvwEYIEKLKE-EFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGT 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
370-565 |
1.54e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.79 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPY-EGSIRINQQELRdiRPESWRTQLSWVGQNPHL-PEQTILDNI--- 444
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQtSGHIRFHGTDVS--RLHARDRKVGFVFQHYALfRHMTVFDNIafg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 -----RLSRPDASA--EEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASL 517
Cdd:PRK10851 99 ltvlpRRERPNAAAikAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 802097265 518 DAHSEERVMHALNEaAHQQ---TTLLVTHLLEETRDY-DEVWVMDKGlIIEQ 565
Cdd:PRK10851 168 DAQVRKELRRWLRQ-LHEElkfTSVFVTHDQEEAMEVaDRVVVMSQG-NIEQ 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
372-567 |
2.36e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 372 FTLNAGQRIALVGQSGAGKSSLLNLLLGFLPY-EGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIRlsrP- 449
Cdd:PTZ00243 1331 FRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD---Pf 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 450 -DASAEEITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHL-LLLDEPSAS----LDAHSEE 523
Cdd:PTZ00243 1408 lEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGfILMDEATANidpaLDRQIQA 1487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 802097265 524 RVMHALneAAHqqTTLLVTHLLEETRDYDEVWVMDKGLIIEQGS 567
Cdd:PTZ00243 1488 TVMSAF--SAY--TVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
376-566 |
2.43e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.23 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 376 AGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPEswrTQLSWvgQNPHL-PEQTILDNIRLS-----R 448
Cdd:PRK11247 37 AGQFVAVVGRSGCGKSTLLRLLAgLETPSAGELLAGTAPLAEARED---TRLMF--QDARLlPWKKVIDNVGLGlkgqwR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDAsAEEITAVmekayvtdfidslpdGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSeeRV-MH 527
Cdd:PRK11247 112 DAA-LQALAAV---------------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT--RIeMQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 802097265 528 ALNEAAHQQ---TTLLVTHLLEETrdydeVWVMDKGLIIEQG 566
Cdd:PRK11247 174 DLIESLWQQhgfTVLLVTHDVSEA-----VAMADRVLLIEEG 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
350-567 |
2.78e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 350 AVTATDLVIFAPSGEKLA-GPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGS--------IRINQQELRDIRp 419
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPAlNDISFSIPRGSWTALIGHNGSGKSTISKLINgLLLPDDNPnskitvdgITLTAKTVWDIR- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 420 eswrTQLSWVGQNP--HLPEQTI-------LDNIRLSRPDAsAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVG 490
Cdd:PRK13640 84 ----EKVGIVFQNPdnQFVGATVgddvafgLENRAVPRPEM-IKIVRDVLADVGMLDYIDSEP-----------ANLSGG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 491 QAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNE--AAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGS 567
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
370-574 |
3.03e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.04 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQEL-------RDIrpeswrtqlSWVGQNPHL-PEQTI 440
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAgLEKPTEGQIFIDGEDVthrsiqqRDI---------CMVFQSYALfPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNI-----RLSRPdaSAEEITAVMEKAYVTD---FIDSLPDgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLLDE 512
Cdd:PRK11432 96 GENVgyglkMLGVP--KEERKQRVKEALELVDlagFEDRYVD-----------QISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 513 PSASLDAHSeERVMHALNEAAHQQ---TTLLVTHllEETRDY---DEVWVMDKGLIIEQGSYAALQQQ 574
Cdd:PRK11432 163 PLSNLDANL-RRSMREKIRELQQQfniTSLYVTH--DQSEAFavsDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
370-567 |
3.26e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 61.26 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSIRINQQELRDIRpESW--RTQLSWVGQNPhlpeqtilDNirl 446
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMnALLIPSEGKVYVDGLDTSDEE-NLWdiRNKAGMVFQNP--------DN--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 447 srpdasaEEITAVMEK--AYVTDFIDSLPDGVNTVVGDNAAR-------------LSVGQAQRIAVARALLNPCHLLLLD 511
Cdd:PRK13633 97 -------QIVATIVEEdvAFGPENLGIPPEEIRERVDESLKKvgmyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 512 EPSASLDAHSEERVMHALNE--AAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGS 567
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
369-566 |
3.34e-10 |
|
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: 60.20 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNF--TLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPEswRTQLSWVGQNPHL-PEQTILDNI 444
Cdd:cd03298 14 PMHFdlTFAQGEITAIVGPSGSGKSTLLNLIAgFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLfAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 RLSRP------DASAEEITAVMEKAYVTDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLLDEPSASLD 518
Cdd:cd03298 92 GLGLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 802097265 519 AHSEERVMHALNEAAHQQ--TTLLVTHLLEETRD-YDEVWVMDKGLIIEQG 566
Cdd:cd03298 161 PALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
361-543 |
3.71e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.82 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 361 PSGEKLAGPL---NFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESW----RTQLSWVGQN 432
Cdd:PRK10535 15 PSGEEQVEVLkgiSLDIYAGEMVAIVGASGSGKSTLMNILGcLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 433 PHL-PEQTILDNIRLSRPDASAEEiTAVMEKAyvTDFIDSLpdGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLD 511
Cdd:PRK10535 95 YHLlSHLTAAQNVEVPAVYAGLER-KQRLLRA--QELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190
....*....|....*....|....*....|....*
gi 802097265 512 EPSASLDAHSEERVM---HALNEAAHqqTTLLVTH 543
Cdd:PRK10535 170 EPTGALDSHSGEEVMailHQLRDRGH--TVIIVTH 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
370-571 |
4.84e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.11 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYEG--------SIRINQQELRDIRPESwrtqlSWVGQNPHL-PEQTI 440
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSgdlivdglKVNDPKVDERLIRQEA-----GMVFQQFYLfPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNI--------RLSRPDAS--AEEITAvmeKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLL 510
Cdd:PRK09493 95 LENVmfgplrvrGASKEEAEkqARELLA---KVGLAERAHHYP-----------SELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802097265 511 DEPSASLDA---HSEERVMHALNEAAhqQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK09493 161 DEPTSALDPelrHEVLKVMQDLAEEG--MTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVL 223
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
368-567 |
8.42e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 59.85 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 368 GPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQEL---------RDIR-----PEswrTQLswvgqN 432
Cdd:COG4167 30 KPVSFTLEAGQTLAIIGENGSGKSTLAKMLAgIIEPTSGEILINGHKLeygdykyrcKHIRmifqdPN---TSL-----N 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 433 PHLPEQTILD-----NIRLSrPDASAEEITAVMEKayvtdfIDSLPDGVNtvvgDNAARLSVGQAQRIAVARALLNPCHL 507
Cdd:COG4167 102 PRLNIGQILEeplrlNTDLT-AEEREERIFATLRL------VGLLPEHAN----FYPHMLSSGQKQRVALARALILQPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 508 LLLDEPSASLDAHSEERVMHALNEAahqQTTL-----LVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:COG4167 171 IIADEALAALDMSVRSQIINLMLEL---QEKLgisyiYVSQHLGIVKHIsDKVLVMHQGEVVEYGK 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
370-581 |
9.46e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 9.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYE-GSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNIrlsr 448
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELErGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---- 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 pDASAE----EITAVMEKAYVTDFIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEER 524
Cdd:PLN03130 1334 -DPFNEhndaDLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDAL 1412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 525 VMHALNEAAHQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQQQG-AFAQL 581
Cdd:PLN03130 1413 IQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGsAFSKM 1470
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
370-572 |
1.07e-09 |
|
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: 58.99 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRP-ESWRTQLSWVGQNPHL-PEQTILDNIRL 446
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISgFLRPTSGSVLFDGEDITGLPPhEIARLGIGRTFQIPRLfPELTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 447 ---------SRPDASAEEITAVMEKAY-VTDFIDsLPDGVNTVVGDnaarLSVGQAQRIAVARALLNPCHLLLLDEPSAS 516
Cdd:cd03219 99 aaqartgsgLLLARARREEREARERAEeLLERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 517 LDAHSEERVMHALNE-AAHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAALQ 572
Cdd:cd03219 174 LNPEETEELAELIRElRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVR 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
370-567 |
1.30e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 59.68 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRD--IRPESWRTQLSWVGQNP--HLPEQTILDNI 444
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNgLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPeyQLFEETIEKDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 RL--SRPDASAEEITAVMEKAY------VTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSAS 516
Cdd:PRK13637 106 AFgpINLGLSEEEIENRVKRAMnivgldYEDYKDKSP-----------FELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 802097265 517 LDAHSEERVMHALNEaAHQQ---TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK13637 175 LDPKGRDEILNKIKE-LHKEynmTIILVSHSMEDVAKLaDRIIVMNKGKCELQGT 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
370-571 |
1.34e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPyEGSIRINQQELRD---IRPESWR-TQLSWVGQNPHL---PEQTILD 442
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILP-AGVRQTAGRVLLDgkpVAPCALRgRKIATIMQNPRSafnPLHTMHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 443 NIR-----LSRPDASAEeITAVMEKAyvtdfidSLPDgVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASL 517
Cdd:PRK10418 101 HARetclaLGKPADDAT-LTAALEAV-------GLEN-AARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 518 DAHSEERVMHALNEAAHQQT--TLLVTHLLE-ETRDYDEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRAlgMLLVTHDMGvVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
370-573 |
1.50e-09 |
|
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: 58.21 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESwRTQ--LSWVGQNPHL-PEQTILDNIR 445
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMgLLPPRSGSIRFDGRDITGLPPHE-RARagIGYVPEGRRIfPELTVEENLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 446 LSRPDASAEEITAVMEKAYvtDFIDSLPDGVNTVVGDnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERV 525
Cdd:cd03224 98 LGAYARRRAKRKARLERVY--ELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 802097265 526 MHALNE-AAHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAALQQ 573
Cdd:cd03224 172 FEAIRElRDEGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
370-567 |
1.73e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.96 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPEswRTQLSWVGQN----PHLpeqTILDNI 444
Cdd:PRK09452 33 LDLTINNGEFLTLLGPSGCGKTTVLRLIAgFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSyalfPHM---TVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 ----RLSRpdASAEEITA-VMEK---AYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSAS 516
Cdd:PRK09452 108 afglRMQK--TPAAEITPrVMEAlrmVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 517 LDaHSEERVMHalNEAAHQQTTL-----LVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK09452 175 LD-YKLRKQMQ--NELKALQRKLgitfvFVTHDQEEALTMsDRIVVMRDGRIEQDGT 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
369-569 |
2.38e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.65 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELrDIRPESWRTQ-LSWVGQNPHL---PEQTI--- 440
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAgMIEPTSGELLIDDHPL-HFGDYSYRSQrIRMIFQDPSTslnPRQRIsqi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LD-----NIRLSrPDASAEEITAVMEKayvtdfIDSLPDGVNTVvgdnAARLSVGQAQRIAVARALLNPCHLLLLDEPSA 515
Cdd:PRK15112 110 LDfplrlNTDLE-PEQREKQIIETLRQ------VGLLPDHASYY----PHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 516 SLDAHSEERVMHALNE--AAHQQTTLLVT-HLLEETRDYDEVWVMDKGLIIEQGSYA 569
Cdd:PRK15112 179 SLDMSMRSQLINLMLElqEKQGISYIYVTqHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
369-567 |
2.82e-09 |
|
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: 57.63 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPesWRTQLSWVGQN----PHLpeqTILDN 443
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAgFETPTSGEILLDGKDITNLPP--HKRPVNTVFQNyalfPHL---TVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 444 I----RLSRPDAS--AEEITAVMEKAYVTDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLLDEPSASL 517
Cdd:cd03300 93 IafglRLKKLPKAeiKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 802097265 518 DAHSEERVMHALNEaAHQQ---TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:cd03300 162 DLKLRKDMQLELKR-LQKElgiTFVFVTHDQEEALTMsDRIAVMNKGKIQQIGT 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
350-566 |
3.41e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.21 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 350 AVTATDLVIFAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLN-LLLGFLPYEGSIRINQQELRDiRPESW-RTQLS 427
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLhLNGIYLPQRGRVKVMGREVNA-ENEKWvRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 428 WVGQNP--HLPEQTILD-------NIRLsRPDASAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVA 498
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDdvafgpvNMGL-DKDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 499 RALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLV-THLLEETRDY-DEVWVMDKGLIIEQG 566
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVaTHDVDLAAEWaDQVIVLKEGRVLAEG 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
371-571 |
4.23e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.18 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLNLLLGFLP-YEGSIRINQQELRDIRPESW---RTQLSWVGQNPHL---PEQTILDN 443
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDPLAslnPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 444 I----RLSRPDASAEEIT----AVMEKayvtdfIDSLPDGVNTVvgdnAARLSVGQAQRIAVARALLNPCHLLLLDEPSA 515
Cdd:PRK15079 121 IaeplRTYHPKLSRQEVKdrvkAMMLK------VGLLPNLINRY----PHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 516 SLDAHSEERVMHALNE-----------AAHQQTtlLVTHLleetrdYDEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQlqremglslifIAHDLA--VVKHI------SDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
370-575 |
4.47e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 58.30 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDiRPESWRTQLSWVGQNPHL-PEQTILDNI--- 444
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILgMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLdLEFTVRENLlvf 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 -RLSRpdASAEEITAVMEKayVTDFIdSLPDGVNTVVGDnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSE- 522
Cdd:PRK13536 139 gRYFG--MSTREIEAVIPS--LLEFA-RLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARh 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 523 ---ERVMHALneaAHQQTTLLVTHLLEET-RDYDEVWVMDKGLIIEQGSYAALQQQQ 575
Cdd:PRK13536 210 liwERLRSLL---ARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
370-546 |
5.08e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDI----RPESWRTQLSWVGQNPHL-PEQTILDN 443
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGgLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQFHHLlPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 444 IRL-----SRPDASAEEITAVMEKAYvtdfidslpdGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLD 518
Cdd:PRK11629 108 VAMplligKKKPAEINSRALEMLAAV----------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|
gi 802097265 519 AHSEERVMHALNEAAHQQTT--LLVTHLLE 546
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
370-543 |
6.40e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPEsWRTQLSWVGqnpHLP----EQTILDNI 444
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAgLARPDAGEVLWQGEPIRRQRDE-YHQDLLYLG---HQPgiktELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 RLSRP---DASAEEITAVMEKAYVTDFIDsLPdgvntvvgdnAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHS 521
Cdd:PRK13538 96 RFYQRlhgPGDDEALWEALAQVGLAGFED-VP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180
....*....|....*....|...
gi 802097265 522 EERVMHALNE-AAHQQTTLLVTH 543
Cdd:PRK13538 165 VARLEALLAQhAEQGGMVILTTH 187
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
378-547 |
8.31e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.71 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 378 QRIALVGQSGAGKSSL------LNLLLGFLPYEGSIRINQQEL--RDIRPESWRTQLSWVGQNPHLPEQTILDNIRL-SR 448
Cdd:PRK14243 37 QITAFIGPSGCGKSTIlrcfnrLNDLIPGFRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYgAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDfidSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:PRK14243 117 INGYKGDMDELVERSLRQA---ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEEL 193
|
170
....*....|....*....
gi 802097265 529 LNEAAHQQTTLLVTHLLEE 547
Cdd:PRK14243 194 MHELKEQYTIIIVTHNMQQ 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-547 |
8.51e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 359 FAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYEGSIRIN------QQEL--RDIRPESWRTQLSWVG 430
Cdd:PRK14258 15 FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgrveffNQNIyeRRVNLNRLRRQVSMVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 431 QNPHLPEQTILDNIrlsrpdASAEEITAVMEKAYVTDFIDS------LPDGVNTVVGDNAARLSVGQAQRIAVARALLNP 504
Cdd:PRK14258 95 PKPNLFPMSVYDNV------AYGVKIVGWRPKLEIDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 802097265 505 CHLLLLDEPSASLDAHSEERVMHALNEAA--HQQTTLLVTHLLEE 547
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQ 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
370-566 |
9.06e-09 |
|
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: 56.13 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLP----YEGSIRINQQELRdirPESWRTQLSWVGQN----PHLP-EQTI 440
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggtTSGQILFNGQPRK---PDQFQKCVAYVRQDdillPGLTvRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNIRLSRPDASAEEITAVMekayvtDFIDSLPDGVNTVVGDNAAR-LSVGQAQRIAVARALLNPCHLLLLDEPSASLDA 519
Cdd:cd03234 103 TYTAILRLPRKSSDAIRKKR------VEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 802097265 520 HSEERVMHALNEAAHQQTTLLVThlLEETRD-----YDEVWVMDKGLIIEQG 566
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILT--IHQPRSdlfrlFDRILLLSSGEIVYSG 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
370-525 |
9.47e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.65 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPeswRTQLSWVG-QNPHLPEQTILDNIR-- 445
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAgLLPPAAGTIKLDGGDIDDPDV---AEACHYLGhRNAMKPALTVAENLEfw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 446 ---LSRPDASAEEITAVMEKAYVTDfidsLPdgvntvvgdnAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSE 522
Cdd:PRK13539 98 aafLGGEELDIAAALEAVGLAPLAH----LP----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
...
gi 802097265 523 ERV 525
Cdd:PRK13539 164 ALF 166
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
26-311 |
9.91e-09 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 56.71 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 26 LSMLLGVLSGLLIigqawclAVLLQSLIMEHVPR---EQLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTV 102
Cdd:cd18545 7 LLMLLSTAASLAG-------PYLIKIAIDEYIPNgdlSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 103 LDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVFMAL 182
Cdd:cd18545 80 FSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 183 VGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFFAAISIA 262
Cdd:cd18545 160 LRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 802097265 263 VVAVYFGFSYLGelnfGSYGMGV-TLFAGFIALilapeFFQPLRDLGTYY 311
Cdd:cd18545 240 LVYWYGGKLVLG----GAITVGVlVAFIGYVGR-----FWQPIRNLSNFY 280
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
487-567 |
1.13e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.78 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 487 LSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEA-AHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIE 564
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEVaDEVIVMDKGKILK 256
|
...
gi 802097265 565 QGS 567
Cdd:PRK13631 257 TGT 259
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
351-567 |
1.31e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.94 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 351 VTATDLVIFAPSGEKLAGpLNFTLNAGQRIALVGQSGAGKSSLLNL------LLGFLPYEGSIRINQQELRDIRPES--W 422
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNS-VSLDFYPNEITALIGPSGSGKSTLLRSinrmndLNPEVTITGSIVYNGHNIYSPRTDTvdL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 423 RTQLSWVGQNPHLPEQTILDNI----RLSrpdasAEEITAVMEKAYVTDFID-SLPDGVNTVVGDNAARLSVGQAQRIAV 497
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENVvyglRLK-----GIKDKQVLDEAVEKSLKGaSIWDEVKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802097265 498 ARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTHLLEE-TRDYDEVWVMDKGLIIEQGS 567
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQaSRISDRTGFFLDGDLIEYND 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
370-566 |
2.46e-08 |
|
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: 54.09 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSS---LLNLLLGFLPYEGSIRINQqelRDIRPESWRTQLSWVGQNPHL-PEQTILDNIR 445
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTllnALAGRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDILhPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 446 LSrpdasaeeitAVMEkayvtdfidslpdgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERV 525
Cdd:cd03213 105 FA----------AKLR------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 802097265 526 MHALNEAAHQQTTLLVT-HLL--EETRDYDEVWVMDKGLIIEQG 566
Cdd:cd03213 151 MSLLRRLADTGRTIICSiHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
371-566 |
3.51e-08 |
|
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: 54.96 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSIRINQQ--------ELRDIRpeswRTQLSWVGQNPHL-PEQTI 440
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCInRLIEPTSGKVLIDGQdiaamsrkELRELR----RKKISMVFQSFALlPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNI----------RLSRPDASAEeitaVMEKAYVTDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLL 510
Cdd:cd03294 120 LENVafglevqgvpRAEREERAAE----ALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802097265 511 DEPSASLD----AHSEERVMhALnEAAHQQTTLLVTHLLEET-RDYDEVWVMDKGLIIEQG 566
Cdd:cd03294 185 DEAFSALDplirREMQDELL-RL-QAELQKTIVFITHDLDEAlRLGDRIAIMKDGRLVQVG 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
370-567 |
3.58e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.63 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTILDNI---- 444
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFArLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVRELvayg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 ---------RLSRPDasAEEITAVMEKAYVTDFIDSLpdgvntvvgdnAARLSVGQAQRIAVARALLNPCHLLLLDEPSA 515
Cdd:PRK11231 101 rspwlslwgRLSAED--NARVNQAMEQTRINHLADRR-----------LTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 516 SLD-AHSEE--RVMHALNEAAhqQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK11231 168 YLDiNHQVElmRLMRELNTQG--KTVVTVLHDLNQASRYcDHLVVLANGHVMAQGT 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
370-571 |
4.98e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRP-ESWRTQLSWVGQNPHL-PEQTILDNI-- 444
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAgIVPPDSGTLEIGGNPCARLTPaKAHQLGIYLVPQEPLLfPNLSVKENIlf 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 RLSRPDASAEEITAVMEKAYVTDFIDSlpdgvntvvgdNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEER 524
Cdd:PRK15439 110 GLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETER 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 802097265 525 VMHALNEAAHQQTTLL-VTHLLEETRDY-DEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK15439 179 LFSRIRELLAQGVGIVfISHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
153-308 |
5.20e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 54.74 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 153 MILITLFPINWAAALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDAT 232
Cdd:cd18542 129 GALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKEN 208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 233 EDFRSRTMEVLRMAFLSSAVLEFFAAISIAVVAVYFGFSYL-GELNFGsygmgvTLFAgFIALILApeFFQPLRDLG 308
Cdd:cd18542 209 EEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVInGEITLG------ELVA-FISYLWM--LIWPVRQLG 276
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
370-566 |
5.90e-08 |
|
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: 53.94 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLP--YEGSIRINQQEL-----RDIRPeswrtQLSWVG---QNPHLPEQT 439
Cdd:COG1119 22 ISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptYGNDVRLFGERRggedvWELRK-----RIGLVSpalQLRFPRDET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 440 ILDNIrLSRPDASA---EEITAVMEKAyVTDFIDSLpdGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSAS 516
Cdd:COG1119 97 VLDVV-LSGFFDSIglyREPTDEQRER-ARELLELL--GLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 802097265 517 LDAHSEERVMHALNEAAHQQ--TTLLVTHLLEE-TRDYDEVWVMDKGLIIEQG 566
Cdd:COG1119 173 LDLGARELLLALLDKLAAEGapTLVLVTHHVEEiPPGITHVLLLKDGRVVAAG 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
370-567 |
8.16e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.46 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPesWRTQLSWVGQN----PHLP-EQTI--- 440
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAgFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSyalfPHMTvEQNIafg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNIRLSRPDASAEeITAVMEKAYVTDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAH 520
Cdd:PRK11607 116 LKQDKLPKAEIASR-VNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 802097265 521 SEERVMHALNEAAHQ--QTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK11607 184 LRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMaGRIAIMNRGKFVQIGE 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
371-567 |
8.52e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 53.62 E-value: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHL--PeQTILDNIRLS 447
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsfP-FTVEEVVAMG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 448 R------PDASAEEITAVMEKAYVTDFidslpdgvntvvgdnAAR----LSVGQAQRIAVARALLNPCHLLLL------D 511
Cdd:PRK13548 101 RaphglsRAEDDALVAAALAQVDLAHL---------------AGRdypqLSGGEQQRVQLARVLAQLWEPDGPprwlllD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 512 EPSASLDAHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNLAARYaDRIVLLHQGRLVADGT 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
369-567 |
8.63e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 54.31 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKS------------SllnlllgflpyEGSIRINQQELRDIRPEswRTQLSWVGQN---- 432
Cdd:COG3839 21 DIDLDIEDGEFLVLLGPSGCGKStllrmiagledpT-----------SGEILIGGRDVTDLPPK--DRNIAMVFQSyaly 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 433 PHLpeqTILDNI-------RLSRP--DASAEEITAVMEkayVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLN 503
Cdd:COG3839 88 PHM---TVYENIafplklrKVPKAeiDRRVREAAELLG---LEDLLDRKP-----------KQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 504 PCHLLLLDEPSASLDAHSeeRV-----MHALneaaHQQ---TTLLVTHlleetrDYDEVW-------VMDKGLIIEQGS 567
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKL--RVemraeIKRL----HRRlgtTTIYVTH------DQVEAMtladriaVMNDGRIQQVGT 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
371-563 |
9.11e-08 |
|
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: 52.05 E-value: 9.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRdirpeswrtqlswvgqnphlpeqtildniRLSRP 449
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSgLYKPDSGEILVDGKEVS-----------------------------FASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 450 DASAEEITAVMEkayvtdfidslpdgvntvvgdnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHAL 529
Cdd:cd03216 71 DARRAGIAMVYQ-------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI 125
|
170 180 190
....*....|....*....|....*....|....*.
gi 802097265 530 NEAAHQQTT-LLVTHLLEETRDY-DEVWVMDKGLII 563
Cdd:cd03216 126 RRLRAQGVAvIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
371-547 |
1.05e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.64 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKS----------SllnlllgflPYEGSIRINQQELRDIRP-ESWRTQLSWVGQNPHL-PEQ 438
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKStlmkilsgvyQ---------PDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLvPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 439 TILDNIRLSRPDASA---------EEITAVMEKAYVTdfIDslpdgVNTVVGDnaarLSVGQAQRIAVARALLNPCHLLL 509
Cdd:COG1129 95 SVAENIFLGREPRRGglidwramrRRARELLARLGLD--ID-----PDTPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 802097265 510 LDEPSASLDAHSEERVMHALNEAAHQQTTLL-VTHLLEE 547
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQGVAIIyISHRLDE 202
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
29-317 |
1.12e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 53.72 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 29 LLGVLSGLLIIGQAWCLAVLLQSLImEHVPREQLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTVLDKLEQ 108
Cdd:cd18565 21 LIGVAIDAVFNGEASFLPLVPASLG-PADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 109 LGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPV----FMALVG 184
Cdd:cd18565 100 LDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAgtywFQRRIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 185 lGAADANRRnflALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFFAAISIAVV 264
Cdd:cd18565 180 -PRYRAVRE---AVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVAT 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 265 AVYFGFSYLgelnFGSYGMGVTLFAG-FIALI-LAPEFFQPLRDLG----TYYHAKAQA 317
Cdd:cd18565 256 FVVGGYWVL----DGPPLFTGTLTVGtLVTFLfYTQRLLWPLTRLGdlidQYQRAMASA 310
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
353-567 |
1.26e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 53.16 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 353 ATDLVIFAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPE--SWRTQLSWV 429
Cdd:PRK13639 4 TRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNgILKPTSGEVLIKGEPIKYDKKSllEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 430 GQNP--HLPEQTILD-------NIRLSRpDASAEEITAVMEKAYVTDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARA 500
Cdd:PRK13639 84 FQNPddQLFAPTVEEdvafgplNLGLSK-EEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 501 LLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLV-THLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIsTHDVDLVPVYaDKVYVMSDGKIIKEGT 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
426-573 |
1.35e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 426 LSWVGQNPHLPEQTILDNIRLSRPDASAEEITAVMEKAYVTDfIDSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPC 505
Cdd:PTZ00243 723 IAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEAD-LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANR 801
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 506 HLLLLDEPSASLDAHSEERVMHALNEAA-HQQTTLLVTHLLEETRDYDEVWVMDKGLIIEQGSYAALQQ 573
Cdd:PTZ00243 802 DVYLLDDPLSALDAHVGERVVEECFLGAlAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
370-576 |
2.80e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.80 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSIRINQQELRDIRPES---WRTQLSWVGQNPHL-PEQTILDN- 443
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLIcGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLlMDRTVYDNv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 444 -IRLSRPDASAEEI----TAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASLD 518
Cdd:PRK10908 101 aIPLIIAGASGDDIrrrvSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 519 AHSEERVMHALNEAAH-QQTTLLVTHlleetrdydevwvmDKGLiIEQGSYAALQQQQG 576
Cdd:PRK10908 170 DALSEGILRLFEEFNRvGVTVLMATH--------------DIGL-ISRRSYRMLTLSDG 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
368-567 |
2.80e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.86 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 368 GPLNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYEGSIRINQQELRDIRPESWRTQLSWVGQ--NP------------ 433
Cdd:PRK03695 13 GPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQqqTPpfampvfqyltl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 434 HLPEQTildnirlsRPDASAEEITAVMEKAYVTDFidsLPDGVNTvvgdnaarLSVGQAQRIAVA-------RALLNPCH 506
Cdd:PRK03695 93 HQPDKT--------RTEAVASALNEVAEALGLDDK---LGRSVNQ--------LSGGEWQRVRLAavvlqvwPDINPAGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802097265 507 LLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVT-HLLEET-RDYDEVWVMDKGLIIEQGS 567
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSsHDLNHTlRHADRVWLLKQGKLLASGR 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
370-566 |
2.93e-07 |
|
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: 51.95 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPE---------SWRTQLSWvgqnpHLPeqt 439
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSgLLQPTSGEVRVAGLVPWKRRKKflrrigvvfGQKTQLWW-----DLP--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 440 ILDNIRLSR-----PDASA----EEITAVMEkayVTDFIDSlpdgvntvvgdNAARLSVGQAQRIAVARALLNPCHLLLL 510
Cdd:cd03267 112 VIDSFYLLAaiydlPPARFkkrlDELSELLD---LEELLDT-----------PVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 511 DEPSASLDAHSEERV---MHALNeAAHQQTTLLVTHLLEE-TRDYDEVWVMDKGLIIEQG 566
Cdd:cd03267 178 DEPTIGLDVVAQENIrnfLKEYN-RERGTTVLLTSHYMKDiEALARRVLVIDKGRLLYDG 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
370-563 |
3.12e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 52.01 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQelrDI--RPESWRTQL-SWVGQNPHL---PEQTILD 442
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAgSLPPDSGSILIDGK---DVtkLPEYKRAKYiGRVFQDPMMgtaPSMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 443 NIRL------SRPDASAeeitavMEKAYVTDFIDS-------LPDGVNTVVGDnaarLSVGQAQRIAVARALLNPCHLLL 509
Cdd:COG1101 102 NLALayrrgkRRGLRRG------LTKKRRELFRELlatlglgLENRLDTKVGL----LSGGQRQALSLLMATLTKPKLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 510 LDEPSASLDAHSEERVMHALNE--AAHQQTTLLVTHLLEETRDY-DEVWVMDKGLII 563
Cdd:COG1101 172 LDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
361-567 |
3.46e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.91 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 361 PSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDI-RPESWRTQLSWVGQNPHL--- 435
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNgLLRPQKGKVLVSGIDTGDFsKLQGIRKLVGIVFQNPETqfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 436 -----------PEQTILDNIRL-SRPDASAEEItavmekayvtdfidslpdGVNTVVGDNAARLSVGQAQRIAVARALLN 503
Cdd:PRK13644 92 grtveedlafgPENLCLPPIEIrKRVDRALAEI------------------GLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802097265 504 PCHLLLLDEPSASLDAHSEERVMHALNEAAHQ-QTTLLVTHLLEETRDYDEVWVMDKGLIIEQGS 567
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
371-547 |
3.55e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLNLLLGFLP---YEGSIRINQQELR--DIRpESWRTQLSWVGQNPHL-PEQTILDNI 444
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtYEGEIIFEGEELQasNIR-DTERAGIAIIHQELALvKELSVLENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 RLsrpdasAEEIT--------AVMEKAY-----VTDFIDslpdgVNTVVGDnaarLSVGQAQRIAVARALLNPCHLLLLD 511
Cdd:PRK13549 104 FL------GNEITpggimdydAMYLRAQkllaqLKLDIN-----PATPVGN----LGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 802097265 512 EPSASLDAHSEERVMHALNE-AAHQQTTLLVTHLLEE 547
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDlKAHGIACIYISHKLNE 205
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-567 |
3.99e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 381 ALVGQSGAGKSSLLNLLLGFLP-YEGSIRINQQ------ELRDIRPESWRTQLSWVGQNPH-LPEQTILDNIRL---SRP 449
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNpFPHLSIYDNIAYplkSHG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 450 DASAEEITAVMEKAY-VTDFIDSLPDGVNTvvgdNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:PRK14246 120 IKEKREIKKIVEECLrKVGLWKEVYDRLNS----PASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 802097265 529 LNEAAHQQTTLLVTHLLEE-TRDYDEVWVMDKGLIIEQGS 567
Cdd:PRK14246 196 ITELKNEIAIVIVSHNPQQvARVADYVAFLYNGELVEWGS 235
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
350-589 |
4.08e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 350 AVTATDLVI-FApsGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLP------YEGSIRINQQELRDIRPE-S 421
Cdd:PRK14271 21 AMAAVNLTLgFA--GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrYSGDVLLGGRSIFNYRDVlE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 422 WRTQLSWVGQNPHLPEQTILDNIRL---SRPDASAEEITAVMEkAYVTDFidSLPDGVNTVVGDNAARLSVGQAQRIAVA 498
Cdd:PRK14271 99 FRRRVGMLFQRPNPFPMSIMDNVLAgvrAHKLVPRKEFRGVAQ-ARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 499 RALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTH-LLEETRDYDEVWVMDKGLIIEQGSYAAL--QQQQ 575
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHnLAQAARISDRAALFFDGRLVEEGPTEQLfsSPKH 255
|
250
....*....|....
gi 802097265 576 GAFAQLLSHRTGDL 589
Cdd:PRK14271 256 AETARYVAGLSGDV 269
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
371-567 |
4.37e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.00 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSllnll-lgflPYEGSIRINQQELRDIRPESWRTQLSWVG---QNPHL-PEQTILDNI- 444
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTlircinllerPTSGSVLVDGVDLTALSERELRAARRKIGmifQHFNLlSSRTVAENVa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 ---RLSRpdASAEEITA-VMEK-AYV--TDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASL 517
Cdd:COG1135 105 lplEIAG--VPKAEIRKrVAELlELVglSDKADAYP-----------SQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 802097265 518 DAHSEERVMHALNEaAHQQ---TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:COG1135 172 DPETTRSILDLLKD-INRElglTIVLITHEMDVVRRIcDRVAVLENGRIVEQGP 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
377-543 |
5.32e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.93 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 377 GQRIALVGQSGAGKSSLLNLLLGFLP-YEGSIRINQQELRDIRPESwRTQL-----SWVGQNPHL-PEQTILDNIRL--- 446
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDgSSGEVSLVGQPLHQMDEEA-RAKLrakhvGFVFQSFMLiPTLNALENVELpal 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 447 ---SRPDASAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEE 523
Cdd:PRK10584 115 lrgESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180
....*....|....*....|...
gi 802097265 524 RV---MHALNEaAHQQTTLLVTH 543
Cdd:PRK10584 184 KIadlLFSLNR-EHGTTLILVTH 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
370-571 |
5.79e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPY------EGSIRIN--------QQELRDIRPEswrtQLSWVGQNPHL 435
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvypSGDIRFHgesllhasEQTLRGVRGN----KIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 436 ---PEQTI-------LDNIRLSRPDASAEEITAVMEKAYVTDFIDSLpdgvntvvGDNAARLSVGQAQRIAVARALLNPC 505
Cdd:PRK15134 104 slnPLHTLekqlyevLSLHRGMRREAARGEILNCLDRVGIRQAAKRL--------TDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 506 HLLLLDEPSASLDAHSEERVMHALNEAAHQ--QTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATL 244
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
21-307 |
7.02e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 51.33 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 21 RRWLRLSMLLGVLSGLLIIgqawcLAVLLQSLIMEHVPREQLLTPFTVLVILFIARAVVAAIRERVgFI--CGQV---VR 95
Cdd:cd18540 1 KKLLILLIILMLLVALLDA-----VFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFL-FIrlAGKIemgVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 96 RDIRRTVLDKLEQLGPVRVKGKPAGsWatIILEQIDDMQ---DYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVT 172
Cdd:cd18540 75 YDLRKKAFEHLQTLSFSYFDKTPVG-W--IMARVTSDTQrlgEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 173 APLIPVFMALVglgaadanRRNFLAL--------SRLSGDFLDRLRGLETIRFFhrGREEvKQIDDA---TEDFRSRTME 241
Cdd:cd18540 152 VPVLAVVSIYF--------QKKILKAyrkvrkinSRITGAFNEGITGAKTTKTL--VREE-KNLREFkelTEEMRRASVR 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 242 VLRMAFLSSAVLEFFAAISIAVVAVYFGFSYL-GELNFGsygmgvTLFAgFIALILapEFFQPLRDL 307
Cdd:cd18540 221 AARLSALFLPIVLFLGSIATALVLWYGGILVLaGAITIG------TLVA-FISYAT--QFFEPIQQL 278
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
370-571 |
7.98e-07 |
|
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: 50.20 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESwRTQLSWVGQNPHLPEQ-TILDNIRL- 446
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTgELRPTSGTAYINGYSIRTDRKAA-RQSLGYCPQFDALFDElTVREHLRFy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 447 ----SRPDASAEEITAVMEKAYvtdfidSLPDGVNTVVGDnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSE 522
Cdd:cd03263 100 arlkGLPKSEIKEEVELLLRVL------GLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 802097265 523 ERVMHALNEAAHQQTTLLVTHLLEETrDY--DEVWVMDKGLIIEQGSYAAL 571
Cdd:cd03263 170 RAIWDLILEVRKGRSIILTTHSMDEA-EAlcDRIAIMSDGKLRCIGSPQEL 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
372-518 |
9.56e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 50.89 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 372 FTLNAGQRIALVGQSGAGKSSLL-NLLLGFLPYEGSIRINQQELRDIRPESWRT-----QLswVGQNPH--L-PEQTI-- 440
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGrLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrrmQM--VFQDPYasLnPRMTVgd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 -----LDNIRLSRPDASAEEITAVMEKayvtdfidslpdgvntvVG---DNAAR----LSVGQAQRIAVARALLNPCHLL 508
Cdd:COG4608 117 iiaepLRIHGLASKAERRERVAELLEL-----------------VGlrpEHADRypheFSGGQRQRIGIARALALNPKLI 179
|
170
....*....|
gi 802097265 509 LLDEPSASLD 518
Cdd:COG4608 180 VCDEPVSALD 189
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
368-567 |
9.81e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.03 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 368 GPLNFTLNA---GQRI-ALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIR------PESWRtqLSWVGQNPHL- 435
Cdd:PRK11144 11 GDLCLTVNLtlpAQGItAIFGRSGAGKTSLINAISgLTRPQKGRIVLNGRVLFDAEkgiclpPEKRR--IGYVFQDARLf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 436 PEQTILDNIRLSRPDASAEEITAVMEKAYVTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSA 515
Cdd:PRK11144 89 PHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 802097265 516 SLDAHSEERVMHALNEAAHQQTT--LLVTHLLEET-RDYDEVWVMDKGLIIEQGS 567
Cdd:PRK11144 158 SLDLPRKRELLPYLERLAREINIpiLYVSHSLDEIlRLADRVVVLEQGKVKAFGP 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
370-571 |
1.04e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 50.96 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELrdirPESWRTQLSWVGQNPHL----PEQTILDNI 444
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLgLTHPDAGSISLCGEPV----PSRARHARQRVGVVPQFdnldPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 RL-SRP-DASAEEITAVMEKayVTDFIdSLPDGVNTVVGDnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSE 522
Cdd:PRK13537 102 LVfGRYfGLSAAAARALVPP--LLEFA-KLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 802097265 523 ----ERVMHALneaAHQQTTLLVTHLLEET-RDYDEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK13537 175 hlmwERLRSLL---ARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
370-571 |
1.06e-06 |
|
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: 50.82 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKS----SLLNLLLGFLPYEGSIRINQQELRDIRPESWRT----QLSWVGQNPH--L-PEQ 438
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKStlarAILGLLPPPGITSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDPMtsLnPVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 439 TILDNI--------RLSRPDAsAEEITAVMEKayvtdfidslpdgvntvVG-DNAAR--------LSVGQAQRIAVARAL 501
Cdd:COG0444 104 TVGDQIaeplrihgGLSKAEA-RERAIELLER-----------------VGlPDPERrldrypheLSGGMRQRVMIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802097265 502 LNPCHLLLLDEPSASLDAHSEERVMHALNE--AAHQQTTLLVTH---LLEETrdYDEVWVMDKGLIIEQGSYAAL 571
Cdd:COG0444 166 ALEPKLLIADEPTTALDVTIQAQILNLLKDlqRELGLAILFITHdlgVVAEI--ADRVAVMYAGRIVEEGPVEEL 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
370-570 |
1.25e-06 |
|
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: 51.36 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLP---YEGSIRINQQEL--RDIRpESWRTQLSWVGQNPHL-PEQTILDN 443
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtWDGEIYWSGSPLkaSNIR-DTERAGIVIIHQELTLvPELSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 444 IRLSRP----------DASAEEITAVMEKAYVTDFIDSLPdgvntvVGDnaarLSVGQAQRIAVARALLNPCHLLLLDEP 513
Cdd:TIGR02633 99 IFLGNEitlpggrmayNAMYLRAKNLLRELQLDADNVTRP------VGD----YGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 514 SASLDAHSEERVMHALNE-AAHQQTTLLVTHLLEETRDydevwVMDKGLIIEQGSYAA 570
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKA-----VCDTICVIRDGQHVA 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
370-567 |
2.00e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.11 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLP----YEGSIRIN--------QQELRDIRPEswrtQLSWVGQNP---- 433
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangrIGGSATFNgreilnlpEKELNKLRAE----QISMIFQDPmtsl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 434 --------HLPEQTILDNiRLSRPDASAEEIT---AV-MEKA------YVTDFidslpdgvntvvgdnaarlSVGQAQRI 495
Cdd:PRK09473 111 npymrvgeQLMEVLMLHK-GMSKAEAFEESVRmldAVkMPEArkrmkmYPHEF-------------------SGGMRQRV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802097265 496 AVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTT--LLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGIcDKVLVMYAGRTMEYGN 245
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
26-322 |
2.06e-06 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 49.74 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 26 LSMLLGVLSGLLIIGQAWclavLLQSLIMEHVPREQLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTVLDK 105
Cdd:cd18551 3 LALLLSLLGTAASLAQPL----LVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 106 LEQLgPVR-VKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVFMALVG 184
Cdd:cd18551 79 LLRL-PVSfFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 185 LGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLR-MAFLSSAVLeffAAISIAV 263
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKiEALIGPLMG---LAVQLAL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 264 VAVyFGFSYL----GELNFGSygmgvtlfagFIALILApeFFQ---PLRDLGTYYHAKAQAVGAAE 322
Cdd:cd18551 235 LVV-LGVGGArvasGALTVGT----------LVAFLLY--LFQlitPLSQLSSFFTQLQKALGALE 287
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
370-566 |
2.66e-06 |
|
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: 48.37 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWR--TQLSWVGQNPHLpeqTILDNIRL 446
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILgLIKPDSGEITFDGKSYQKNIEALRRigALIEAPGFYPNL---TARENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 447 S-----RPDASAEEITAVMekayvtdfidslpdGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDA-- 519
Cdd:cd03268 96 LarllgIRKKRIDEVLDVV--------------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPdg 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 802097265 520 -HSEERVMHALNEAAHqqTTLLVTHLLEE-TRDYDEVWVMDKGLIIEQG 566
Cdd:cd03268 162 iKELRELILSLRDQGI--TVLISSHLLSEiQKVADRIGIINKGKLIEEG 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
371-567 |
2.93e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 49.65 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSI--------RINQQELRDIRpeswRTQLSWVGQNPHL-PEQTI 440
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLnRLIEPTRGQVlidgvdiaKISDAELREVR----RKKIAMVFQSFALmPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNIrlsrpdASAEEITAVMEKAYVTDFIDSLPD-GVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDA 519
Cdd:PRK10070 124 LDNT------AFGMELAGINAEERREKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 802097265 520 HSEERVMHALN--EAAHQQTTLLVTHLLEET-RDYDEVWVMDKGLIIEQGS 567
Cdd:PRK10070 198 LIRTEMQDELVklQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEVVQVGT 248
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
370-560 |
2.93e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.34 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYE-GSIRINQQELRDIRPESWRTQLSWVGQNP--HLPEQTILDNIR- 445
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVEDDVAf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 446 -LSRPDASAEEITAVMEKAY----VTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAH 520
Cdd:PRK13650 106 gLENKGIPHEEMKERVNEALelvgMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 802097265 521 SEERVMHALNE--AAHQQTTLLVTHLLEETRDYDEVWVMDKG 560
Cdd:PRK13650 175 GRLELIKTIKGirDDYQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
26-307 |
3.08e-06 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 49.32 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 26 LSMLLGVLSGLLIIGQAWCLAVLLQSLIMEHVPR-----EQLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIRR 100
Cdd:cd18547 3 LVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGggvdfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 101 TVLDKLEQLgPVR-VKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVF 179
Cdd:cd18547 83 DLFEKLQRL-PLSyFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 180 MALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRsrtmEVLRMA-FLSSA---VLEF 255
Cdd:cd18547 162 TKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELY----KASFKAqFYSGLlmpIMNF 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 802097265 256 FAAISIAVVAVYFGFSYLgelnfgSYGMGVTLFAGFIalILAPEFFQPLRDL 307
Cdd:cd18547 238 INNLGYVLVAVVGGLLVI------NGALTVGVIQAFL--QYSRQFSQPINQI 281
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
154-322 |
3.27e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 49.02 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 154 ILITLFPINWAAALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATE 233
Cdd:cd18546 130 IAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 234 DFRSRTMEVLRMAFLSSAVLEFFAAISIAVVAVYFGFSYL-GELNFGsygmgvTLFAGFIALILapeFFQPLRDLGTYYH 312
Cdd:cd18546 210 DYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAaGTLTVG------VLVAFLLYLRR---FFAPIQQLSQVFD 280
|
170
....*....|
gi 802097265 313 AKAQAVGAAE 322
Cdd:cd18546 281 SYQQARAALE 290
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
370-571 |
3.57e-06 |
|
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: 49.68 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPY-----EGSIRINQQELRDIRPESWRT----QLSWVGQ------NPH 434
Cdd:COG4172 29 VSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahpSGSILFDGQDLLGLSERELRRirgnRIAMIFQepmtslNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 435 lpeQTILDNI--------RLSRPDASAEeITAVMEKayvtdfidslpdgvntvVG-DNAAR--------LSVGQAQRIAV 497
Cdd:COG4172 109 ---HTIGKQIaevlrlhrGLSGAAARAR-ALELLER-----------------VGiPDPERrldayphqLSGGQRQRVMI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 498 ARALLNPCHLLLLDEPSASLDAHSEERVMHALNE--AAHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAAL 571
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDVTVQAQILDLLKDlqRELGMALLLITHDLGVVRRFaDRVAVMRQGEIVEQGPTAEL 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
370-568 |
4.61e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.29 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSS-LLNLLLGFLPYEGSIRINQqelrdirpeswRTQLSWVGQNPHL--PEQTILDNIRL 446
Cdd:COG0488 334 LSLRIDRGDRIGLIGPNGAGKSTlLKLLAGELEPDSGTVKLGE-----------TVKIGYFDQHQEEldPDKTVLDELRD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 447 SRPDASAEEITAVMEkayvtDFIDSlPDGVNTVVGDnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSeervM 526
Cdd:COG0488 403 GAPGGTEQEVRGYLG-----RFLFS-GDDAFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET----L 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 802097265 527 HALNEA--AHQQTTLLVTH---LLEETRdyDEVWVMDKGLIIE-QGSY 568
Cdd:COG0488 469 EALEEAldDFPGTVLLVSHdryFLDRVA--TRILEFEDGGVREyPGGY 514
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
144-269 |
4.71e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 48.56 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 144 MTLSATIPMMILItlfpiNWAAALILLVTAPLIPVFMALVGlgaaDANRRNFL----ALSRLSGDFLDRLRGLETIRFFH 219
Cdd:cd18541 126 FLGVLVLVMMFTI-----SPKLTLIALLPLPLLALLVYRLG----KKIHKRFRkvqeAFSDLSDRVQESFSGIRVIKAFV 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 802097265 220 RGREEVKQIDDATEDFRSRTMEVLRMAFLSSAVLEFFAAISIAVVaVYFG 269
Cdd:cd18541 197 QEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIV-LWYG 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
372-547 |
6.04e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 372 FTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELR--DIRpESWRTQLSWVGQNPHL-PEQTILDNIRLS 447
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSgNYQPDAGSILIDGQEMRfaSTT-AALAAGVAIIYQELHLvPEMTVAENLYLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 448 RPDASAEEITAVMEKAYVTDFIDSLPDGV--NTVVGdnaaRLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERV 525
Cdd:PRK11288 104 QLPHKGGIVNRRLLNYEAREQLEHLGVDIdpDTPLK----YLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQL 179
|
170 180
....*....|....*....|...
gi 802097265 526 MHALNEAAHQQTTLL-VTHLLEE 547
Cdd:PRK11288 180 FRVIRELRAEGRVILyVSHRMEE 202
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
371-560 |
6.12e-06 |
|
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: 47.81 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLNLLLGF-LPYEGSIRINQQ-ELRDIrpeswrtqlswvgqnPHLPEQTILDnIRlsr 448
Cdd:COG4778 31 SFSVAAGECVALTGPSGAGKSTLLKCIYGNyLPDSGSILVRHDgGWVDL---------------AQASPREILA-LR--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 pdasAEEItavmekAYVTDFIDSLP--------------DGVNTVVG-DNAARL------------------SVGQAQRI 495
Cdd:COG4778 92 ----RRTI------GYVSQFLRVIPrvsaldvvaeplleRGVDREEArARARELlarlnlperlwdlppatfSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 496 AVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLL-VTHlLEETRDY--DEVWVMDKG 560
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH-DEEVREAvaDRVVDVTPF 228
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
143-269 |
6.64e-06 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 48.16 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 143 QMTLSATI------PMMI---LITLFPINWAAALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLE 213
Cdd:cd18548 110 QNFVMMLLrmlvraPIMLigaIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIR 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 214 TIRFFHRGREEVKQIDDATEDFRSRTMEVLR-MAFLSSAvleFFAAISIAVVAV-YFG 269
Cdd:cd18548 190 VIRAFNREDYEEERFDKANDDLTDTSLKAGRlMALLNPL---MMLIMNLAIVAIlWFG 244
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
361-567 |
7.12e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 47.92 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 361 PSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPE--SWRTQLSWVGQNP--HL 435
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNgILKPSSGRILFDGKPIDYSRKGlmKLRESVGMVFQDPdnQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 436 PEQTILDNI-----RLSRP-DASAEEITAVMEKAyvtdfidslpdGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLL 509
Cdd:PRK13636 96 FSASVYQDVsfgavNLKLPeDEVRKRVDNALKRT-----------GIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802097265 510 LDEPSASLDAHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYcDNVFVMKEGRVILQGN 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
369-567 |
8.54e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKSSLLNLLLG-----FLPYEGSIRINQQELRDIRPEsWRTQLSWVGQN----PHLPEQT 439
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgfHIGVEGVITYDGITPEEIKKH-YRGDVVYNAETdvhfPHLTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 440 ILD-NIRLSRPDASAEEITAVMEKAYVTDF---IDSLPDGVNTVVGDNAAR-LSVGQAQRIAVARALLNPCHLLLLDEPS 514
Cdd:TIGR00956 158 TLDfAARCKTPQNRPDGVSREEYAKHIADVymaTYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097265 515 ASLDAHSEERVMHALNEAAH-QQTTLLVTHLL--EETRD-YDEVWVMDKGLIIEQGS 567
Cdd:TIGR00956 238 RGLDSATALEFIRALKTSANiLDTTPLVAIYQcsQDAYElFDKVIVLYEGYQIYFGP 294
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
336-566 |
9.47e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.86 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 336 ELPGTEPltpaeqiAVTATDLV-IFAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQE 413
Cdd:TIGR01257 921 ELPGLVP-------GVCVKNLVkIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTgLLPPTSGTVLVGGKD 993
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 414 LrDIRPESWRTQLSWVGQ-NPHLPEQTILDNIRL--SRPDASAEEITAVMEkAYVTDfidslpDGVNTVVGDNAARLSVG 490
Cdd:TIGR01257 994 I-ETNLDAVRQSLGMCPQhNILFHHLTVAEHILFyaQLKGRSWEEAQLEME-AMLED------TGLHHKRNEEAQDLSGG 1065
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 491 QAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLVTHLLEETRdydevWVMDKGLIIEQG 566
Cdd:TIGR01257 1066 MQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAD-----LLGDRIAIISQG 1136
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
373-564 |
1.02e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 47.37 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 373 TLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRT-----QLswVGQNPHL---PEQTILDN 443
Cdd:PRK10419 34 SLKSGETVALLGRSGCGKSTLARLLVgLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiQM--VFQDSISavnPRKTVREI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 444 IR--------LSRPD--ASAEEITAVMEKAyvTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEP 513
Cdd:PRK10419 112 IReplrhllsLDKAErlARASEMLRAVDLD--DSVLDKRP-----------PQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 802097265 514 SASLDAHSEERVMHALNEAAHQQTT--LLVTHLLEETRDY-DEVWVMDKGLIIE 564
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFcQRVMVMDNGQIVE 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
69-324 |
1.47e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 47.09 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 69 LVILFIARAVVAAIRERVGFICGQVVRRDIRRTVLDKLEQLgPV------RVkgkpaGSWATIILEQIDDMQDYYSRYLP 142
Cdd:cd18576 42 LLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRL-PLsffherRV-----GELTSRLSNDVTQIQDTLTTTLA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 143 QMtLSATIPMMI-LITLFPINWAAALILLVTAPLIPVFMALVGlgaadanRRnflaLSRLSGDFLDRL-----------R 210
Cdd:cd18576 116 EF-LRQILTLIGgVVLLFFISWKLTLLMLATVPVVVLVAVLFG-------RR----IRKLSKKVQDELaeantiveetlQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 211 GLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRM--AFLSSAVLEFFAAIsiaVVAVYFGFSYL--GELnfgSYGMGVT 286
Cdd:cd18576 184 GIRVVKAFTREDYEIERYRKALERVVKLALKRARIraLFSSFIIFLLFGAI---VAVLWYGGRLVlaGEL---TAGDLVA 257
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 802097265 287 --LFAGFIAlilapeffQPLRDLGTYYHAKAQAVGAAESL 324
Cdd:cd18576 258 flLYTLFIA--------GSIGSLADLYGQLQKALGASERV 289
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
370-580 |
1.52e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.11 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPH------LPEQTIL- 441
Cdd:PRK13652 23 INFIAPRNSRIAVIGPNGAGKSTLFRHFNgILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDdqifspTVEQDIAf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 442 --DNIRLSRpDASAEEITAVMEKAYVTDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLLDEPSASLDA 519
Cdd:PRK13652 103 gpINLGLDE-ETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 520 HSEERVMHALNE--AAHQQTTLLVTH---LLEETRDYdeVWVMDKGLIIEQGSYAALQQQQGAFAQ 580
Cdd:PRK13652 171 QGVKELIDFLNDlpETYGMTVIFSTHqldLVPEMADY--IYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
370-553 |
1.62e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.10 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPeSWRTQLSWVGQ----NPHLP-EQTILDN 443
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAgLLNPEKGEILFERQSIKKDLC-TYQKQLCFVGHrsgiNPYLTlRENCLYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 444 IRLSRPDASAEEITAVMEKAYVTDFidslPDGVntvvgdnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEE 523
Cdd:PRK13540 99 IHFSPGAVGITELCRLFSLEHLIDY----PCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180 190
....*....|....*....|....*....|...
gi 802097265 524 RVMHALNEAAHQQTTLLVTH---LLEETRDYDE 553
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTShqdLPLNKADYEE 197
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
382-567 |
1.63e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.92 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 382 LVGQSGAGKSSLLNLLLGFLPYEG--------SIRINQQELRDIRpeSWRTQLSWVGQNP--HLPEQTILDNIRLSRPDA 451
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETgqtivgdyAIPANLKKIKEVK--RLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 452 SAEEITAVMEKAYVTDFIdSLPDgvnTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMH---A 528
Cdd:PRK13645 120 GENKQEAYKKVPELLKLV-QLPE---DYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINlfeR 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 802097265 529 LNEaAHQQTTLLVTHLLEET-RDYDEVWVMDKGLIIEQGS 567
Cdd:PRK13645 196 LNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
370-566 |
2.05e-05 |
|
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: 45.73 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLL-NLLLGFLPYEGSIRINQqelrdiRPESWRTQlSWVGqnpHLPE-------QTIL 441
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIrMILGIILPDSGEVLFDG------KPLDIAAR-NRIG---YLPEerglypkMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 442 DNIR-------LSRPDAsAEEITAVMEKAYVTDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLLDEPS 514
Cdd:cd03269 89 DQLVylaqlkgLKKEEA-RRRIDEWLERLELSEYANKRVE-----------ELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 802097265 515 ASLDAHSEERVMHALNEAAHQQTT-LLVTHLLEETRDY-DEVWVMDKGLIIEQG 566
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTvILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
334-543 |
2.33e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.61 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 334 DDELPGTEPLTPAEQIAVTATDLVIFapsgeklaGPLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQ 412
Cdd:PRK13543 2 IEPLHTAPPLLAAHALAFSRNEEPVF--------GPLDFHVDAGEALLVQGDNGAGKTTLLRVLAgLLHVESGQIQIDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 413 ELRdiRPESWRtQLSWVGQNPHL-PEQTILDNI---------RLSRPDASAEEITAVmekayvTDFIDSLpdgvntvvgd 482
Cdd:PRK13543 74 TAT--RGDRSR-FMAYLGHLPGLkADLSTLENLhflcglhgrRAKQMPGSALAIVGL------AGYEDTL---------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802097265 483 nAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQ-TTLLVTH 543
Cdd:PRK13543 135 -VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGgAALVTTH 195
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
351-566 |
2.57e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 46.76 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 351 VTATDLVIFAPSGEKLAGpLNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQ--ELRDIRPESWR---- 423
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDG-VDLSVREGSLVGLVGPNGAGKTTLLRAINgTLTPTAGTVLVAGDdvEALSARAASRRvasv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 424 ---TQLSW---------VGQNPHLPeqtildniRLSRPDASAEeiTAV---MEKAYVTDFIDSlpdgvntvvgdNAARLS 488
Cdd:PRK09536 83 pqdTSLSFefdvrqvveMGRTPHRS--------RFDTWTETDR--AAVeraMERTGVAQFADR-----------PVTSLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 489 VGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQ-QTTLLVTHLLEETRDY-DEVWVMDKGLIIEQG 566
Cdd:PRK09536 142 GGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYcDELVLLADGRVRAAG 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
370-566 |
2.78e-05 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 45.60 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRInqqelrdirpeswRTQLSW-----VGQNPHLpeqTILDN 443
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAgIYPPDSGTVTV-------------RGRVSSllglgGGFNPEL---TGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 444 IRLS------RPDASAEEITAVMEKAYVTDFIDsLPdgVNTvvgdnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASL 517
Cdd:cd03220 105 IYLNgrllglSRKEIDEKIDEIIEFSELGDFID-LP--VKT--------YSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 802097265 518 DAHSEERVMHALNE-AAHQQTTLLVTHLLEETRDY-DEVWVMDKGLIIEQG 566
Cdd:cd03220 174 DAAFQEKCQRRLRElLKQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
370-531 |
3.19e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 45.77 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYEGSI--------RINQQE---LRDIRPEswRTQLSWVGQNPHLPEQ 438
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshiellgRTVQREgrlARDIRKS--RANTGYIFQQFNLVNR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 439 -TILDNIRLSRPDASAEEITAV-----MEKAYVTDFIDSLpdGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDE 512
Cdd:PRK09984 101 lSVLENVLIGALGSTPFWRTCFswftrEQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170
....*....|....*....
gi 802097265 513 PSASLDAHSEERVMHALNE 531
Cdd:PRK09984 179 PIASLDPESARIVMDTLRD 197
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
370-547 |
3.22e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.85 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYE-GSIRINQQELRDirPESWRtqlSWVGQNPH-LPEQTILDNI--- 444
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEG--PGAER---GVVFQNEGlLPWRNVQDNVafg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 445 -------RLSRPDASAEEITAVMEKAYVTDFIdslpdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEPSASL 517
Cdd:PRK11248 95 lqlagveKMQRLEIAHQMLKKVGLEGAEKRYI---------------WQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190
....*....|....*....|....*....|..
gi 802097265 518 DAHSEERVMHALNEAAHQQ--TTLLVTHLLEE 547
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETgkQVLLITHDIEE 191
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
355-532 |
3.86e-05 |
|
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: 44.45 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 355 DLVIFAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPY-EGSIrinqqelrdIRPEswRTQLSWVGQNP 433
Cdd:cd03223 5 NLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWgSGRI---------GMPE--GEDLLFLPQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 434 HLPEQTILDNIrlsrpdasaeeitavmekAYVTDfidslpdgvntvvgdnaARLSVGQAQRIAVARALLNPCHLLLLDEP 513
Cdd:cd03223 74 YLPLGTLREQL------------------IYPWD-----------------DVLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170
....*....|....*....
gi 802097265 514 SASLDAHSEERVMHALNEA 532
Cdd:cd03223 119 TSALDEESEDRLYQLLKEL 137
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
371-566 |
4.68e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.41 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSllnll------lgflpYEGSIRINQQEL--RDIRPESWRTQLSWVGQ--NPhLPeQTI 440
Cdd:COG1117 31 NLDIPENKVTALIGPSGCGKSTllrclnrmndlipgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQkpNP-FP-KSI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNI----RLS--RPDASAEEIT-AVMEKAyvtdfidSLPDGVNTVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEP 513
Cdd:COG1117 109 YDNVayglRLHgiKSKSELDEIVeESLRKA-------ALWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 514 SASLDAHSEERVMHALNEAAHQQTTLLVTHLLEETR---DYdeVWVMDKGLIIEQG 566
Cdd:COG1117 182 TSALDPISTAKIEELILELKKDYTIVIVTHNMQQAArvsDY--TAFFYLGELVEFG 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
369-567 |
4.91e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.56 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 369 PLNFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSIRINQQEL-----RDIRPEswRTQLSWVGQnpH---LPEQT 439
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTLIRCInLLERPTSGRVLVDGQDLtalseKELRKA--RRQIGMIFQ--HfnlLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 440 ILDNIRLSRPDA--SAEEItavmeKAYVTDFIDslpdgvntVVG--DNA----ARLSVGQAQRIAVARALLNPCHLLLLD 511
Cdd:PRK11153 99 VFDNVALPLELAgtPKAEI-----KARVTELLE--------LVGlsDKAdrypAQLSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 512 EPSASLDAHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK11153 166 EATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
346-584 |
5.45e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 45.26 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 346 AEQIAVTATDLVIFAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPY-EGSIRINQQELRdirpESWRT 424
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLaSGKISILGQPTR----QALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 425 QL-SWVGQN-------PHLPEQTILDNIR-----LSRPDASAEEI-TAVMEKAYVTDFidslpdgVNTVVGDnaarLSVG 490
Cdd:PRK15056 78 NLvAYVPQSeevdwsfPVLVEDVVMMGRYghmgwLRRAKKRDRQIvTAALARVDMVEF-------RHRQIGE----LSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 491 QAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLV-THLLEETRDYDEVWVMDKGLIIEQG--- 566
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVsTHNLGSVTEFCDYTVMVKGTVLASGpte 226
|
250
....*....|....*....
gi 802097265 567 -SYAALQQQQgAFAQLLSH 584
Cdd:PRK15056 227 tTFTAENLEL-AFSGVLRH 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
370-566 |
5.84e-05 |
|
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: 45.95 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGS--IRINQQ--ELRDIRPESWRTQLSWVG---QNPHL-PEQTI 440
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAgVLEPTSGEvnVRVGDEwvDMTKPGPDGRGRAKRYIGilhQEYDLyPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDN----IRLSRPDASAEE---ITAVM---EKAYVTDFIDSLPDgvntvvgdnaaRLSVGQAQRIAVARALLNPCHLLLL 510
Cdd:TIGR03269 383 LDNlteaIGLELPDELARMkavITLKMvgfDEEKAEEILDKYPD-----------ELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 802097265 511 DEPSASLDAHSEERVMHALNEAAHQ--QTTLLVTHLLEETRDY-DEVWVMDKGLIIEQG 566
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDVcDRAALMRDGKIVKIG 510
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
357-573 |
6.06e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.16 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 357 VIFAPSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLL-LGFLPYEGSIRINQQELrdirpESWRTQlSWVGQNPHL 435
Cdd:PRK10575 17 VSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLgRHQPPSEGEILLDAQPL-----ESWSSK-AFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 436 PEQ-------TILDNI------------RLSRPDASA--EEITAVMEKAYVTDFIDSlpdgvntvvgdnaarLSVGQAQR 494
Cdd:PRK10575 91 PQQlpaaegmTVRELVaigrypwhgalgRFGAADREKveEAISLVGLKPLAHRLVDS---------------LSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 495 IAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAEL 235
|
..
gi 802097265 572 QQ 573
Cdd:PRK10575 236 MR 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
437-567 |
6.48e-05 |
|
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: 45.95 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 437 EQTILDNIRLSRPDASAEEITAVMEKAYVTDFIDsLPDGVNTVVGDnaarLSVGQAQRIAVARALLNPCHLLLLDEPSAS 516
Cdd:TIGR03269 124 DDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQ-LSHRITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGT 198
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 517 LDAHSEERVMHALNEAAHQQ--TTLLVTH---LLEETRDYdEVWvMDKGLIIEQGS 567
Cdd:TIGR03269 199 LDPQTAKLVHNALEEAVKASgiSMVLTSHwpeVIEDLSDK-AIW-LENGEIKEEGT 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
370-543 |
8.59e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.18 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLlnlllgflpyegsIRINQQELRDiRPESWRTQLSWvgqNPHLPEQTILDNI-RLSR 448
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTL-------------LRLLAGALKG-TPVAGCVDVPD---NQFGREASLIDAIgRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVmekayvtdfidslpdGVNTVVGDNA--ARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVM 526
Cdd:COG2401 112 FKDAVELLNAV---------------GLSDAVLWLRrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170
....*....|....*....
gi 802097265 527 HALNEAA--HQQTTLLVTH 543
Cdd:COG2401 177 RNLQKLArrAGITLVVATH 195
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
360-567 |
9.51e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.11 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 360 APSGEKLAGPLNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYE-GSIRINQQELrDIRP--ESWRTQLSWVGQNPHLP 436
Cdd:PRK10895 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDI-SLLPlhARARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 437 EQ-TILDNIRLS---RPDASAEE----ITAVMEKAYVTDFIDSLpdgvntvvgdnAARLSVGQAQRIAVARALLNPCHLL 508
Cdd:PRK10895 91 RRlSVYDNLMAVlqiRDDLSAEQredrANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802097265 509 LLDEPSASLDAHSEERVMHALNEAAHQQTTLLVT-HLLEETRDYDE-VWVMDKGLIIEQGS 567
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCErAYIVSQGHLIAHGT 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
371-462 |
1.73e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 44.29 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIrinqqelrdIRPESWRtqLSWVGQNPHL-PEQTILDNIRlsr 448
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAgELEPDSGEV---------SIPKGLR--IGYLPQEPPLdDDLTVLDTVL--- 83
|
90
....*....|....
gi 802097265 449 pdASAEEITAVMEK 462
Cdd:COG0488 84 --DGDAELRALEAE 95
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
26-308 |
2.80e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 43.24 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 26 LSMLLGVLSGLLIigqawclAVLLQSLI---MEHVPREQLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTV 102
Cdd:cd18543 6 LAALLATLAGLAI-------PLLTRRAIdgpIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 103 LDKLEQLGPVRVKGKPAG---SWATIILEQIddmQDYYSrYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVF 179
Cdd:cd18543 79 FAHLQRLDGAFHDRWQSGqllSRATSDLSLV---QRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 180 MALvglgaadaNRRNFLALSRLSGDFLDRL--------RGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSA 251
Cdd:cd18543 155 ARR--------FRRRYFPASRRAQDQAGDLatvveesvTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWP 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 252 VLEFFAAISIAVVAVYFGFSYL-GELNFGsygmgvTLFAgFIALILApeFFQPLRDLG 308
Cdd:cd18543 227 LLEALPELGLAAVLALGGWLVAnGSLTLG------TLVA-FSAYLTM--LVWPVRMLG 275
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
61-307 |
3.23e-04 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 42.82 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 61 QLLTPFTVLVILFIARAVVAAIRERVGFICGQVVRRDIRRTVLDKLEQLG-----PVRVkgkpaGSWATIILEQIDDMQD 135
Cdd:cd18549 40 LILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSfsffdNNKT-----GQLMSRITNDLFDISE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 136 YYSRyLPQMTLSATIpMMI--LITLFPINWAAALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLE 213
Cdd:cd18549 115 LAHH-GPEDLFISII-TIIgsFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 214 TIRFFHRGREEVKQIDDATEDFRSRTMEVLR-MAFLSSaVLEFFAAIsIAVVAVYFG--FSYLGELNFGSygmgvtlFAG 290
Cdd:cd18549 193 VVKAFANEEYEIEKFDEGNDRFLESKKKAYKaMAYFFS-GMNFFTNL-LNLVVLVAGgyFIIKGEITLGD-------LVA 263
|
250
....*....|....*..
gi 802097265 291 FIALILApeFFQPLRDL 307
Cdd:cd18549 264 FLLYVNV--FIKPIRRL 278
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
371-560 |
3.44e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.48 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKS----------SllnlllgflPYEGSIRINQQELRdIR-P-ESWRTQLSWVGQNPHL-PE 437
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKStlmkilyglyQ---------PDSGEILIDGKPVR-IRsPrDAIALGIGMVHQHFMLvPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 438 QTILDNIRLSRPD---------ASAEEITAVMEKayvTDF-IDslPDgvnTVVGDnaarLSVGQAQRIAVARALLNPCHL 507
Cdd:COG3845 95 LTVAENIVLGLEPtkggrldrkAARARIRELSER---YGLdVD--PD---AKVED----LSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 802097265 508 LLLDEPSASLDAHSEERVMHALNEAAHQQTT-LLVTHLLEETRDY-DEVWVMDKG 560
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAEGKSiIFITHKLREVMAIaDRVTVLRRG 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
484-566 |
4.03e-04 |
|
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: 41.97 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 484 AARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTTLLV-THLLEET-RDYDEVWVMDKGL 561
Cdd:cd03266 134 VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFsTHIMQEVeRLCDRVVVLHRGR 213
|
....*
gi 802097265 562 IIEQG 566
Cdd:cd03266 214 VVYEG 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
370-571 |
4.75e-04 |
|
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: 41.89 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESwRTQL--SWVGQNPHL-PEQTILDNIR 445
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISgLLPPRSGSIRFDGEDITGLPPHR-IARLgiGYVPEGRRIfPSLTVEENLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 446 L-SRPDASAEEITAVMEKAY-----VTDFIDSLpdgvntvvgdnAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDA 519
Cdd:COG0410 101 LgAYARRDRAEVRADLERVYelfprLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 802097265 520 HSEERVMHALNEAAHQQTT-LLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAAL 571
Cdd:COG0410 170 LIVEEIFEIIRRLNREGVTiLLVEQNARFALEIaDRAYVLERGRIVLEGTAAEL 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
377-569 |
5.81e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.94 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 377 GQRIALVGQSGAGKSSLLNLLL---GFLPYEGSIRINQQELrdIRPESWRTqlSWVGQN----PHLPEQTILDNIRLSR- 448
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgriQGNNFTGTILANNRKP--TKQILKRT--GFVTQDdilyPHLTVRETLVFCSLLRl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 449 PDASAEEITAVMEKAYVTDFidSLPDGVNTVVGDNAAR-LSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMH 527
Cdd:PLN03211 170 PKSLTKQEKILVAESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 802097265 528 ALNEAAHQQTTLLVTHLLEETRDY---DEVWVMDKG--LIIEQGSYA 569
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPSSRVYqmfDSVLVLSEGrcLFFGKGSDA 294
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
377-560 |
7.62e-04 |
|
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: 41.07 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 377 GQRIALVGQSGAGKSS---LLNLLLGFLPYEGSIRINQQELrdirPESWRTQLSWVGQNP-HLPEQTILDNIRLSrpdas 452
Cdd:cd03232 33 GTLTALMGESGAGKTTlldVLAGRKTAGVITGEILINGRPL----DKNFQRSTGYVEQQDvHSPNLTVREALRFS----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 453 aeeitavmekAYVTDfidslpdgvntvvgdnaarLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNE- 531
Cdd:cd03232 104 ----------ALLRG-------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKl 154
|
170 180 190
....*....|....*....|....*....|....
gi 802097265 532 AAHQQTTLLVTH-----LLEEtrdYDEVWVMDKG 560
Cdd:cd03232 155 ADSGQAILCTIHqpsasIFEK---FDRLLLLKRG 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
371-566 |
1.04e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.06 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 371 NFTLNAGQRIALVGQSGAGKSS-LLNLLLGFLPYEGSI--RINQQELRDI--RPES-----WRTQLSWVGQNPhlpeqti 440
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTlLNALSARLAPDAGEVhyRMRDGQLRDLyaLSEAerrrlLRTEWGFVHQHP------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNIrlsRPDASA-----EEITAVMEKAY----------------VTDFIDSLPdgvntvvgdnaARLSVGQAQRIAVAR 499
Cdd:PRK11701 99 RDGL---RMQVSAggnigERLMAVGARHYgdiratagdwlerveiDAARIDDLP-----------TTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 500 ALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQQ--TTLLVTHLLEETRDY-DEVWVMDKGLIIEQG 566
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLaHRLLVMKQGRVVESG 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
370-547 |
1.07e-03 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 41.00 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLL-GFLPYEGSIRINQQELRDirPESWRtqlSWVGQNpH--LPEQTILDNIRL 446
Cdd:COG4525 26 VSLTIESGEFVVALGASGCGKTTLLNLIAgFLAPSSGEITLDGVPVTG--PGADR---GVVFQK-DalLPWLNVLDNVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 447 S----------RPDASAEEITAVMEKAYVTDFIDSLpdgvntvvgdnaarlSVGQAQRIAVARALLNPCHLLLLDEPSAS 516
Cdd:COG4525 100 GlrlrgvpkaeRRARAEELLALVGLADFARRRIWQL---------------SGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180 190
....*....|....*....|....*....|....
gi 802097265 517 LDAHSEERvMHAL---NEAAHQQTTLLVTHLLEE 547
Cdd:COG4525 165 LDALTREQ-MQELlldVWQRTGKGVFLITHSVEE 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
370-571 |
1.26e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.76 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSL-LNLLLGFLPYEGSIRINQQE---LRDIRPESWRTQLSWVGQNPHL---PEQTILD 442
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTgRALLRLVESQGGEIIFNGQRidtLSPGKLQALRRDIQFIFQDPYAsldPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 443 NI-------RLSRPDASAEEITAVMEKayvtdfIDSLPdgvntvvgDNAAR----LSVGQAQRIAVARALLNPCHLLLLD 511
Cdd:PRK10261 423 SImeplrvhGLLPGKAAAARVAWLLER------VGLLP--------EHAWRypheFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802097265 512 EPSASLDAHSEERVMHALNEAAHQQ--TTLLVTHLLEET-RDYDEVWVMDKGLIIEQGSYAAL 571
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAV 551
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
362-392 |
1.84e-03 |
|
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: 38.97 E-value: 1.84e-03
10 20 30
....*....|....*....|....*....|.
gi 802097265 362 SGEKLAGPLNFTLNAGQRIALVGQSGAGKSS 392
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKST 41
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
370-575 |
1.87e-03 |
|
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: 40.96 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLP--YEGSIRINQQELrDIR-------------PESWRTQ----LSWVG 430
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkFEGNVFINGKPV-DIRnpaqairagiamvPEDRKRHgivpILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 431 QNPHLpeqTILDNI-RLSRPDASAEE--ITAVMEKAYVTDFIDSLPDGvntvvgdnaaRLSVGQAQRIAVARALLNPCHL 507
Cdd:TIGR02633 358 KNITL---SVLKSFcFKMRIDAAAELqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802097265 508 LLLDEPSASLDAHSEERVMHALNEAAHQQTTLLV--THLLEETRDYDEVWVMDKGLIieQGSYA--ALQQQQ 575
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVvsSELAEVLGLSDRVLVIGEGKL--KGDFVnhALTQEQ 494
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
374-567 |
1.87e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.19 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 374 LNAGQRIALVGQSGAGKSSLLNLLLGFLP----YEGSIRINQQ--ELRDIRPESwrtqlSWVGQN----PHLPEQ---TI 440
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkGSGSVLLNGMpiDAKEMRAIS-----AYVQQDdlfiPTLTVRehlMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNIRLSRPDASAEEITAVmeKAYVTDFidSLPDGVNTVVGDNAAR--LSVGQAQRIAVARALLNPCHLLLLDEPSASLD 518
Cdd:TIGR00955 123 QAHLRMPRRVTKKEKRERV--DEVLQAL--GLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 802097265 519 AHSEERVMHALNEAAHQQTTLLVT------HLLEEtrdYDEVWVMDKGLIIEQGS 567
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTihqpssELFEL---FDKIILMAEGRVAYLGS 250
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
97-264 |
2.10e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 40.54 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 97 DIRRTVLDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSR-YLPQMTLSATIPMMILITLFpINWAAALI----LLV 171
Cdd:cd18585 69 NLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRvLSPPVVALLVILATILFLAF-FSPALALIllagLLL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 172 TAPLIPVFMALVGLGAADANRRnflALSRLSGDFLDRLRGLETIRFFHRGREEVKQIDDATEDFRSRTMEVLRMAFLSSA 251
Cdd:cd18585 148 AGVVIPLLFYRLGKKIGQQLVQ---LRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQA 224
|
170
....*....|...
gi 802097265 252 VLEFFAAISIAVV 264
Cdd:cd18585 225 LMILLSGLTVWLV 237
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
60-298 |
2.10e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 40.48 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 60 EQLLTPFTVLVILF-IARAVVAAIRERVGFICGQVVRRDIRRTVLDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYS 138
Cdd:cd18554 42 YKLFTIIGIMFFIFlILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFIT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 139 RYLPQMTLSATIPMMILITLFPINWAAALILLVTAPLIPVFMALVGLGAADANRRNFLALSRLSGDFLDRLRGLETIRFF 218
Cdd:cd18554 122 TGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 219 HRGREEVKQIDDATEDFRSRTMEVLR---MAFLSSAVLEFFAAISIAVVAVYFGFSylGELNFGSygmgVTLFAGFIALI 295
Cdd:cd18554 202 ALEKHEQKQFDKRNGHFLTRALKHTRwnaKTFSAVNTITDLAPLLVIGFAAYLVIE--GNLTVGT----LVAFVGYMERM 275
|
...
gi 802097265 296 LAP 298
Cdd:cd18554 276 YSP 278
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
370-566 |
2.18e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYEG-----SIRINQQELRDIrPESWRTQL-----SWVGQNPHL---P 436
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaeKLEFNGQDLQRI-SEKERRNLvgaevAMIFQDPMTslnP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 437 EQT----ILDNIRLSRPDASAEEItavmEKAyvtdfIDSLpdgvnTVVG--DNAARLSV-------GQAQRIAVARALLN 503
Cdd:PRK11022 105 CYTvgfqIMEAIKVHQGGNKKTRR----QRA-----IDLL-----NQVGipDPASRLDVyphqlsgGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 504 PCHLLLLDEPSASLDAHSEERVMHALNEAAHQQTT--LLVTH---LLEETRDYdeVWVMDKGLIIEQG 566
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHdlaLVAEAAHK--IIVMYAGQVVETG 236
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
377-560 |
2.28e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.25 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 377 GQRIALVGQSGAGKSSLLNLLLGFLP---YEGSIRINQQELRDirpESWRTQLSWVGQNP-HLPEQTILDNIRLSRPDAS 452
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD---SSFQRSIGYVQQQDlHLPTSTVRESLRFSAYLRQ 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 453 AEEITAVMEKAYVTDFIDSL--PDGVNTVVGDNAARLSVGQAQR--IAVARAlLNPCHLLLLDEPSASLDAHSEERVMHA 528
Cdd:TIGR00956 866 PKSVSKSEKMEYVEEVIKLLemESYADAVVGVPGEGLNVEQRKRltIGVELV-AKPKLLLFLDEPTSGLDSQTAWSICKL 944
|
170 180 190
....*....|....*....|....*....|....*...
gi 802097265 529 L-NEAAHQQTTLLVTH-----LLEEtrdYDEVWVMDKG 560
Cdd:TIGR00956 945 MrKLADHGQAILCTIHqpsaiLFEE---FDRLLLLQKG 979
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
370-567 |
2.77e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.61 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPYEGS----------------IRINQQ---ELRDIRPESWRT--QLSW 428
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdkmllrrrsrqvIELSEQsaaQMRHVRGADMAMifQEPM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 429 VGQNPHLP--EQtILDNIRLSRpDASAEEitAVMEKAYVTDFIdSLPDGvNTVVGDNAARLSVGQAQRIAVARALLNPCH 506
Cdd:PRK10261 115 TSLNPVFTvgEQ-IAESIRLHQ-GASREE--AMVEAKRMLDQV-RIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802097265 507 LLLLDEPSASLDAHSEERVMHALNEAAHQQT--TLLVTHLLEETRDY-DEVWVMDKGLIIEQGS 567
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIaDRVLVMYQGEAVETGS 252
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
446-577 |
2.80e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.10 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 446 LSRPDASAEEiTAVMEKAYVTDfidslpdgvntVVGDNAARLSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERV 525
Cdd:NF000106 116 LSRKDARARA-DELLERFSLTE-----------AAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 802097265 526 MHALNEAAHQ-QTTLLVTHLLEETRDY-DEVWVMDKGLIIEQGSYAALQQQQGA 577
Cdd:NF000106 184 WDEVRSMVRDgATVLLTTQYMEEAEQLaHELTVIDRGRVIADGKVDELKTKVGG 237
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
316-440 |
3.37e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 40.34 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 316 QAVGAaesLFTLLSAENNDDELPGTE--PLTPAEQIAVTATDL-------VIFAPSGEKLA-GPLNFTLNAGQRIALVGQ 385
Cdd:PRK10522 281 SAVGA---LPTLLSAQVAFNKLNKLAlaPYKAEFPRPQAFPDWqtlelrnVTFAYQDNGFSvGPINLTIKRGELLFLIGG 357
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 802097265 386 SGAGKSSLLNLLL-GFLPYEGSIRINQQELRDIRPESWRTQLSWVGQNPHLPEQTI 440
Cdd:PRK10522 358 NGSGKSTLAMLLTgLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL 413
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
26-322 |
5.66e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 39.03 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 26 LSMLLGVLSGLLIIgqaWCLAVLLQSLIMEHVPREQL-------LTPFTVL-------VILFIARAVVAAIRERVGFICG 91
Cdd:cd18564 6 LALLLETALRLLEP---WPLKVVIDDVLGDKPLPGLLglapllgPDPLALLllaaaalVGIALLRGLASYAGTYLTALVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 92 QVVRRDIRRTVLDKLEQLGPVRVKGKPAGSWATIILEQIDDMQDYYSRYLPQMTLSATIPMMILITLFPINWAAALILLV 171
Cdd:cd18564 83 QRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 172 TAPLIPVFMALVGLGAADANRRnflaLSRLSGDFLDRL-RGLETIRF---FHRGREEVKQIDDATEDFRSRTMEVLRMAF 247
Cdd:cd18564 163 VAPLLLLAARRFSRRIKEASRE----QRRREGALASVAqESLSAIRVvqaFGREEHEERRFARENRKSLRAGLRAARLQA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802097265 248 LSSAVLEFFAAISIAVVaVYFGfSYL---GELNFGsygmGVTLFAGFIALilapeFFQPLRDLGTYYHAKAQAVGAAE 322
Cdd:cd18564 239 LLSPVVDVLVAVGTALV-LWFG-AWLvlaGRLTPG----DLLVFLAYLKN-----LYKPVRDLAKLTGRIAKASASAE 305
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
487-571 |
6.15e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 38.91 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 487 LSVGQAQRIAVARALLNPCHLLLLDEPSASLDAHSEERVMHALNEAAHQ-QTTLLVTHLLEETRDYDE-VWVMDKGLIIE 564
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKrTIFFKDGKIIK 245
|
....*...
gi 802097265 565 QG-SYAAL 571
Cdd:PRK13651 246 DGdTYDIL 253
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
370-567 |
8.88e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.08 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 370 LNFTLNAGQRIALVGQSGAGKSSLLNLLLGFLPY---EGSIRINQQELRDIRPESwRTQLswvG-----QNP-HLPEQTI 440
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYkilEGDILFKGESILDLEPEE-RAHL---GiflafQYPiEIPGVSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097265 441 LDNIRLS---------RPDASAEE-ITAVMEKayvTDFIDSLPDGVNTVVGDNaarLSVGQAQRIAVARALLNPCHLLLL 510
Cdd:CHL00131 102 ADFLRLAynskrkfqgLPELDPLEfLEIINEK---LKLVGMDPSFLSRNVNEG---FSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 802097265 511 DEPSASLDAHSEERVMHALNEAAHQQTT-LLVTH---LLeetrDY---DEVWVMDKGLIIEQGS 567
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLMTSENSiILITHyqrLL----DYikpDYVHVMQNGKIIKTGD 235
|
|
| |
