|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-588 |
0e+00 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 1076.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 1 MNKTRQQELTRWLKEQSILSRRWLMISRALGVISGLLIVGQAWLLARILHRMIMENIPATALVLPFIVLVLIFVLRAWVV 80
Cdd:PRK11174 1 MDKSRQKELTRWLKQQSKPAKRWLNLSILLGFLSGLLLIAQAWLLATILQALIIENIPREALLPPFILLILLFVLRALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 81 WLRERVGFYAGQHIRYEIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFP 160
Cdd:PRK11174 81 WLRERVGFKAGQHIRQQIRQQVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 161 INWAAALILLGTAPLIPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTM 240
Cdd:PRK11174 161 INWAAGLILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 241 EVLRLAFLSSGVLEFFTSLSIALVAVYFGFSYLGELNFGHYGVGVTLMSGFLALILAPEFFQPLRDLGTFYHAKAQAIGA 320
Cdd:PRK11174 241 EVLRMAFLSSAVLEFFASISIALVAVYFGFSYLGELNFGHYGTGVTLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 321 ADSLKTFMEKPLAQETRGEKLLSDNEPIGLEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL 400
Cdd:PRK11174 321 AESLVTFLETPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 401 PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVG 480
Cdd:PRK11174 401 PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 481 DQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQ 560
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
570 580
....*....|....*....|....*...
gi 695777692 561 IVEQGTYSQLAMANGPFAALLAHRQEEI 588
Cdd:PRK11174 561 IVQQGDYAELSQAGGLFATLLAHRQEEI 588
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-575 |
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: 748.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 6 QQELTRWLKEQSILSRRWLMISRALGVISGLLIVGQAWLLARILHRMIMENIPATALVLPFIVLVLIFVLRAWVVWLRER 85
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 86 VGFYAGQHIRYEIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAA 165
Cdd:COG4988 81 AAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 166 ALILLGTAPLIPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRL 245
Cdd:COG4988 161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 246 AFLSSGVLEFFTSLSIALVAVYFGFSYLGElnfghygvGVTLMSGFLALILAPEFFQPLRDLGTFYHAKAQAIGAADSLK 325
Cdd:COG4988 241 AFLSSAVLEFFASLSIALVAVYIGFRLLGG--------SLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 326 TFMEKPLAQETRGEKLLSDNEPIGLEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDG 404
Cdd:COG4988 313 ALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 405 SLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAG 484
Cdd:COG4988 393 SILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 485 RLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQ 564
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
570
....*....|.
gi 695777692 565 GTYSQLAMANG 575
Cdd:COG4988 553 GTHEELLAKNG 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-556 |
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: 557.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 21 RRWLMISRALGVISGLLIVGQAWLLARILHRMIMENIPATALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRR 100
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 101 QVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFM 180
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 181 ALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLS 260
Cdd:TIGR02857 162 ILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 261 IALVAVYFGFSYLGElnfghygvGVTLMSGFLALILAPEFFQPLRDLGTFYHAKAQAIGAADSLKTFMEKPlAQETRGEK 340
Cdd:TIGR02857 242 VALVAVYIGFRLLAG--------DLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAA-PRPLAGKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 341 LLSDNEPIGLEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDAS 419
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVdPTEGSIAVNGVPLADADAD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 420 RWHRLLSWVGQNPQLPAATLRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARA 499
Cdd:TIGR02857 393 SWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 500 LLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVM 556
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
29-324 |
1.64e-132 |
|
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: 388.69 E-value: 1.64e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 29 ALGVISGLLIVGQAWLLARILHRMIMENIPATALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVLDRLQQ 108
Cdd:cd18584 3 LLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 109 AGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFMALVGMGAA 188
Cdd:cd18584 83 LGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKAAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 189 EANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVAVYF 268
Cdd:cd18584 163 AASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAVYI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 269 GFSYLGElnfghygvGVTLMSGFLALILAPEFFQPLRDLGTFYHAKAQAIGAADSL 324
Cdd:cd18584 243 GFRLLGG--------SLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-587 |
3.87e-108 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 336.37 E-value: 3.87e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 21 RRWLMISRALGVISGLLIVGQAWLLARILhRMIMENIPATALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRR 100
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRII-DALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 101 QVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFM 180
Cdd:COG1132 99 DLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 181 ALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLS 260
Cdd:COG1132 179 RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 261 IALVAVYFGFSYL-GELNFGhygvgvTLMSgFLALILApeFFQPLRDLGTFYHAKAQAIGAADSLKTFMEKPLAQETRGE 339
Cdd:COG1132 259 LALVLLVGGLLVLsGSLTVG------DLVA-FILYLLR--LFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 340 KLLSDNEPIGLEARDAIVKSPEGK-ILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLD 417
Cdd:COG1132 330 AVPLPPVRGEIEFENVSFSYPGDRpVLKD-ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdPTSGRILIDGVDIRDLT 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 418 ASRWHRLLSWVGQNPQLPAATLRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVA 497
Cdd:COG1132 409 LESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIA 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 498 RALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPF 577
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLY 568
|
570
....*....|
gi 695777692 578 AALLAHRQEE 587
Cdd:COG1132 569 ARLYRLQFGE 578
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
27-324 |
1.64e-101 |
|
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: 309.21 E-value: 1.64e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 27 SRALGVISGLLIVGQAWLLARILHRMIMeNIPATALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVLDRL 106
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFA-GGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 107 QQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFMALVGMG 186
Cdd:cd18561 80 LKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 187 AAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVAV 266
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 267 YFGFSYLGElnfghygvGVTLMSGFLALILAPEFFQPLRDLGTFYHAKAQAIGAADSL 324
Cdd:cd18561 240 VGALRVLGG--------QLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
97-583 |
1.32e-86 |
|
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: 279.73 E-value: 1.32e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 97 EIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLG----T 172
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALglllA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 173 APLIPLFMALVGMGAAEANRRnflALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGV 252
Cdd:COG4987 169 GLLLPLLAARLGRRAGRRLAA---ARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 253 LEFFTSLSIALVAVyfgfsyLGELNFGHYGVGVTLMSGFLALILApeFFQPLRDLGTFYHAKAQAIGAADSLKTFMEKPL 332
Cdd:COG4987 246 LQLAAGLAVVAVLW------LAAPLVAAGALSGPLLALLVLAALA--LFEALAPLPAAAQHLGRVRAAARRLNELLDAPP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 333 AQETRGEKLLSDNEPiGLEARDAIVKSP-EGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNG 410
Cdd:COG4987 318 AVTEPAEPAPAPGGP-SLELEDVSFRYPgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQsGSITLGG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 411 VELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQ 490
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 491 AQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQL 570
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
490
....*....|...
gi 695777692 571 AMANGPFAALLAH 583
Cdd:COG4987 557 LAQNGRYRQLYQR 569
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-580 |
4.08e-78 |
|
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: 260.92 E-value: 4.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 11 RWLKEQSILSRRWLMISRALGVISGLLIVGQAWLLARILHRMIMENIPATALVLpFIVLVLIFVLRAWVVWLRERVGFYA 90
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVL-AIGLLLALLFEGLLRLLRSYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 91 GQHIRYEIRRQVLDRLQQAGPAWIQGKPAGSWATLV--LEQIDDMhdyyaryLPQMTLAASVPLLIVIT----IFPINWA 164
Cdd:COG2274 224 GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFrdVESIREF-------LTGSLLTALLDLLFVLIflivLFFYSPP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 165 AALILLGTAPLIPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLR 244
Cdd:COG2274 297 LALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 245 LAFLSSGVLEFFTSLSIALVaVYFGfSYL---GELNFGhygvgvTLMSgFLALILApeFFQPLRDLGTFYHAKAQAIGAA 321
Cdd:COG2274 377 LSNLLSTLSGLLQQLATVAL-LWLG-AYLvidGQLTLG------QLIA-FNILSGR--FLAPVAQLIGLLQRFQDAKIAL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 322 DSLKTFMEKPLAQETRGEKLLSDNEPIGLEARDAIVKSPEGK--ILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF 399
Cdd:COG2274 446 ERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSppVLDN-ISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 400 L-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTP 478
Cdd:COG2274 525 YePTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 479 VGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQD 558
Cdd:COG2274 605 VGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDK 684
|
570 580
....*....|....*....|..
gi 695777692 559 GQIVEQGTYSQLAMANGPFAAL 580
Cdd:COG2274 685 GRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
360-585 |
3.96e-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: 191.98 E-value: 3.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 360 PEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAAT 438
Cdd:cd03249 14 PDVPILKG-LSLTIPPGKTVALVGSSGCGKSTVVSLLERFyDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 439 LRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDA 518
Cdd:cd03249 93 IAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 519 HSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLaMANGPFAALLAHRQ 585
Cdd:cd03249 173 ESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL-MAQKGVYAKLVKAQ 238
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-544 |
8.49e-54 |
|
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: 191.42 E-value: 8.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 18 ILSRRWLMISR-ALGVISGLLIVG----QAWLLARIlhrmiMENIPATALVLPfIVLVLIF-VLRAWVVWLRERVGFYAG 91
Cdd:TIGR02868 8 LKPRRRRLALAvLLGALALGSAVAllgvSAWLISRA-----AEMPPVLYLSVA-AVAVRAFgIGRAVFRYLERLVGHDAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 92 QHIRYEIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLG 171
Cdd:TIGR02868 82 LRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 172 TAPLIPLFMALVgmgAAEANRRNFLALARLSGHFLDR----LRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAF 247
Cdd:TIGR02868 162 GLLLAGFVAPLV---SLRAARAAEQALARLRGELAAQltdaLDGAAELVASGALPAALAQVEEADRELTRAERRAAAATA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 248 LSSGVLEFFTSLSIALVAVYFGFSYLGElnfghyGVGVTLMSGFLALILApeFFQPLRDLGTFYHAKAQAIGAADSLKTF 327
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAVADG------RLAPVTLAVLVLLPLA--AFEAFAALPAAAQQLTRVRAAAERIVEV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 328 MEKPLAQ---ETRGEKLLSDNEPiGLEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYD 403
Cdd:TIGR02868 311 LDAAGPVaegSAPAAGAVGLGKP-TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLdPLQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 404 GSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQA 483
Cdd:TIGR02868 390 GEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGG 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 484 GRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQL 544
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
360-580 |
7.12e-50 |
|
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: 172.41 E-value: 7.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 360 PEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFlpYD---GSLLVNGVELRDLDASRWHRLLSWVGQNPQLPA 436
Cdd:cd03253 12 PGRPVLKD-VSFTIPAGKKVAIVGPSGSGKSTILRLLFRF--YDvssGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 437 ATLRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:cd03253 89 DTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 517 DAHSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAAL 580
Cdd:cd03253 169 DTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
369-580 |
1.29e-49 |
|
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: 171.64 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFlpYD---GSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLL 445
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRF--YDvdsGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 446 AWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVM 525
Cdd:cd03251 99 GRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQ 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 526 QALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAAL 580
Cdd:cd03251 179 AALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
361-575 |
3.48e-48 |
|
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: 167.79 E-value: 3.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 361 EGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATL 439
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 440 RENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAH 519
Cdd:cd03254 94 MENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 520 SEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANG 575
Cdd:cd03254 174 TEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
369-560 |
3.24e-47 |
|
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: 162.94 E-value: 3.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLlaw 447
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENIL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 peaseaqlqlaldkawvsefisqlpqgintpvgdqagrlSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQA 527
Cdd:cd03228 98 ---------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
|
170 180 190
....*....|....*....|....*....|...
gi 695777692 528 LFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQ 560
Cdd:cd03228 139 LRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
360-587 |
5.28e-44 |
|
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: 165.76 E-value: 5.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 360 PEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFlpYD---GSLLVNGVELRDLDASRWHRLLSWVGQNPQLPA 436
Cdd:COG5265 369 PERPILKG-VSFEVPAGKTVAIVGPSGAGKSTLARLLFRF--YDvtsGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 437 ATLRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:COG5265 446 DTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 517 DAHSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAALLAHRQEE 587
Cdd:COG5265 526 DSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEE 596
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
24-292 |
1.44e-43 |
|
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: 156.65 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 24 LMISRALGVISGLLIVGQAWLLARILHRMIMENIPAT-ALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQV 102
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 103 LDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFMAL 182
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 183 VGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIA 262
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|..
gi 695777692 263 LVAvYFGFSYL--GELNFGHYGVGVTLMSGFL 292
Cdd:pfam00664 241 LAL-WFGAYLVisGELSVGDLVAFLSLFAQLF 271
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
147-584 |
2.83e-42 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 160.57 E-value: 2.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 147 AASVPLLIVItiFPINWAAALILLGTAPLIPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETD 226
Cdd:PRK11176 151 ASIIGLFIMM--FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 227 NIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVAVYFGF-SYLGELNFGHYGVgvtLMSGFLALIlapeffQPLR 305
Cdd:PRK11176 229 RFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVMDTLTAGTITV---VFSSMIALM------RPLK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 306 DLgTFYHAKAQ-AIGAADSLKTFMEkpLAQETRGEKLLSDNEPIGLEARDAIVKSPEGKILA-GPLNFTLPAGKRVVLVG 383
Cdd:PRK11176 300 SL-TNVNAQFQrGMAACQTLFAILD--LEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVPAlRNINFKIPAGKTVALVG 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 384 QSGSGKSSLLNALTGFlpYD---GSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAWPEA-SEAQLQLAL 459
Cdd:PRK11176 377 RSGSGKSTIANLLTRF--YDideGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAA 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 460 DKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLM 539
Cdd:PRK11176 455 RMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV 534
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 695777692 540 VTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAALlaHR 584
Cdd:PRK11176 535 IAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL--HK 577
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
369-565 |
3.62e-42 |
|
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: 151.20 E-value: 3.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAW 447
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQA 527
Cdd:cd03245 103 PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKER 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 695777692 528 LFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQG 565
Cdd:cd03245 183 LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
66-565 |
1.59e-41 |
|
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: 159.65 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 66 FIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVLD-RLQQagpawiqgKPA--GSWATLV--LEQIDDmhdyyarY 140
Cdd:TIGR03375 194 ALAIVFDFVLKTLRSYFLDVAGKKADLILSAKLFERVLGlRMEA--------RPAsvGSFANQLreFESVRD-------F 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 141 LPQMTLAASVPL----LIVITIFPINWAAALILLGTAPLIPLF--------MALVGMGAAEANRRNflalarlsGHFLDR 208
Cdd:TIGR03375 259 FTSATLTALIDLpfalLFLLVIAIIGGPLVWVPLVAIPLILLPglllqrplSRLAEESMRESAQRN--------AVLVES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 209 LRGMETLRLFhRGEAEtdnirhasqdfRQRTMEVLRLAFLSSGV-LEFFTSLSIALVAVYFGFSYLGELNFGHYGVGVTL 287
Cdd:TIGR03375 331 LSGLETIKAL-NAEGR-----------FQRRWEQTVAALARSGLkSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 288 MS-GFL--ALILAPEFFQPLRD----LGTFYHAKAqaigAADSLKTFMEKPlaQETRGEKLLSDNEPI--GLEARDAIVK 358
Cdd:TIGR03375 399 LTmGGLiaCVMLSGRALAPLGQlaglLTRYQQAKT----ALQSLDELMQLP--VERPEGTRFLHRPRLqgEIEFRNVSFA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 359 SPEGKILA-GPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPA 436
Cdd:TIGR03375 473 YPGQETPAlDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYqPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFY 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 437 ATLRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:TIGR03375 553 GTLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAM 632
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 695777692 517 DAHSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQG 565
Cdd:TIGR03375 633 DNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADG 681
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
61-581 |
2.51e-41 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 159.12 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 61 ALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARY 140
Cdd:TIGR00958 199 ALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 141 LPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHR 220
Cdd:TIGR00958 279 VNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 221 GEAETDNIRHASQDFRQ--RTMEVLRLAFLSsgVLEFFTSLSIALVavyfgfsylgeLNFGHYGVGVTLMS--GFLALIL 296
Cdd:TIGR00958 359 EEGEASRFKEALEETLQlnKRKALAYAGYLW--TTSVLGMLIQVLV-----------LYYGGQLVLTGKVSsgNLVSFLL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 297 APEFF-QPLRDLGTFYHAKAQAIGAADSLKTFME-KPLAQETRGEKLLSDNEPIglEARD---AIVKSPEGKILAGpLNF 371
Cdd:TIGR00958 426 YQEQLgEAVRVLSYVYSGMMQAVGASEKVFEYLDrKPNIPLTGTLAPLNLEGLI--EFQDvsfSYPNRPDVPVLKG-LTF 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 372 TLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAWPEA 450
Cdd:TIGR00958 503 TLHPGEVVALVGPSGSGKSTVAALLQNLYqPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDT 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 451 SEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQAlfN 530
Cdd:TIGR00958 583 PDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--R 660
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 695777692 531 ASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAALL 581
Cdd:TIGR00958 661 SRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
135-575 |
3.09e-40 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 154.88 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 135 DYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMET 214
Cdd:PRK10790 137 DLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 215 LRLFHRGEAETDNIRHASQDFRQRTMEVLRL-AFLSSGVLEFFTSLSIALVAVYFGFSYLGELnfghyGVGVtlMSGFLA 293
Cdd:PRK10790 217 IQQFRQQARFGERMGEASRSHYMARMQTLRLdGFLLRPLLSLFSALILCGLLMLFGFSASGTI-----EVGV--LYAFIS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 294 LIlaPEFFQPLRDLGTFYHAKAQAIGAADSLKTFMEKPlaQETRGekllSDNEPIG---LEARDAIVKSPEGKILAGPLN 370
Cdd:PRK10790 290 YL--GRLNEPLIELTTQQSMLQQAVVAGERVFELMDGP--RQQYG----NDDRPLQsgrIDIDNVSFAYRDDNLVLQNIN 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 371 FTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAwPE 449
Cdd:PRK10790 362 LSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTeGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG-RD 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 450 ASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALf 529
Cdd:PRK10790 441 ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL- 519
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 695777692 530 NASSQQTTLMV-THQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANG 575
Cdd:PRK10790 520 AAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
146-583 |
7.14e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 153.44 E-value: 7.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 146 LAASVPLLIVITIFP--INWAAALILLGTAPLIPLFMALVGMGAAEANRRNFLAL-ARLSGHFLDRLRGMETLRLFHRGE 222
Cdd:PRK11160 141 LVAALVVILVLTIGLsfFDLTLALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLrAQYRVQLTEWLQGQAELTLFGAED 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 223 AETDNIRHASQDF--RQRTMEvlRLAFLSSGVLEFFTSLSIALVavyfgfsylgeLNFGHYGVGVTLMSG-FLALIL--- 296
Cdd:PRK11160 221 RYRQQLEQTEQQWlaAQRRQA--NLTGLSQALMILANGLTVVLM-----------LWLAAGGVGGNAQPGaLIALFVfaa 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 297 --APEFFQPLRdlGTFYHAkAQAIGAADSLKTFME-KPLAQETRGEKLLSDNEPIGLEARDAIVKSPEGKILAGpLNFTL 373
Cdd:PRK11160 288 laAFEALMPVA--GAFQHL-GQVIASARRINEITEqKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKG-LSLQI 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 374 PAGKRVVLVGQSGSGKSSLLNALT-GFLPYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAWPEASE 452
Cdd:PRK11160 364 KAGEKVALLGRTGCGKSTLLQLLTrAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASD 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 453 AQLQLALDKAWVSEFISQlPQGINTPVGDqAGR-LSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNA 531
Cdd:PRK11160 444 EALIEVLQQVGLEKLLED-DKGLNAWLGE-GGRqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH 521
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 695777692 532 SSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAALLAH 583
Cdd:PRK11160 522 AQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQR 573
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
369-566 |
1.86e-39 |
|
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: 143.79 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENvLLAW 447
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSN-LDPF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQA 527
Cdd:cd03244 102 GEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 695777692 528 LFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:cd03244 182 IREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
360-561 |
1.95e-37 |
|
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: 138.37 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 360 PEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAAT 438
Cdd:cd03248 25 PDTLVLQD-VSFTLHPGEVTALVGPSGSGKSTVVALLENFYqPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 439 LRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDA 518
Cdd:cd03248 104 LQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695777692 519 HSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQI 561
Cdd:cd03248 184 ESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
360-580 |
7.87e-37 |
|
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: 137.23 E-value: 7.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 360 PEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAAT 438
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 439 LRENVLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDA 518
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695777692 519 HSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAAL 580
Cdd:cd03252 172 ESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
146-581 |
1.27e-36 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 144.33 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 146 LAASVPLLIVI-TIFPINWAAALILLGTAPLIPLFMALV------GMGAAEANRRNflalarLSGHFLDRLRGMETLRLF 218
Cdd:PRK13657 138 LATLVALVVLLpLALFMNWRLSLVLVVLGIVYTLITTLVmrktkdGQAAVEEHYHD------LFAHVSDAIGNVSVVQSY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 219 HRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEffTSLSIALVAVYFGFSYL---GELNFGHYgvgVTLMSgflali 295
Cdd:PRK13657 212 NRIEAETQALRDIADNLLAAQMPVLSWWALASVLNR--AASTITMLAILVLGAALvqkGQLRVGEV---VAFVG------ 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 296 LAPEFFQPLRDLGTFYHakaQAIGAADSLKTFME----KPLAQETRGEKLLSDNEpiGLEARDAIVKSPEGKILA-GPLN 370
Cdd:PRK13657 281 FATLLIGRLDQVVAFIN---QVFMAAPKLEEFFEvedaVPDVRDPPGAIDLGRVK--GAVEFDDVSFSYDNSRQGvEDVS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 371 FTLPAGKRVVLVGQSGSGKSSLLNALT-GFLPYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAWPE 449
Cdd:PRK13657 356 FEAKPGQTVAIVGPTGAGKSTLINLLQrVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 450 ASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALF 529
Cdd:PRK13657 436 ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALD 515
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 695777692 530 NASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAALL 581
Cdd:PRK13657 516 ELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
29-322 |
5.44e-36 |
|
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: 136.53 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 29 ALGVISGLLIVGQAWLLARILHRMIMENIPA---TALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVLDR 105
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAgdlSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 106 LQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFMALVGM 185
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 186 GAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVA 265
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 266 VYFGFSYL-GELNFGhygvgvTLMSgFLALIlaPEFFQPLRDLGTFYHAKAQAIGAAD 322
Cdd:cd07346 242 LYGGYLVLqGSLTIG------ELVA-FLAYL--GMLFGPIQRLANLYNQLQQALASLE 290
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
29-322 |
3.61e-35 |
|
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: 134.20 E-value: 3.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 29 ALGVISGLLIVGQAWLLARILHRMIMENIPATALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVLDRLQQ 108
Cdd:cd18781 3 LLQWISLLANIAFVFSIANLLQKLLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 109 AGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQM--TLAASVPLLIVitIFPINWAAALILLGTAPLIPLFMALVGMG 186
Cdd:cd18781 83 LGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFfySMLAPLTLFVV--LAPINWKAALVLLICVPLIPISIIAVQKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 187 AAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFF----TSLSIA 262
Cdd:cd18781 161 AKKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVayggAALGII 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 263 LVAVYFgfsYLGELNFGhygvgvtlmSGFLALILAPEFFQPLRDLGTFYHAKAQAIGAAD 322
Cdd:cd18781 241 LALLQF---ANGSISLA---------GALFIILLSAEFFLPLRLLGSFFHIAMNGMAASD 288
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
350-561 |
8.49e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.32 E-value: 8.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDaIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWHRLLSWV 428
Cdd:COG4619 1 LELEG-LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTsGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 429 GQNPQLPAATLRENvLLAWPEASEAQLQLALDKAWVSEFisQLPQGI-NTPVGdqagRLSVGQAQRIAVARALLVPCRLL 507
Cdd:COG4619 80 PQEPALWGGTVRDN-LPFPFQLRERKFDRERALELLERL--GLPPDIlDKPVE----RLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 508 LLDEPAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQLEGIADW-DAIWVMQDGQI 561
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLreYLAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
369-583 |
1.94e-33 |
|
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: 135.64 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLL-A 446
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgA 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 447 WPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQ 526
Cdd:TIGR01193 573 KENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVN 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 527 ALFNAsSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAALLAH 583
Cdd:TIGR01193 653 NLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
350-564 |
1.61e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 124.77 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDaIVKS-PEGK----ILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHR 423
Cdd:COG1136 5 LELRN-LTKSyGTGEgevtALRG-VSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDrPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 424 L----LSWVGQNPQL-PAATLRENVLLAW------PEASEAQLQLALDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQ 492
Cdd:COG1136 83 LrrrhIGFVFQFFNLlPELTALENVALPLllagvsRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 493 RIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALF--NASSQQTTLMVTHQLEgIADW-DAIWVMQDGQIVEQ 564
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPE-LAARaDRVIRLRDGRIVSD 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
369-560 |
1.64e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 115.64 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNP--QLPAATLRENVLL 445
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQFFGPTVEEEVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 446 AwPEaseaqlQLALDKAWVSEFISQLPQ--GINtpvgDQAGR----LSVGQAQRIAVARALLVPCRLLLLDEPAASLDAH 519
Cdd:cd03225 100 G-LE------NLGLPEEEIEERVEEALElvGLE----GLRDRspftLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695777692 520 SEQRVMQALFNASSQQTT-LMVTHQLEGIADW-DAIWVMQDGQ 560
Cdd:cd03225 169 GRRELLELLKKLKAEGKTiIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
368-514 |
1.80e-29 |
|
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: 113.51 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 368 PLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQL-PAATLRENVLL 445
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLfPRLTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 446 AwpeASEAQLQLALDKAWVSEFISQLPQG--INTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAA 514
Cdd:pfam00005 83 G---LLLKGLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
350-566 |
2.18e-29 |
|
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: 122.55 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGK--ILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLS 426
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRG-VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWpPTAGSVRLDGADLSQWDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 427 WVGQNPQLPAATLRENVllA-WPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCR 505
Cdd:COG4618 410 YLPQDVELFDGTIAENI--ArFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695777692 506 LLLLDEPAASLDAHSEQRVMQALFNASSQQTT-LMVTHQLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKARGATvVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
370-561 |
2.49e-29 |
|
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: 115.66 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRL----LSWVGQNPQL-PAATLRENV 443
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDrPTSGEVRVDGTDISKLSEKELAAFrrrhIGFVFQSFNLlPDLTALENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAwpeASEAQLQLALDKAWVSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQR 523
Cdd:cd03255 104 ELP---LLLAGVPKKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695777692 524 VMQALF--NASSQQTTLMVTHQLEgIADW-DAIWVMQDGQI 561
Cdd:cd03255 179 VMELLRelNKEAGTTIVVVTHDPE-LAEYaDRIIELRDGKI 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
369-560 |
1.16e-28 |
|
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: 113.33 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP-YDGSLLVNGVelrdldasrwhrlLSWVGQNPQLPAATLRENVLLAW 447
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEkLSGSVSVPGS-------------IAYVSQEPWIQNGTIRENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PeaseaqlqlaLDKAWVSEFI---------SQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDA 518
Cdd:cd03250 91 P----------FDEERYEKVIkacalepdlEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695777692 519 HSEQRVMQALF--NASSQQTTLMVTHQLEGIADWDAIWVMQDGQ 560
Cdd:cd03250 161 HVGRHIFENCIlgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
317-566 |
6.28e-28 |
|
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: 117.83 E-value: 6.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 317 AIGAADSLKTFmekpLAQETRGEKLLSDNEPIG-LEARDAIVKSPEGK--ILAGpLNFTLPAGKRVVLVGQSGSGKSSLL 393
Cdd:TIGR01842 287 ARQAYKRLNEL----LANYPSRDPAMPLPEPEGhLSVENVTIVPPGGKkpTLRG-ISFSLQAGEALAIIGPSGSGKSTLA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 394 NALTG-FLPYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAWPEASEAQLQLALDKAWVSEFISQLP 472
Cdd:TIGR01842 362 RLIVGiWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLP 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 473 QGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQ-TTLMVTHQLEGIADWD 551
Cdd:TIGR01842 442 DGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVD 521
|
250
....*....|....*
gi 695777692 552 AIWVMQDGQIVEQGT 566
Cdd:TIGR01842 522 KILVLQDGRIARFGE 536
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
369-565 |
7.51e-28 |
|
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: 110.10 E-value: 7.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHrLLSWVGQNPQLPAATLRENVllaw 447
Cdd:cd03247 21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLkPQQGEITLDGVPVSDLEKALSS-LISVLNQRPYLFDTTLRNNL---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 peaseaqlqlaldkawvsefisqlpqGIntpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQA 527
Cdd:cd03247 96 --------------------------GR---------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 695777692 528 LFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQG 565
Cdd:cd03247 141 IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
369-587 |
2.26e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 116.35 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALT-GFLPYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAW 447
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQrHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQA 527
Cdd:PRK10789 414 PDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 528 LFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAALLAHRQEE 587
Cdd:PRK10789 494 LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLE 553
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
350-570 |
2.45e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 115.77 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILA-GPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP----YDGSLLVNGVELRDLDASRWHRL 424
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAvDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 425 LSWVGQNP--QLPAATLRENVllawpeaSEAQLQLALDKAWVSEFISQLPQ--GINTPVGDQAGRLSVGQAQRIAVARAL 500
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDQI-------AEALENLGLSRAEARARVLELLEavGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695777692 501 LVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQ--TTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
351-560 |
1.47e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 102.71 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 351 EARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVG 429
Cdd:cd00267 1 EIENLSFRYGGRTALDN-VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 430 QnpqlpaatlrenvllawpeaseaqlqlaldkawvsefisqlpqgintpvgdqagrLSVGQAQRIAVARALLVPCRLLLL 509
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695777692 510 DEPAASLDAHSEQRVMQALFNASSQQTT-LMVTHQLEGIADW-DAIWVMQDGQ 560
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTvIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
368-565 |
4.29e-25 |
|
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: 103.74 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 368 PLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASR---WHRLLSWVGQNPQL---PAAT-- 438
Cdd:cd03257 23 DVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGKDLLKLSRRLrkiRRKEIQMVFQDPMSslnPRMTig 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 439 --LRENVLLAWPEASEAQLQLALDKAWV-----SEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDE 511
Cdd:cd03257 103 eqIAEPLRIHGKLSKKEARKEAVLLLLVgvglpEEVLNRYPH-----------ELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 512 PAASLDAHSEQRVMQALFNASSQQ--TTLMVTHQLEGIADW-DAIWVMQDGQIVEQG 565
Cdd:cd03257 172 PTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
350-561 |
4.59e-24 |
|
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: 99.21 E-value: 4.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGK--ILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLS 426
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRN-VSFSIEPGESLAIIGPSGSGKSTLARLILGLLrPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 427 WVGQNPQLPAATLRENVLlawpeaseaqlqlaldkawvsefisqlpqgintpvgdqagrlSVGQAQRIAVARALLVPCRL 506
Cdd:cd03246 80 YLPQDDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 507 LLLDEPAASLDAHSEQRVMQALFNASSQQTT-LMVTHQLEGIADWDAIWVMQDGQI 561
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATrIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
362-565 |
1.87e-23 |
|
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: 97.51 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 362 GKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQnpqlpaatlr 440
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkPSSGEILLDGKDLASLSPKELARKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 441 envllawpeaseaqlqlALDKAWVSEFisqLPQGINTpvgdqagrLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHS 520
Cdd:cd03214 81 -----------------ALELLGLAHL---ADRPFNE--------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695777692 521 EQRVMQAL--FNASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQG 565
Cdd:cd03214 133 QIELLELLrrLARERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
350-557 |
2.93e-23 |
|
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: 97.93 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDlDASRWHRLLSWV 428
Cdd:COG4133 3 LEAENLSCRRGERLLFSG-LSFTLAAGEALALTGPNGSGKTTLLRILAGLLpPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 429 GQNPQLPAA-TLRENvLLAW-----PEASEAQLQLALDKAwvsefisQLPQGINTPVGdqagRLSVGQAQRIAVARALLV 502
Cdd:COG4133 81 GHADGLKPElTVREN-LRFWaalygLRADREAIDEALEAV-------GLAGLADLPVR----QLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 503 PCRLLLLDEPAASLDAHSEQRVMQALFNASSQQ-TTLMVTHQLEGIADWDAIWVMQ 557
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGgAVLLTTHQPLELAAARVLDLGD 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
369-566 |
4.02e-23 |
|
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: 97.48 E-value: 4.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENvLLAW 447
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSN-LDPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASEAQLQLALDkawVSEfisqlpQGINtpvgdqagrLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSE---QRV 524
Cdd:cd03369 106 DEYSDEEIYGALR---VSE------GGLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDaliQKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695777692 525 MQALFNASsqqTTLMVTHQLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:cd03369 168 IREEFTNS---TILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
370-571 |
4.54e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 98.34 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQL---PAATLRE---- 441
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAslhPRHTVDRilae 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 442 -----NVLLAWPEASEAQLQLALDKAWVSEFISQLpqgintpvgdqagrlSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:COG1124 105 plrihGLPDREERIAELLEQVGLPPSFLDRYPHQL---------------SGGQRQRVAIARALILEPELLLLDEPTSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695777692 517 DAHSEQRVMqALFNASSQQ---TTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQLA 571
Cdd:COG1124 170 DVSVQAEIL-NLLKDLREErglTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLL 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
233-576 |
5.58e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 104.43 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 233 QDFRQRTMEVLRLAFLSSGVLEF-FTSLSIALVAVYFG-FSYLGelnfghyGVgVTLMSGFLALILapefFQPLR-DLGT 309
Cdd:PLN03130 506 QTVRDDELSWFRKAQLLSAFNSFiLNSIPVLVTVVSFGvFTLLG-------GD-LTPARAFTSLSL----FAVLRfPLFM 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 310 FYHAKAQAIGAADSLKTFMEKPLAQEtrgeKLLSDNEPIGLEARDAIVK-------SPEGKILAGPLNFTLPAGKRVVLV 382
Cdd:PLN03130 574 LPNLITQAVNANVSLKRLEELLLAEE----RVLLPNPPLEPGLPAISIKngyfswdSKAERPTLSNINLDVPVGSLVAIV 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 383 GQSGSGKSSLLNALTGFLP--YDGSLLVNGVelrdldasrwhrlLSWVGQNPQLPAATLRENVLLAWPEASEaQLQLALD 460
Cdd:PLN03130 650 GSTGEGKTSLISAMLGELPprSDASVVIRGT-------------VAYVPQVSWIFNATVRDNILFGSPFDPE-RYERAID 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 461 KAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVM-QALFNASSQQTTLM 539
Cdd:PLN03130 716 VTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDELRGKTRVL 795
|
330 340 350
....*....|....*....|....*....|....*..
gi 695777692 540 VTHQLEGIADWDAIWVMQDGQIVEQGTYSQLaMANGP 576
Cdd:PLN03130 796 VTNQLHFLSQVDRIILVHEGMIKEEGTYEEL-SNNGP 831
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
350-570 |
9.82e-23 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 96.87 E-value: 9.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLL------NALTGFLPYDGSLLVNGVELRDLDASR-WH 422
Cdd:cd03260 1 IELRDLNVYYGDKHALKD-ISLDIPKGEITALIGPSGCGKSTLLrllnrlNDLIPGAPDEGEVLLDGKDIYDLDVDVlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 423 RL-LSWVGQNPQLPAATLRENVLLA-------WPEASEAQLQLALDKAWVSEfisqlpqgintPVGDQ--AGRLSVGQAQ 492
Cdd:cd03260 80 RRrVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWD-----------EVKDRlhALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 493 RIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTH---QLEGIADWdaIWVMQDGQIVEQGTYSQ 569
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqQAARVADR--TAFLLNGRLVEFGPTEQ 226
|
.
gi 695777692 570 L 570
Cdd:cd03260 227 I 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
354-565 |
1.82e-22 |
|
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: 95.66 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 354 DAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRwhRLLSWVGQNP 432
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDsGEILIDGRDVTGVPPER--RNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 433 QL-PAATLRENV-----LLAWPEAS-EAQLQLALDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCR 505
Cdd:cd03259 82 ALfPHLTVAENIafglkLRGVPKAEiRARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695777692 506 LLLLDEPAASLDAHSEQRVMQALFNASSQQ--TTLMVTH-QLEGIADWDAIWVMQDGQIVEQG 565
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
343-563 |
2.73e-22 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 95.96 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 343 SDNEPIgLEARDA--IVKSPEGK--ILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLD 417
Cdd:COG4181 3 SSSAPI-IELRGLtkTVGTGAGEltILKG-ISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 418 ----ASRWHRLLSWVGQNPQL-PAATLRENVLLAWPEASEAQLQ----LALDKAWVSEFISQLPqgintpvgdqaGRLSV 488
Cdd:COG4181 81 edarARLRARHVGFVFQSFQLlPTLTALENVMLPLELAGRRDARararALLERVGLGHRLDHYP-----------AQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 489 GQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALF--NASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVE 563
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
209-581 |
3.23e-22 |
|
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: 101.95 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 209 LRGMETLRLFHRGEAETDNIrhasQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVAV--YFGFSYLGELNFghygvgVT 286
Cdd:TIGR00957 503 LNGIKVLKLYAWELAFLDKV----EGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALitFAVYVTVDENNI------LD 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 287 LMSGFLALILAPEFFQPLRDLGTFYHAKAQAIGAADSLKTFM-EKPLAQETRGEKLLSDNEPIGLEARDAIVKSPEGK-- 363
Cdd:TIGR00957 573 AEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLsHEELEPDSIERRTIKPGEGNSITVHNATFTWARDLpp 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 364 ILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVelrdldasrwhrlLSWVGQNPQLPAATLREN 442
Cdd:TIGR00957 653 TLNG-ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMdKVEGHVHMKGS-------------VAYVPQQAWIQNDSLREN 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLLAWPeASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQ 522
Cdd:TIGR00957 719 ILFGKA-LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695777692 523 RVMQALFNAS---SQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAALL 581
Cdd:TIGR00957 798 HIFEHVIGPEgvlKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
370-581 |
3.33e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.59 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRwhRLLSWVGQNPQL-PAATLRENVLLAW 447
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLpPDSGRILWNGQDLTALPPAE--RPVSMLFQENNLfPHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 P------EASEAQLQLALDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSE 521
Cdd:COG3840 97 RpglkltAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 522 QRvMQALFN---ASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQLAMANGP--FAALL 581
Cdd:COG3840 166 QE-MLDLVDelcRERGLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLDGEPPpaLAAYL 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
350-566 |
5.69e-22 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 95.06 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLL---NALtgFLPYDGSLLVNGVELRDLDASRWHRLLS 426
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMkmiNRL--IEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 427 WVGQNPQL-PAATLRENV-----LLAWPEASEaqlqlaldKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARAL 500
Cdd:cd03295 79 YVIQQIGLfPHMTVEENIalvpkLLKWPKEKI--------RERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695777692 501 LVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQ--QTTLMVTHQL-EGIADWDAIWVMQDGQIVEQGT 566
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGT 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
368-545 |
5.77e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 95.54 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 368 PLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRwhrllSWVGQNPQL-PAATLRENVLL 445
Cdd:COG1116 29 DVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEkPTSGEVLVDGKPVTGPGPDR-----GVVFQEPALlPWLTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 446 AwPEAseAQLQLALDKAWVSEFISQlpqgintpVG--DQAGR----LSVGQAQRIAVARALLVPCRLLLLDEPAASLDAH 519
Cdd:COG1116 104 G-LEL--RGVPKAERRERARELLEL--------VGlaGFEDAyphqLSGGMRQRVAIARALANDPEVLLMDEPFGALDAL 172
|
170 180
....*....|....*....|....*....
gi 695777692 520 SEQRvMQALF---NASSQQTTLMVTHQLE 545
Cdd:COG1116 173 TRER-LQDELlrlWQETGKTVLFVTHDVD 200
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
370-566 |
6.46e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 95.06 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELrDLDASRWHRLLSWVG---QNPQL-PAATLRENVL 444
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTITVDGEDL-TDSKKDINKLRRKVGmvfQQFNLfPHLTVLENVT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 445 LA------WP--EASEAQLQLaLDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:COG1126 100 LApikvkkMSkaEAEERAMEL-LERVGLADKADAYP-----------AQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 517 DAhsE-----QRVMQALfnASSQQTTLMVTHQLE---GIADWdaIWVMQDGQIVEQGT 566
Cdd:COG1126 168 DP--ElvgevLDVMRDL--AKEGMTMVVVTHEMGfarEVADR--VVFMDGGRIVEEGP 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
369-570 |
1.50e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 99.67 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENvLLAW 447
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFN-IDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQA 527
Cdd:PLN03232 1334 SEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695777692 528 LFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQL 570
Cdd:PLN03232 1414 IREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-321 |
1.95e-21 |
|
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: 94.91 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 24 LMISRALGVISGLLIVGQAWLLARILHRMIMENIPATALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVL 103
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 104 DRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFMALV 183
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 184 GMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIAL 263
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 264 VaVYFG--FSYLGELNFGhygvgvTLMSGFLALILapeFFQPLRDLGTFYHAKAQAIGAA 321
Cdd:cd18778 241 V-LGFGgrLVLAGELTIG------DLVAFLLYLGL---FYEPITSLHGLNEMLQRALAGA 290
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
369-564 |
2.20e-21 |
|
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: 92.92 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRwhrllSWVGQNPQL-PAATLRENVLL- 445
Cdd:cd03293 23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsGEVLVDGEPVTGPGPDR-----GYVFQQDALlPWLTVLDNVALg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 446 ------AWPEASEAQLQLaLDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAH 519
Cdd:cd03293 98 lelqgvPKAEARERAEEL-LELVGLSGFENAYP-----------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695777692 520 SEQRVMQALFN--ASSQQTTLMVTHQL-EGIADWDAIWVM--QDGQIVEQ 564
Cdd:cd03293 166 TREQLQEELLDiwRETGKTVLLVTHDIdEAVFLADRVVVLsaRPGRIVAE 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
233-581 |
3.08e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 98.89 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 233 QDFRQRTMEVLRLAFLSSGVLEF-FTSLSIALVAVYFGFSYLgelnfghYGVGVTLMSGFLALILapefFQPLR-DLGTF 310
Cdd:PLN03232 506 QGIRNEELSWFRKAQLLSAFNSFiLNSIPVVVTLVSFGVFVL-------LGGDLTPARAFTSLSL----FAVLRsPLNML 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 311 YHAKAQAIGAADSLKTFMEKPLAQEtrgeKLLSDNEP-------IGLEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVG 383
Cdd:PLN03232 575 PNLLSQVVNANVSLQRIEELLLSEE----RILAQNPPlqpgapaISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVG 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 384 QSGSGKSSLLNALTGFLPY--DGSLLVNGVelrdldasrwhrlLSWVGQNPQLPAATLRENVLLAWPEASEAQLQlALDK 461
Cdd:PLN03232 651 GTGEGKTSLISAMLGELSHaeTSSVVIRGS-------------VAYVPQVSWIFNATVRENILFGSDFESERYWR-AIDV 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 462 AWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQ-QTTLMV 540
Cdd:PLN03232 717 TALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKgKTRVLV 796
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 695777692 541 THQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAALL 581
Cdd:PLN03232 797 TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
370-570 |
3.58e-21 |
|
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: 92.63 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWHRLLSWVG---QNPQL-PAATLRENVL 444
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTsGSVLIDGTDINKLKGKALRQLRRQIGmifQQFNLiERLSVLENVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 445 LA--------------WPEAsEAQLQL-ALDKAWVSEFISQlpqgintpvgdQAGRLSVGQAQRIAVARALLVPCRLLLL 509
Cdd:cd03256 101 SGrlgrrstwrslfglFPKE-EKQRALaALERVGLLDKAYQ-----------RADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 510 DEPAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:cd03256 169 DEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAREYaDRIVGLKDGRIVFDGPPAEL 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-566 |
5.52e-21 |
|
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: 96.51 E-value: 5.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 333 AQETRGEKLLSDNEPIgLEARD-----AIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSL 406
Cdd:COG1123 245 AARGRAAPAAAAAEPL-LEVRNlskryPVRGKGGVRAVDD-VSLTLRRGETLGLVGESGSGKSTLARLLLGLLrPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 407 LVNGVELRDLDASRWHRLLSWVG---QNP--QL-PAATLRENV---LLAWPEASEAQLqlaldKAWVSEFISQlpqgint 477
Cdd:COG1123 323 LFDGKDLTKLSRRSLRELRRRVQmvfQDPysSLnPRMTVGDIIaepLRLHGLLSRAER-----RERVAELLER------- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 478 pVG---DQAGR----LSVGQAQRIAVARALLVPCRLLLLDEPAASLDAhSEQRVMQALFNASSQQ---TTLMVTHQLEGI 547
Cdd:COG1123 391 -VGlppDLADRypheLSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAQILNLLRDLQRElglTYLFISHDLAVV 468
|
250 260
....*....|....*....|
gi 695777692 548 ADW-DAIWVMQDGQIVEQGT 566
Cdd:COG1123 469 RYIaDRVAVMYDGRIVEDGP 488
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
368-565 |
6.60e-21 |
|
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: 91.40 E-value: 6.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 368 PLNF--TLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASRwhRLLSWVGQ-NPQLPAATLRENV 443
Cdd:cd03298 14 PMHFdlTFAQGEITAIVGPSGSGKSTLLNLIAGFeTPQSGRVLINGVDVTAAPPAD--RPVSMLFQeNNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAW-------PEASEAqLQLALDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:cd03298 92 GLGLspglkltAEDRQA-IEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695777692 517 DAHSEQRvMQALFNASSQQ---TTLMVTHQLEGIADWDA-IWVMQDGQIVEQG 565
Cdd:cd03298 160 DPALRAE-MLDLVLDLHAEtkmTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
369-559 |
9.43e-21 |
|
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: 91.24 E-value: 9.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGV----ELRDLDASRWHRLLSWVGQNPQLPAATLRENV 443
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMqTLEGKVHWSNKnesePSFEATRSRNRYSVAYAAQKPWLLNATVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAWPeASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQR 523
Cdd:cd03290 100 TFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 695777692 524 VMQA---LFNASSQQTTLMVTHQLEGIADWDAIWVMQDG 559
Cdd:cd03290 179 LMQEgilKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
361-586 |
1.22e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 96.77 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 361 EGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTG-FLPYDGSLLVngvelrdldasrwHRLLSWVGQNPQLPAATL 439
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSqFEISEGRVWA-------------ERSIAYVPQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 440 RENVLLaWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAH 519
Cdd:PTZ00243 738 RGNILF-FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 520 SEQRVMQALF-NASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLaMANGPFAALLAHRQE 586
Cdd:PTZ00243 817 VGERVVEECFlGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADF-MRTSLYATLAAELKE 883
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
376-581 |
1.68e-20 |
|
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: 91.51 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 376 GKRVVLVGQSGSGKSSLLNALTGFLP-YDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLlawPE--ASE 452
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD---PEckCTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 453 AQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNAS 532
Cdd:cd03288 124 DRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695777692 533 SQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQL-AMANGPFAALL 581
Cdd:cd03288 204 ADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLlAQEDGVFASLV 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
361-562 |
2.86e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.92 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 361 EGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWHRLLSWVGQNPQL---PA 436
Cdd:COG1101 18 EKRALDG-LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDsGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 437 ATLRENVLLAWPEASEAQLQLALDKAWVSEF---ISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPA 513
Cdd:COG1101 97 MTIEENLALAYRRGKRRGLRRGLTKKRRELFrelLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 514 ASLDAHSEQRVMQALFNASSQQ--TTLMVTHQLEgiadwDAI------WVMQDGQIV 562
Cdd:COG1101 177 AALDPKTAALVLELTEKIVEENnlTTLMVTHNME-----QALdygnrlIMMHEGRII 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
350-565 |
5.97e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.59 E-value: 5.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLL---NALTGFLP---YDGSLLVNGVELRDLDASRWHR 423
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDG-VNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPearVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 424 LLSWVGQNPQ-LPAATLRENVLLAWP----EASEAQLQ----LALDKAwvsefisQLPQGINTPVGDQAGRLSVGQAQRI 494
Cdd:PRK14247 83 RVQMVFQIPNpIPNLSIFENVALGLKlnrlVKSKKELQervrWALEKA-------QLWDEVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 495 AVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTH---QLEGIADWDAIwvMQDGQIVEQG 565
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDYVAF--LYKGQIVEWG 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
369-561 |
7.11e-20 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 88.36 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELrDLDASRWHRLLSWVG---QNPQL-PAATLRENV 443
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTIIIDGLKL-TDDKKNINELRQKVGmvfQQFNLfPHLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLA------WP--EASEAQLQLaLDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAAS 515
Cdd:cd03262 98 TLApikvkgMSkaEAEERALEL-LEKVGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695777692 516 LD---AHSEQRVMQALfnASSQQTTLMVTHQLeGIAD--WDAIWVMQDGQI 561
Cdd:cd03262 166 LDpelVGEVLDVMKDL--AEEGMTMVVVTHEM-GFARevADRVIFMDDGRI 213
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
29-307 |
7.26e-20 |
|
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: 90.14 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 29 ALGVISGLLIVG----QAWLLARILHRMIMENIPATALVLP-----FIVLVLIFVLRAWVVWLRErvgfYAGQHIRYEIR 99
Cdd:cd18544 2 ILALLLLLLATAlellGPLLIKRAIDDYIVPGQGDLQGLLLlallyLGLLLLSFLLQYLQTYLLQ----KLGQRIIYDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 100 RQVLDRLQQAGPAWIQGKPAGSWATLV---LEQIDDMhdyYARYLPQMtLAASVPLL-IVITIFPINWAAALILLGTAPL 175
Cdd:cd18544 78 RDLFSHIQRLPLSFFDRTPVGRLVTRVtndTEALNEL---FTSGLVTL-IGDLLLLIgILIAMFLLNWRLALISLLVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 176 IPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEF 255
Cdd:cd18544 154 LLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVEL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 695777692 256 FTSLSIALVAVYFGFSYL-GELNFGhygvgvTLMSgFLALILapEFFQPLRDL 307
Cdd:cd18544 234 LSSLALALVLWYGGGQVLsGAVTLG------VLYA-FIQYIQ--RFFRPIRDL 277
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
369-580 |
1.43e-19 |
|
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: 93.47 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENvLLAW 447
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINeSAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN-LDPF 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQA 527
Cdd:TIGR00957 1384 SQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 1463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695777692 528 LFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAAL 580
Cdd:TIGR00957 1464 IRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
356-565 |
1.89e-19 |
|
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: 86.93 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 356 IVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASrwHRLLSWVGQNPQL 434
Cdd:cd03301 6 VTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLeEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 435 -PAATLRENvlLAWPEASEAQLQLALDK--AWVSEFIsqlpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDE 511
Cdd:cd03301 84 yPHMTVYDN--IAFGLKLRKVPKDEIDErvREVAELL-----QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 512 PAASLDAH------SEQRVMQALFNAssqqTTLMVTH-QLEGIADWDAIWVMQDGQIVEQG 565
Cdd:cd03301 157 PLSNLDAKlrvqmrAELKRLQQRLGT----TTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
363-570 |
2.39e-19 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 87.34 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 363 KILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVG---QNpqlpAA- 437
Cdd:COG1127 19 VVLDG-VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPDSGEILVDGQDITGLSEKELYELRRRIGmlfQG----GAl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 438 ----TLRENV---LLAWPEASEAQL-QLALDK-AWV--SEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCRL 506
Cdd:COG1127 94 fdslTVFENVafpLREHTDLSEAEIrELVLEKlELVglPGAADKMP-----------SELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695777692 507 LLLDEPAASLDAHSEQRV------MQALFNAssqqTTLMVTHQLE---GIADWdaIWVMQDGQIVEQGTYSQL 570
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIdelireLRDELGL----TSVVVTHDLDsafAIADR--VAVLADGKIIAEGTPEEL 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
322-543 |
2.48e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.79 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 322 DSLKTFMEKPLAQETRGEKLLSDNEPiGLEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP 401
Cdd:COG4178 336 AGFEEALEAADALPEAASRIETSEDG-ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 402 Y-DGSllvngVELRDLDasrwhRLLsWVGQNPQLPAATLREnvLLAWPEA----SEAQLQLALDKAWVSEFISQLPQgin 476
Cdd:COG4178 415 YgSGR-----IARPAGA-----RVL-FLPQRPYLPLGTLRE--ALLYPATaeafSDAELREALEAVGLGHLAERLDE--- 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 477 tpVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQ 543
Cdd:COG4178 479 --EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
368-581 |
4.93e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.56 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 368 PLNFTL--PAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRwhRLLSWVGQ-NPQLPAATLRENV 443
Cdd:PRK10771 15 PMRFDLtvERGERVAILGPSGAGKSTLLNLIAGFLTPAsGSLTLNGQDHTTTPPSR--RPVSMLFQeNNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLA------WPEASEAQLQLALDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLD 517
Cdd:PRK10771 93 GLGlnpglkLNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695777692 518 AHSEQRVMQALFNASSQQ--TTLMVTHQLEgiadwDAI------WVMQDGQIVEQGTYSQLAMANGPFAALL 581
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERqlTLLMVSHSLE-----DAAriaprsLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
369-561 |
6.37e-19 |
|
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: 84.37 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDlDASRWHRLLSWVGQNPQLPAA-TLRENVlla 446
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTVRENL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 447 wpeaseaqlqlaldkawvsefisqlpqgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQ 526
Cdd:cd03230 95 --------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 695777692 527 ALFNASSQQTT-LMVTHQL---EGIADWdaIWVMQDGQI 561
Cdd:cd03230 137 LLRELKKEGKTiLLSSHILeeaERLCDR--VAILNNGRI 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
369-570 |
1.67e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.84 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTG-FLPYDGSLLVNGVELRDldASRW--HRLLSWVGQNP--QLPAATLRENV 443
Cdd:PRK13635 26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlLLPEAGTITVGGMVLSE--ETVWdvRRQVGMVFQNPdnQFVGATVQDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAW-------PEASEaQLQLALDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:PRK13635 104 AFGLenigvprEEMVE-RVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQPDIIILDEATSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 517 DAHSEQRVMQALFNASSQQ--TTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK13635 172 DPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
369-570 |
4.19e-18 |
|
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: 83.78 E-value: 4.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVEL-----RDLDASRwhRLLSWVGQNPQLPAA-TLRE 441
Cdd:cd03258 24 VSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVDGTDLtllsgKELRKAR--RRIGMIFQHFNLLSSrTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 442 NVllAWPeaseaqLQLA-LDKAWVSEFISQLPQGINtpVGDQAGR----LSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:cd03258 102 NV--ALP------LEIAgVPKAEIEERVLELLELVG--LEDKADAypaqLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 517 DAHSEQRVMQAL--FNASSQQTTLMVTHQLEGIAD-WDAIWVMQDGQIVEQGTYSQL 570
Cdd:cd03258 172 DPETTQSILALLrdINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
361-570 |
4.60e-18 |
|
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: 83.71 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 361 EGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWHRL--------------- 424
Cdd:cd03261 12 GRTVLKG-VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDISGLSEAELYRLrrrmgmlfqsgalfd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 425 -LSwVGQNPQLPaatLRENVLLawPEAS-EAQLQLALDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLV 502
Cdd:cd03261 91 sLT-VFENVAFP---LREHTRL--SEEEiREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 503 PCRLLLLDEPAASLD---AHSEQRVMQALfNASSQQTTLMVTHQLE---GIADWdaIWVMQDGQIVEQGTYSQL 570
Cdd:cd03261 154 DPELLLYDEPTAGLDpiaSGVIDDLIRSL-KKELGLTSIMVTHDLDtafAIADR--IAVLYDGKIVAEGTPEEL 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
24-324 |
5.46e-18 |
|
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: 84.78 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 24 LMISRALGVISGLLIVGQAWLLARILHRMIMENIPATALVLPFIVlVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVL 103
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAI-IGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 104 DRLQQAGPAWIQGKPAGSWATLVL---EQIddmhdyyarylpQMTLAASV------PLLIVITI---FPINWAAALILLG 171
Cdd:cd18552 80 DKLLRLPLSFFDRNSSGDLISRITndvNQV------------QNALTSALtvlvrdPLTVIGLLgvlFYLDWKLTLIALV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 172 TAPLIPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSG 251
Cdd:cd18552 148 VLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSP 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 252 VLEFFTSLSIALVAVYFGFSYL-GELNFGhygvgvTLMSGFLALILApefFQPLRDLGTFYHAKAQAIGAADSL 324
Cdd:cd18552 228 LMELLGAIAIALVLWYGGYQVIsGELTPG------EFISFITALLLL---YQPIKRLSNVNANLQRGLAAAERI 292
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
369-563 |
8.65e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.41 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTG-FLPYDGSLLVNGVELRDLDASRWHRL---LSWVGQNPQL-PAATLRENV 443
Cdd:COG2884 21 VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPTSGQVLVNGQDLSRLKRREIPYLrrrIGVVFQDFRLlPDRTVYENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLA-----WPEAS-EAQLQLALDkaWV--SEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAAS 515
Cdd:COG2884 101 ALPlrvtgKSRKEiRRRVREVLD--LVglSDKAKALPH-----------ELSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695777692 516 LDAHSEQRVMQALFNASSQQTT-LMVTHQLEGIADWDA-IWVMQDGQIVE 563
Cdd:COG2884 168 LDPETSWEIMELLEEINRRGTTvLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
350-561 |
9.31e-18 |
|
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: 83.75 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPE-GKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVNGVELRDLDASRWHRLLSWV 428
Cdd:cd03289 3 MTVKDLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 429 GQNPQLPAATLRENvLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLL 508
Cdd:cd03289 83 PQKVFIFSGTFRKN-LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695777692 509 LDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQI 561
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
354-560 |
9.34e-18 |
|
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: 81.08 E-value: 9.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 354 DAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASR--WHRLLSWVGQ 430
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEePDSGSILIDGEDLTDLEDELppLRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 431 NPQL-PAATLRENVLLAwpeaseaqlqlaldkawvsefisqlpqgintpvgdqagrLSVGQAQRIAVARALLVPCRLLLL 509
Cdd:cd03229 84 DFALfPHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 510 DEPAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQLE---GIAdwDAIWVMQDGQ 560
Cdd:cd03229 125 DEPTSALDPITRREVRALLksLQAQLGITVVLVTHDLDeaaRLA--DRVVVLRDGK 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
369-565 |
9.56e-18 |
|
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: 82.34 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGkRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRD----LDASRWHRLLSWVGQNPQL-PAATLREN 442
Cdd:cd03297 17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEkPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALfPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLLAWPEASEAQLQLALDKAWVSEFISQLpqgintpVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQ 522
Cdd:cd03297 96 LAFGLKRKRNREDRISVDELLDLLGLDHL-------LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695777692 523 RVMQAL--FNASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQG 565
Cdd:cd03297 169 QLLPELkqIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
369-542 |
2.09e-17 |
|
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: 81.30 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQ----LPAATLRENV 443
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQdfrlLPDRNVYENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAWpEASEAQLQLALDKawVSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQR 523
Cdd:cd03292 100 AFAL-EVTGVPPREIRKR--VPAALELV--GLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180
....*....|....*....|.
gi 695777692 524 VMQaLFNASSQQ--TTLMVTH 542
Cdd:cd03292 175 IMN-LLKKINKAgtTVVVATH 194
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
369-570 |
2.58e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 86.33 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENvLLAW 447
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVeLERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN-LDPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSE---QRV 524
Cdd:PLN03130 1337 NEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDaliQKT 1416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695777692 525 MQALFNASsqqTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQL 570
Cdd:PLN03130 1417 IREEFKSC---TMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
369-570 |
5.84e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.08 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFlpYD--------------------------------------------- 403
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRF--YDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeg 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 404 ------------GSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLRENVLLAWPEASEAQLQLALDKAWVSEFISQL 471
Cdd:PTZ00265 1265 gsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESL 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 472 PQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQ--QTTLMVTHQLEGIAD 549
Cdd:PTZ00265 1345 PNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKadKTIITIAHRIASIKR 1424
|
250 260
....*....|....*....|....*.
gi 695777692 550 WDAIWVMQD----GQIVE-QGTYSQL 570
Cdd:PTZ00265 1425 SDKIVVFNNpdrtGSFVQaHGTHEEL 1450
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
369-566 |
7.88e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.90 E-value: 7.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSL---LNALtgFLPYDGSLLVNGVELRDLDaSRW--HRLLSWVGQNP--QLPAATLRE 441
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIakhMNAL--LIPSEGKVYVDGLDTSDEE-NLWdiRNKAGMVFQNPdnQIVATIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 442 NV------LLAWPEASEAQLQLALDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAAS 515
Cdd:PRK13633 106 DVafgpenLGIPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695777692 516 LDAHSEQRVMQAL--FNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:PRK13633 175 LDPSGRREVVNTIkeLNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
347-565 |
1.77e-16 |
|
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: 77.98 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 347 PIGLEARDAIVKSPEG------KILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPY---DGSLLVNGvelRDLD 417
Cdd:cd03213 1 GVTLSFRNLTVTVKSSpsksgkQLLKN-VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgvSGEVLING---RPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 418 ASRWHRLLSWVGQNPQL-PAATLRENVLLAwpeaseAQLQlaldkawvsefisqlpqgintpvgdqagRLSVGQAQRIAV 496
Cdd:cd03213 77 KRSFRKIIGYVPQDDILhPTLTVRETLMFA------AKLR----------------------------GLSGGERKRVSI 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695777692 497 ARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVT-HQL--EGIADWDAIWVMQDGQIVEQG 565
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSiHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
369-569 |
2.42e-16 |
|
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: 78.63 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDAS-RWHRLLSWVGQNPQL-PAATLRENVLL 445
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrPTSGSVLFDGEDITGLPPHeIARLGIGRTFQIPRLfPELTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 446 A---------WPEASEAQLQLALDKAWvsEFISQLpqGInTPVGDQ-AGRLSVGQAQRIAVARALLVPCRLLLLDEPAAS 515
Cdd:cd03219 99 AaqartgsglLLARARREEREARERAE--ELLERV--GL-ADLADRpAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 516 LdAHSEQRVMQALFN--ASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQ 569
Cdd:cd03219 174 L-NPEETEELAELIRelRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
350-548 |
2.90e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.53 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASrWHRLLSWV 428
Cdd:cd03231 1 LEADELTCERDGRALFSG-LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLaGRVLLNGGPLDFQRDS-IARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 429 GQNPQLPAA-TLRENVLLAWPEASEAQLQLALDKAWVSEFiSQLPqgintpvgdqAGRLSVGQAQRIAVARALLVPCRLL 507
Cdd:cd03231 79 GHAPGIKTTlSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695777692 508 LLDEPAASLDAHSEQRVMQALFNASSQ-QTTLMVTHQLEGIA 548
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMAGHCARgGMVVLTTHQDLGLS 189
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-415 |
3.02e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 81.77 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 20 SRRWLMISRALGVISGLLIvgqAWLLARILHRMIMENIPATALVLPFIVLVLIFVL-RAWVVWLRERVGfyagQHIRYEI 98
Cdd:COG4615 11 SRWLLLLALLLGLLSGLAN---AGLIALINQALNATGAALARLLLLFAGLLVLLLLsRLASQLLLTRLG----QHAVARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 99 RRQVLDR--------LQQAGPAWIQgkpagswATLVlEQIDDMHDYYARyLPQMTLAASVPLLIVITIFPINWAAALILL 170
Cdd:COG4615 84 RLRLSRRilaaplerLERIGAARLL-------AALT-EDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFLLTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 171 gtaplipLFMALVGMGAAEANRR--NFLALAR-----LSGHFLDRLRGMETLRLfHRGEAE---TDNIRHASQDFRQRTM 240
Cdd:COG4615 155 -------VLLGLGVAGYRLLVRRarRHLRRAReaedrLFKHFRALLEGFKELKL-NRRRRRaffDEDLQPTAERYRDLRI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 241 EVLRLAFLSSGVLEFFTSLSIALVavYFGFSYLGELNfghygvgVTLMSGFLALILapeF-FQPLRDLGTFYHAKAQAIG 319
Cdd:COG4615 227 RADTIFALANNWGNLLFFALIGLI--LFLLPALGWAD-------PAVLSGFVLVLL---FlRGPLSQLVGALPTLSRANV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 320 AADSLKTFMEKPLAQETRGEKLLSDNEPIG---LEARDAI-----VKSPEGKILaGPLNFTLPAGKRVVLVGQSGSGKSS 391
Cdd:COG4615 295 ALRKIEELELALAAAEPAAADAAAPPAPADfqtLELRGVTyrypgEDGDEGFTL-GPIDLTIRRGELVFIVGGNGSGKST 373
|
410 420
....*....|....*....|....*
gi 695777692 392 LLNALTG-FLPYDGSLLVNGVELRD 415
Cdd:COG4615 374 LAKLLTGlYRPESGEILLDGQPVTA 398
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
350-565 |
3.20e-16 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 78.59 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP--YDGSLLVNGVELRDLDASRWHRLLSW 427
Cdd:COG1119 4 LELRNVTVRRGGKTILDD-ISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptYGNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 428 VgqNPQL-----PAATLRENVLLA-------WPEASEAQLQLAldKAWVSEF-ISQLpqgINTPVgdqaGRLSVGQAQRI 494
Cdd:COG1119 83 V--SPALqlrfpRDETVLDVVLSGffdsiglYREPTDEQRERA--RELLELLgLAHL---ADRPF----GTLSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 495 AVARALLVPCRLLLLDEPAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQG 565
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
369-584 |
3.60e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 78.21 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDldasRWHRLlSWVGQ----NPQLPAaTLRENV 443
Cdd:COG1121 25 VSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLpPTSGTVRLFGKPPRR----ARRRI-GYVPQraevDWDFPI-TVRDVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LL-AWPEASEAQLQLALDKAWVSEFISQLpqGI----NTPVGDqagrLSVGQAQRIAVARALLVPCRLLLLDEPAASLDA 518
Cdd:COG1121 99 LMgRYGRRGLFRRPSRADREAVDEALERV--GLedlaDRPIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 519 HSEQRVMQALFNASSQQTT-LMVTHQLEGIADW-DAIWVMqDGQIVEQGTYSQ------LAMANGPFAALLAHR 584
Cdd:COG1121 173 ATEEALYELLRELRREGKTiLVVTHDLGAVREYfDRVLLL-NRGLVAHGPPEEvltpenLSRAYGGPVALLAHG 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
370-566 |
3.92e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 79.29 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSL------LVNGVELRDLDASRWHrllswVGQNPQLPAATLREN 442
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPTSGTVtigervITAGKKNKKLKPLRKK-----VGIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLLA----WPE---ASEAQlqlALDKAwvSEFISQLpqGINTPVGDQAG-RLSVGQAQRIAVARALLVPCRLLLLDEPAA 514
Cdd:PRK13634 102 TVEKdicfGPMnfgVSEED---AKQKA--REMIELV--GLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 515 SLDAHSEQRVMQALFNASSQQ--TTLMVTHQLEGIADW-DAIWVMQDGQIVEQGT 566
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGT 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
369-545 |
4.49e-16 |
|
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: 77.19 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLdasrwHRLLSWVGQ----NPQLPAaTLRENV 443
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFGKPLEKE-----RKRIGYVPQrrsiDRDFPI-SVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLA---------WPEASEAQLQL-ALDKAWVSEFISQlpqgintpvgdQAGRLSVGQAQRIAVARALLVPCRLLLLDEPA 513
Cdd:cd03235 92 LMGlyghkglfrRLSKADKAKVDeALERVGLSELADR-----------QIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190
....*....|....*....|....*....|...
gi 695777692 514 ASLDAHSEQRVMQALFNASSQQTT-LMVTHQLE 545
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTiLVVTHDLG 193
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
23-322 |
4.94e-16 |
|
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: 79.09 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 23 WLMISRALGVISGLLIvgqAWLLARILHRMIMENIP--ATALVLPFI-VLVLIFVLRAWVVWLRERVGFYAGQHIRYEIR 99
Cdd:cd18563 3 LGFLLMLLGTALGLVP---PYLTKILIDDVLIQLGPggNTSLLLLLVlGLAGAYVLSALLGILRGRLLARLGERITADLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 100 RQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLF 179
Cdd:cd18563 80 RDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 180 MALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSL 259
Cdd:cd18563 160 SYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 260 SIALVaVYFGFSYL--GELNFGhygvgvTLMSgFLALILapEFFQPLRDLGTFYHAKAQAIGAAD 322
Cdd:cd18563 240 GTLIV-WYFGGRQVlsGTMTLG------TLVA-FLSYLG--MFYGPLQWLSRLNNWITRALTSAE 294
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
368-566 |
5.16e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 79.73 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 368 PLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRwhRLLSWVGQNPQL-PAATLRENvlL 445
Cdd:COG3839 21 DIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTsGEILIGGRDVTDLPPKD--RNIAMVFQSYALyPHMTVYEN--I 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 446 AWPeaseaqLQLA-LDKA-------WVSEfISQLpqgintpvGDQAGR----LSVGQAQRIAVARALLVPCRLLLLDEPA 513
Cdd:COG3839 97 AFP------LKLRkVPKAeidrrvrEAAE-LLGL--------EDLLDRkpkqLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 514 ASLDAHSeqRV-----MQALFnASSQQTTLMVTH-QLE--GIADWdaIWVMQDGQIVEQGT 566
Cdd:COG3839 162 SNLDAKL--RVemraeIKRLH-RRLGTTTIYVTHdQVEamTLADR--IAVMNDGRIQQVGT 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
369-570 |
6.08e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.67 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHR-LLSWVGQNPQLPAATLRE----- 441
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPTTGTVTVDDITITHKTKDKYIRpVRKRIGMVFQFPESQLFEdtver 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 442 -------NVLLAWPEASEAQLQLALDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAA 514
Cdd:PRK13646 106 eiifgpkNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSP-----------FQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695777692 515 SLDAHSEQRVMQAL--FNASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK13646 175 GLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKEL 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
370-585 |
8.55e-16 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 78.99 E-value: 8.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRW----HRLLSWVGQNPQL-PAATLRENV 443
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLErPDSGRIRLGGEVLQDSARGIFlpphRRRIGYVFQEARLfPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAWPEASEAQLQLALDKAwvsefISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQR 523
Cdd:COG4148 99 LYGRKRAPRAERRISFDEV-----VELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 524 VMQALFNASSQQTT--LMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQLaMANGPFAALLAHRQ 585
Cdd:COG4148 172 ILPYLERLRDELDIpiLYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEV-LSRPDLLPLAGGEE 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
287-558 |
8.82e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.23 E-value: 8.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 287 LMSGFLALILAPEFFQPLRdlgtfyhakaqAIGAADSLKTFM-EKPLAQETRGEKLLSDNEPIGLEARDAIVKSPEGKIL 365
Cdd:PTZ00265 332 LISMFMLTIILPNITEYMK-----------SLEATNSLYEIInRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 366 AGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVE-LRDLDASRWHRLLSWVGQNPQLPAATLRENV 443
Cdd:PTZ00265 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEGDIIINDSHnLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 ---------LLAWPEASE---------------AQLQLALD---------------------------------KAWVSE 466
Cdd:PTZ00265 481 kyslyslkdLEALSNYYNedgndsqenknkrnsCRAKCAGDlndmsnttdsneliemrknyqtikdsevvdvskKVLIHD 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 467 FISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFN--ASSQQTTLMVTHQL 544
Cdd:PTZ00265 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNlkGNENRITIIIAHRL 640
|
330
....*....|....
gi 695777692 545 EGIADWDAIWVMQD 558
Cdd:PTZ00265 641 STIRYANTIFVLSN 654
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
369-566 |
1.02e-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: 76.61 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRwhRLLSWVGQNPQL-PAATLRENVLLA 446
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDsGKILLNGKDITNLPPEK--RDISYVPQNYALfPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 447 WPEASEAQLQLALDKAWVSEFIsqlpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQ 526
Cdd:cd03299 96 LKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695777692 527 ALFNA--SSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGT 566
Cdd:cd03299 171 ELKKIrkEFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGK 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
350-566 |
1.06e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.43 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELrDLDASRWHRLLSWV 428
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSGEVLIKGEPI-KYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 429 G---QNP--QLPAATLRENVL-----LAWP-EASEAQLQLALDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVA 497
Cdd:PRK13639 81 GivfQNPddQLFAPTVEEDVAfgplnLGLSkEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 498 RALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMV-THQLEGIADW-DAIWVMQDGQIVEQGT 566
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIsTHDVDLVPVYaDKVYVMSDGKIIKEGT 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
354-566 |
1.23e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 76.51 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 354 DAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASRwhRLLSWVGQNP 432
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEILLDGKDITNLPPHK--RPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 433 QL-PAATLRENVllAWPeaseaqLQLA-LDKAWVSEFISQLPQGINtpVGDQAGR----LSVGQAQRIAVARALLVPCRL 506
Cdd:cd03300 82 ALfPHLTVFENI--AFG------LRLKkLPKAEIKERVAEALDLVQ--LEGYANRkpsqLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 507 LLLDEPAASLDAHSEQRvMQALFNASSQQ---TTLMVTH-QLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:cd03300 152 LLLDEPLGALDLKLRKD-MQLELKRLQKElgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
370-570 |
1.39e-15 |
|
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: 76.56 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLL------NALTGFLPYDGSLLVNGVELRD--LDASRWHRLLSWVGQNPQLPAATLRE 441
Cdd:TIGR00972 21 NLDIPKNQVTALIGPSGCGKSTLLrslnrmNDLVPGVRIEGKVLFDGQDIYDkkIDVVELRRRVGMVFQKPNPFPMSIYD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 442 NVLLAwPEASEAQLQLALDKAwVSEFISQ--LPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAH 519
Cdd:TIGR00972 101 NIAYG-PRLHGIKDKKELDEI-VEESLKKaaLWDEVKDRLHDSALGLSGGQQQRLCIARALAVEPEVLLLDEPTSALDPI 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695777692 520 SEQRVMQALFNASSQQTTLMVTH---QLEGIADWDAIwvMQDGQIVEQGTYSQL 570
Cdd:TIGR00972 179 ATGKIEELIQELKKKYTIVIVTHnmqQAARISDRTAF--FYDGELVEYGPTEQI 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
369-569 |
2.00e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 76.23 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWHRLlswvG-----QNPQL-PAATLRE 441
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTsGRILFDGRDITGLPPHRIARL----GiartfQNPRLfPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 442 NVLLA--------------WPEASEAQLQLALDKAWvsEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLL 507
Cdd:COG0411 99 NVLVAaharlgrgllaallRLPRARREEREARERAE--ELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 508 LLDEPAASLDAHSEQRVMQALFNASSQQ--TTLMVTHQLE---GIADWdaIWVMQDGQIVEQGTYSQ 569
Cdd:COG0411 175 LLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDlvmGLADR--IVVLDFGRVIAEGTPAE 239
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
130-547 |
2.42e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 79.95 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 130 IDDMhdyyaryLPqMTLAASVPLLIVI--TIFPINWAAALILLGTAPLIPLFMALvgmgaaeanRRNFL----------- 196
Cdd:TIGR01271 995 IDDM-------LP-LTLFDFIQLTLIVlgAIFVVSVLQPYIFIAAIPVAVIFIML---------RAYFLrtsqqlkqles 1057
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 197 -ALARLSGHFLDRLRGMETLRLFHRgEAETDNIRHASQDFRQRTMevlrlaFLSSGVLEFFtSLSIALVAVYFgFSYLGE 275
Cdd:TIGR01271 1058 eARSPIFSHLITSLKGLWTIRAFGR-QSYFETLFHKALNLHTANW------FLYLSTLRWF-QMRIDIIFVFF-FIAVTF 1128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 276 LNFGHYGVGvtlmSGFLALILApeffQPLRDLGTFYHAKAQAIgAADSL-----KTFMEKPLAQE-----------TRGE 339
Cdd:TIGR01271 1129 IAIGTNQDG----EGEVGIILT----LAMNILSTLQWAVNSSI-DVDGLmrsvsRVFKFIDLPQEeprpsggggkyQLST 1199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 340 KLLSDNE------PIG--LEARDAIVKSPE-GKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVNG 410
Cdd:TIGR01271 1200 VLVIENPhaqkcwPSGgqMDVQGLTAKYTEaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDG 1279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 411 VELRDLDASRWHRLLSWVGQNPQLPAATLRENvLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQ 490
Cdd:TIGR01271 1280 VSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN-LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGH 1358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 491 AQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQLEGI 547
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEAL 1415
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
369-566 |
2.78e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 77.45 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDAsrWHRLLSWVGQNPQL-PAATLRENV--- 443
Cdd:COG3842 24 VSLSIEPGEFVALLGPSGCGKTTLLRMIAGFEtPDSGRILLDGRDVTGLPP--EKRNVGMVFQDYALfPHLTVAENVafg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 --LLAWPEAsEAqlqlaldKAWVSEFISQLpqGIntpvGDQAGR----LSVGQAQRIAVARAllvpcrllllDEPAASLD 517
Cdd:COG3842 102 lrMRGVPKA-EI-------RARVAELLELV--GL----EGLADRyphqLSGGQQQRVALARAlapeprvlllDEPLSALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 518 AHSEQRVMQALFNAssQQ----TTLMVTH-QLE--GIADWdaIWVMQDGQIVEQGT 566
Cdd:COG3842 168 AKLREEMREELRRL--QRelgiTFIYVTHdQEEalALADR--IAVMNDGRIEQVGT 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
371-572 |
3.06e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.44 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 371 FTLPAGKRVVLVGQSGSGKSSLLnaLTGFLPYD---GSLLVNGVE-----LRDLdasrwHRLLSWVGQNPQLPAATLREN 442
Cdd:PTZ00243 1331 FRIAPREKVGIVGRTGSGKSTLL--LTFMRMVEvcgGEIRVNGREigaygLREL-----RRQFSMIPQDPVLFDGTVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLlAWPEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRL-LLLDEPAASLDAHSE 521
Cdd:PTZ00243 1404 VD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGfILMDEATANIDPALD 1482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695777692 522 QRVMQALFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAM 572
Cdd:PTZ00243 1483 RQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
369-545 |
3.14e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.51 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLL---NAL---TGflpydGSLLVNGVELRDLDAS-RWHRLLS-WVGQNPQL-PAATL 439
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLrciNKLeeiTS-----GDLIVDGLKVNDPKVDeRLIRQEAgMVFQQFYLfPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 440 RENVLL-------AWPEASEAQLQLALDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEP 512
Cdd:PRK09493 95 LENVMFgplrvrgASKEEAEKQARELLAKVGLAERAHHYP-----------SELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 695777692 513 AASLDA---HSEQRVMQALfnASSQQTTLMVTHQLE 545
Cdd:PRK09493 164 TSALDPelrHEVLKVMQDL--AEEGMTMVIVTHEIG 197
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
350-545 |
5.17e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 75.28 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGK----ILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRW--- 421
Cdd:COG4525 4 LTVRHVSVRYPGGGqpqpALQD-VSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSsGEITLDGVPVTGPGADRGvvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 422 --HRLLSWVgqnpqlpaaTLRENVLLAwpeaseaqLQLA-LDKA----WVSEFISQlpqgintpVG--DQAGR----LSV 488
Cdd:COG4525 83 qkDALLPWL---------NVLDNVAFG--------LRLRgVPKAerraRAEELLAL--------VGlaDFARRriwqLSG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 489 GQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRvMQALF---NASSQQTTLMVTHQLE 545
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQ-MQELLldvWQRTGKGVFLITHSVE 196
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
369-581 |
7.18e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 78.41 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGvelrdldasrwhrLLSWVGQNPQLPAATLRENVLLAW 447
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELePSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFGL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 pEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQA 527
Cdd:TIGR01271 512 -SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 528 -LFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAALL 581
Cdd:TIGR01271 591 cLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
364-571 |
8.25e-15 |
|
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: 73.62 E-value: 8.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 364 ILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP-YDGSLLVNGVELRDLDASRWHRL-LSWVGQNPQL-PAATLR 440
Cdd:cd03224 15 ILFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPpRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIfPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 441 ENVLLAWPEASEAQLQLALDkaWVSEFISQLPQGINTPvgdqAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHS 520
Cdd:cd03224 94 ENLLLGAYARRRAKRKARLE--RVYELFPRLKERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 521 EQRVMQALFN-ASSQQTTLMVTHQLE---GIAdwDAIWVMQDGQIVEQGTYSQLA 571
Cdd:cd03224 168 VEEIFEAIRElRDEGVTILLVEQNARfalEIA--DRAYVLERGRVVLEGTAAELL 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
350-566 |
8.67e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.42 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWV 428
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDD-VSLTLRPGEVVAILGPNGAGKSTLLRALSGELsPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 429 GQNPQLPAA-TLRENV---LLAWPEASEAQLQL---ALDKAWVSEFisqlpqgintpvgdqAGR----LSVGQAQRIAVA 497
Cdd:PRK13548 82 PQHSSLSFPfTVEEVVamgRAPHGLSRAEDDALvaaALAQVDLAHL---------------AGRdypqLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 498 RALLVPCRLLLL------DEPAASLDAHSEQRVMQALFN-ASSQQTT-LMVTHQLEGIADW-DAIWVMQDGQIVEQGT 566
Cdd:PRK13548 147 RVLAQLWEPDGPprwlllDEPTSALDLAHQHHVLRLARQlAHERGLAvIVVLHDLNLAARYaDRIVLLHQGRLVADGT 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
369-571 |
1.57e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.00 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTG-FLPYDGSLLVNGVELRDlDASRWHRllSWVG---QNP--QLPAATLREN 442
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGRVKVMGREVNA-ENEKWVR--SKVGlvfQDPddQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLLA------WPEASEAQLQLALDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:PRK13647 101 VAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 517 DAHSEQRVMQALFNASSQQTTLMV-THQLEGIADW-DAIWVMQDGQIVEQGTYSQLA 571
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVaTHDVDLAAEWaDQVIVLKEGRVLAEGDKSLLT 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
350-550 |
2.13e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.03 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVngvelrdldaSRWHRLLSWVG 429
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG----------MPEGEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 430 QNPQLPAATLRENVLLAWPEaseaqlqlaldkawvsefisqlpqgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLL 509
Cdd:cd03223 71 QRPYLPLGTLREQLIYPWDD-----------------------------------VLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695777692 510 DEPAASLDAHSEQRVMQALFNASSqqTTLMVTHQ--LEGIADW 550
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKELGI--TVISVGHRpsLWKFHDR 156
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
370-566 |
3.47e-14 |
|
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: 73.06 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRL----LSWVGQNPQL-PAATLRENV 443
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIePTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALlPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAW------PEASEAQLQLALDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLD 517
Cdd:cd03294 124 AFGLevqgvpRAEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695777692 518 AhSEQRVMQALF---NASSQQTTLMVTHQL-EGIADWDAIWVMQDGQIVEQGT 566
Cdd:cd03294 193 P-LIRREMQDELlrlQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGT 244
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
370-566 |
3.71e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 74.03 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELR-DLDASRwhRLLSWVGQNPQL-PAATLRENV--- 443
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLEtPDSGRIVLNGRDLFtNLPPRE--RRVGFVFQHYALfPHMTVAENIafg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAWPeASEAQLqlaldKAWVSEFIS--QLPqGIntpvgdqAGR----LSVGQAQRIAVARALLVPCRLLLLDEPAASLD 517
Cdd:COG1118 100 LRVRP-PSKAEI-----RARVEELLElvQLE-GL-------ADRypsqLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695777692 518 AHSEQRVMQALFN--ASSQQTTLMVTHQLE---GIAdwDAIWVMQDGQIVEQGT 566
Cdd:COG1118 166 AKVRKELRRWLRRlhDELGGTTVFVTHDQEealELA--DRVVVMNQGRIEQVGT 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
350-562 |
5.30e-14 |
|
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: 69.76 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDaIVKS-PEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDasrwhrllsw 427
Cdd:cd03216 1 LELRG-ITKRfGGVKALDG-VSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDsGEILVDGKEVSFAS---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 428 vgqnpqlPAATLRENVllawpeaseaqlqlaldkawvsEFISQLpqgintpvgdqagrlSVGQAQRIAVARALLVPCRLL 507
Cdd:cd03216 69 -------PRDARRAGI----------------------AMVYQL---------------SVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 508 LLDEPAASLDAHSEQRVMQALFNASSQQTT-LMVTHQLEGIADW-DAIWVMQDGQIV 562
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAvIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
355-566 |
6.00e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.83 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 355 AIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASrwHRLLSWVGQNPQ 433
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 434 L-PAATLRENVLLAW-----PEAS-EAQLQLALDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRL 506
Cdd:PRK09452 97 LfPHMTVFENVAFGLrmqktPAAEiTPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 507 LLLDEPAASLDaHSEQRVMQALFNASSQQ---TTLMVTH-QLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:PRK09452 166 LLLDESLSALD-YKLRKQMQNELKALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
369-570 |
6.43e-14 |
|
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: 72.78 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPY----DGSLLVNGVELRDLDASRWHRL----LSWVGQNP-------- 432
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgitSGEILFDGEDLLKLSEKELRKIrgreIQMIFQDPmtslnpvm 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 433 ----QLpAATLRENVLLAWPEASEAQLQLaLDKAwvsefisqlpqGINTPVgDQAGR----LSVGQAQRIAVARALLVPC 504
Cdd:COG0444 104 tvgdQI-AEPLRIHGGLSKAEARERAIEL-LERV-----------GLPDPE-RRLDRypheLSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 505 RLLLLDEPAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQL---EGIADWdaIWVMQDGQIVEQGTYSQL 570
Cdd:COG0444 170 KLLIADEPTTALDVTIQAQILNLLkdLQRELGLAILFITHDLgvvAEIADR--VAVMYAGRIVEEGPVEEL 238
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
369-566 |
6.46e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.55 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASR-WHRLLSWVGQNPQLPAATLRENVLLA 446
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLkPSSGTITIAGYHITPETGNKnLKKLRKKVSLVFQFPEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 447 WPEASEAQLQLALDKAWVS--EFISQLpqGINTPVGDQAG-RLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQR 523
Cdd:PRK13641 106 DVEFGPKNFGFSEDEAKEKalKWLKKV--GLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695777692 524 VMQALFN-ASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGT 566
Cdd:PRK13641 184 MMQLFKDyQKAGHTVILVTHNMDDVAEYaDDVLVLEHGKLIKHAS 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
369-566 |
9.22e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.58 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAA-TLRENV--- 443
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRELVayg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 ----LLAWPEAS---EAQLQLALDKAWVSEFisqlpqgINTPVGDqagrLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:PRK11231 101 rspwLSLWGRLSaedNARVNQAMEQTRINHL-------ADRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695777692 517 DAHSEQRVMQALFNASSQ-QTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGT 566
Cdd:PRK11231 170 DINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYcDHLVVLANGHVMAQGT 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
369-565 |
1.32e-13 |
|
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: 70.25 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVelrdldasrwhrlLSW-----VGQNPQLpaaTLREN 442
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDsGTVTVRGR-------------VSSllglgGGFNPEL---TGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLL--AWPEASEAQLQLALDkaWVSEFiSQLPQGINTPVgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHS 520
Cdd:cd03220 105 IYLngRLLGLSRKEIDEKID--EIIEF-SELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695777692 521 EQRVMQALFNASSQQTTL-MVTHQLEGIADW-DAIWVMQDGQIVEQG 565
Cdd:cd03220 178 QEKCQRRLRELLKQGKTViLVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
332-566 |
1.40e-13 |
|
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: 73.57 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 332 LAQETRGEKL-LSDNEPIGLEARDAIVKSPEGK-ILAGP---------LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL 400
Cdd:COG4172 257 LAAEPRGDPRpVPPDAPPLLEARDLKVWFPIKRgLFRRTvghvkavdgVSLTLRRGETLGLVGESGSGKSTLGLALLRLI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 401 PYDGSLLVNGVELRDLDASRWHRLLSW---VGQ------NPQLP-AATLRENVLLAWPEASEAQLQLA---------LDK 461
Cdd:COG4172 337 PSEGEIRFDGQDLDGLSRRALRPLRRRmqvVFQdpfgslSPRMTvGQIIAEGLRVHGPGLSAAERRARvaealeevgLDP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 462 AWVS----EFisqlpqgintpvgdqagrlSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALfnASSQQ-- 535
Cdd:COG4172 417 AARHryphEF-------------------SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLL--RDLQReh 475
|
250 260 270
....*....|....*....|....*....|....*.
gi 695777692 536 --TTLMVTHQL---EGIADWdaIWVMQDGQIVEQGT 566
Cdd:COG4172 476 glAYLFISHDLavvRALAHR--VMVMKDGKVVEQGP 509
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
369-570 |
1.51e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 71.28 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTG-FLPYDGSLLVNGVELRDLDASRWHRLLSWVGQNP--QLPAATLRENVLL 445
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGlFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 446 AWPEASEAQLQLA--LDKAWVSefISQLPQGINTPvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQR 523
Cdd:PRK13642 106 GMENQGIPREEMIkrVDEALLA--VNMLDFKTREP-----ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695777692 524 VMQALFNASSQQ--TTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK13642 179 IMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
369-583 |
1.59e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVEL---RDLDASRWHRLLSWVG---QNPQL-PAATLR 440
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLeMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGmvfQQYNLwPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 441 ENVL--------LAWPEASEAQLQLaLDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEP 512
Cdd:PRK11124 101 QNLIeapcrvlgLSKDQALARAEKL-LERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 513 AASLDAHSEQRVMqALFNASSQQ--TTLMVTHQLEgIADWDAIWV--MQDGQIVEQGTYSQLAMANGP-FAALLAH 583
Cdd:PRK11124 169 TAALDPEITAQIV-SIIRELAETgiTQVIVTHEVE-VARKTASRVvyMENGHIVEQGDASCFTQPQTEaFKNYLSH 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
369-562 |
1.61e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.60 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALtGFL--PYDGSLLVNGVELRDLDA---------------SRWHRLlswvgqn 431
Cdd:PRK10535 27 ISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLdkPTSGTYRVAGQDVATLDAdalaqlrrehfgfifQRYHLL------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 432 PQLPAAtlrENVLLAwpeASEAQLQLALDKAWVSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDE 511
Cdd:PRK10535 99 SHLTAA---QNVEVP---AVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695777692 512 PAASLDAHSEQRVMQALFNASSQ-QTTLMVTHQLEGIADWDAIWVMQDGQIV 562
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
369-581 |
1.67e-13 |
|
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: 71.04 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGvelrdldasrwhrLLSWVGQNPQLPAATLRENVLLAw 447
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELePSEGKIKHSG-------------RISFSSQFSWIMPGTIKENIIFG- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQA 527
Cdd:cd03291 122 VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 528 -LFNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQLAMANGPFAALL 581
Cdd:cd03291 202 cVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
369-574 |
2.19e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.67 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDldASRWHRLLSWVGQNPQL-PAATLRENV--- 443
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLeKPTEGQIFIDGEDVTH--RSIQQRDICMVFQSYALfPHMSLGENVgyg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 --LLAWPEASEAQ-----LQLALDKAWVSEFISQLpqgintpvgdqagrlSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:PRK11432 103 lkMLGVPKEERKQrvkeaLELVDLAGFEDRYVDQI---------------SGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695777692 517 DAHSeQRVMQALFNASSQQ---TTLMVTH-QLEGIADWDAIWVMQDGQIVEQGT----YSQ---LAMAN 574
Cdd:PRK11432 168 DANL-RRSMREKIRELQQQfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSpqelYRQpasRFMAS 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
369-572 |
4.74e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRD----------------LDASRWHRLLSWVGQN 431
Cdd:PRK13631 45 ISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkSKYGTIQVGDIYIGDkknnhelitnpyskkiKNFKELRRRVSMVFQF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 432 P--QLPAATLRENVL-----LAWPEASEAQL------QLALDkawvSEFISQLPQGintpvgdqagrLSVGQAQRIAVAR 498
Cdd:PRK13631 125 PeyQLFKDTIEKDIMfgpvaLGVKKSEAKKLakfylnKMGLD----DSYLERSPFG-----------LSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 499 ALLVPCRLLLLDEPAASLDAHSEQRVMQALFNA-SSQQTTLMVTHQLEGIAD-WDAIWVMQDGQIVEQGTYSQLAM 572
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFT 265
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
369-545 |
5.50e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.27 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGS------LLVNGVE-----LRDLDASRWHRllSWVGQNPQL-PA 436
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshieLLGRTVQregrlARDIRKSRANT--GYIFQQFNLvNR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 437 ATLRENVL-------------LAW--PEASEAQLQlALDKAWVSEFISQlpqgintpvgdQAGRLSVGQAQRIAVARALL 501
Cdd:PRK09984 101 LSVLENVLigalgstpfwrtcFSWftREQKQRALQ-ALTRVGMVHFAHQ-----------RVSTLSGGQQQRVAIARALM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695777692 502 VPCRLLLLDEPAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQLE 545
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVD 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
350-570 |
9.60e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.11 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGvelRDLDASR-----WHR 423
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILkPSSGRILFDG---KPIDYSRkglmkLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 424 LLSWVGQNP--QLPAATLRENVllawpeaSEAQLQLALDKAWVSEFISQLPQ--GINTPVGDQAGRLSVGQAQRIAVARA 499
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDV-------SFGAVNLKLPEDEVRKRVDNALKrtGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 500 LLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQ--TTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
350-570 |
1.23e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDaIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWHRL-LSW 427
Cdd:PRK15439 12 LCARS-ISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDsGTLEIGGNPCARLTPAKAHQLgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 428 VGQNPQL-PAATLRENVLLAWPEASEAQLQLAldkawvsEFISQLPQGINTPVgdQAGRLSVGQAQRIAVARALLVPCRL 506
Cdd:PRK15439 91 VPQEPLLfPNLSVKENILFGLPKRQASMQKMK-------QLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 507 LLLDEPAASLDAHSEQRVMQALFNASSQQTTLM-VTHQLEGI---ADWdaIWVMQDGQIVEQGTYSQL 570
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVfISHKLPEIrqlADR--ISVMRDGTIALSGKTADL 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
369-566 |
1.40e-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: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASRwhRLLSWVGQNPQL-PAATLRENV--- 443
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLeRPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALfRHMTVFDNVafg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAWPEA---SEAQLQLA----LDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:cd03296 99 LRVKPRSerpPEAEIRAKvhelLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695777692 517 DA--HSEQRVMQALFNASSQQTTLMVTH-QLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:cd03296 168 DAkvRKELRRWLRRLHDELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
350-565 |
1.60e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.94 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVNGvELR---------DLDASR 420
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKG-VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEG-EVRlfgrniyspDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 421 WHRLLSWVGQNPQ-LPAATLRENV--------LLAWPEASEAQLQLALDKAwvsefisQLPQGINTPVGDQAGRLSVGQA 491
Cdd:PRK14267 83 VRREVGMVFQYPNpFPHLTIYDNVaigvklngLVKSKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 492 QRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTH---QLEGIADWDAIWVMqdGQIVEQG 565
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLYL--GKLIEVG 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
354-565 |
1.95e-12 |
|
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: 66.45 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 354 DAIVKSPEGKILAGPLNFTLPAGKrVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDlDASRWHRLLSWVGQNP 432
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSsGTIRIDGQDVLK-QPQKLRRRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 433 QL-PAATLRENV-LLAW-----PEASEAQLQLALDKAwvsefisqlpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCR 505
Cdd:cd03264 82 GVyPNFTVREFLdYIAWlkgipSKEVKARVDEVLELV-----------NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 506 LLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQLEGIAD-WDAIWVMQDGQIVEQG 565
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
369-570 |
2.14e-12 |
|
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: 66.76 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGvelRDLDASRwHRLLSWVGQNPQ----LPAATLRENV 443
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTsGTAYING---YSIRTDR-KAARQSLGYCPQfdalFDELTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAwpeaseAQLQ---LALDKAWVSEFISQ--LPQGINTPVGDqagrLSVGQAQRIAVARALLVPCRLLLLDEPAASLDA 518
Cdd:cd03263 97 RFY------ARLKglpKSEIKEEVELLLRVlgLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 519 HSEQRVMQALFNASSQQTTLMVTHQL---EGIADWDAIwvMQDGQIVEQGTYSQL 570
Cdd:cd03263 167 ASRRAIWDLILEVRKGRSIILTTHSMdeaEALCDRIAI--MSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
369-570 |
2.24e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.84 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHR-LLSWVGQNPQLPAATLRENVLLA 446
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDIVVSSTSKQKEIKpVRKKVGVVFQFPESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 447 wpEASEAQLQLALDKAWVSEFISQLPQ--GINTPVGDQAG-RLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQR 523
Cdd:PRK13643 105 --DVAFGPQNFGIPKEKAEKIAAEKLEmvGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695777692 524 VMQaLFNASSQ--QTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK13643 183 MMQ-LFESIHQsgQTVVLVTHLMDDVADYaDYVYLLEKGHIISCGTPSDV 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
350-565 |
2.48e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 68.71 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWV 428
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDG-VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 429 GQNPQLPAA-TLRENV----------LLAWPEASEAQLQLALDKAWVSEFISQlpqgintPVGDqagrLSVGQAQRIAVA 497
Cdd:PRK09536 83 PQDTSLSFEfDVRQVVemgrtphrsrFDTWTETDRAAVERAMERTGVAQFADR-------PVTS----LSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 498 RALLVPCRLLLLDEPAASLDAHSEQRVMQALFN-ASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQG 565
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRlVDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAG 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
367-566 |
3.18e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 367 GPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVNGVELRDLDASRWHRLLSWVGQNpQLPAATLreNVLLA 446
Cdd:PRK03695 13 GPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQ-QTPPFAM--PVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 447 WPEASEAQLQLALDKAWVSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVA-------RALLVPCRLLLLDEPAASLDAh 519
Cdd:PRK03695 90 LTLHQPDKTRTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDV- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695777692 520 SEQRVMQALFNASSQQ--TTLMVTHQLEGIADW-DAIWVMQDGQIVEQGT 566
Cdd:PRK03695 167 AQQAALDRLLSELCQQgiAVVMSSHDLNHTLRHaDRVWLLKQGKLLASGR 216
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
349-566 |
3.26e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 349 GLEARDAIVKSPEGkilagpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASRWHRL--- 424
Cdd:PRK11308 20 GLFKPERLVKALDG------VSFTLERGKTLAVVGESGCGKSTLARLLTMIeTPTGGELYYQGQDLLKADPEAQKLLrqk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 425 LSWVGQNPQlpaATL--RENV--LLAWPEASEAQLQLALDKAWVSEFISQlpqgintpVG---DQAGR----LSVGQAQR 493
Cdd:PRK11308 94 IQIVFQNPY---GSLnpRKKVgqILEEPLLINTSLSAAERREKALAMMAK--------VGlrpEHYDRyphmFSGGQRQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 494 IAVARALLVPCRLLLLDEPAASLDAHSEQRV------MQALFNASsqqtTLMVTHQL---EGIAdwDAIWVMQDGQIVEQ 564
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdLQQELGLS----YVFISHDLsvvEHIA--DEVMVMYLGRCVEK 236
|
..
gi 695777692 565 GT 566
Cdd:PRK11308 237 GT 238
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
367-570 |
4.90e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 66.40 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 367 GPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNP-----------QL 434
Cdd:COG4167 30 KPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIePTSGEILINGHKLEYGDYKYRCKHIRMIFQDPntslnprlnigQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 435 PAATLRENVLLAwPEASEAQLQLALDKawvsefisqlpqgintpVG---DQAG----RLSVGQAQRIAVARALLVPCRLL 507
Cdd:COG4167 110 LEEPLRLNTDLT-AEEREERIFATLRL-----------------VGllpEHANfyphMLSSGQKQRVALARALILQPKII 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695777692 508 LLDEPAASLDahseqrvmqalFNASSQQTTLM-------------VTHQL---EGIAdwDAIWVMQDGQIVEQGTYSQL 570
Cdd:COG4167 172 IADEALAALD-----------MSVRSQIINLMlelqeklgisyiyVSQHLgivKHIS--DKVLVMHQGEVVEYGKTAEV 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
369-570 |
5.20e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.75 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNP--QLPAATLRENVLL 445
Cdd:PRK13652 23 INFIAPRNSRIAVIGPNGAGKSTLFRHFNGILkPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 446 AwpeaseaQLQLALDKAWVSEFISQLPQ--GINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQR 523
Cdd:PRK13652 103 G-------PINLGLDEETVAHRVSSALHmlGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695777692 524 VMqALFNASSQQ---TTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK13652 176 LI-DFLNDLPETygmTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-570 |
6.04e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.22 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 353 RDAIVKSPEGKILAgplnftlpagkrvvLVGQSGSGKSSLLNALTGFL-------PYDGSLLVNGVELRDLDASRWHRLL 425
Cdd:PRK14246 27 KDITIKIPNNSIFG--------------IMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQIDAIKLRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 426 SWVGQNPQ-LPAATLRENVllAWPEASEAQLQLALDKAWVSEFISQ--LPQGINTPVGDQAGRLSVGQAQRIAVARALLV 502
Cdd:PRK14246 93 GMVFQQPNpFPHLSIYDNI--AYPLKSHGIKEKREIKKIVEECLRKvgLWKEVYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 503 PCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVTH---QLEGIADWDAIwvMQDGQIVEQGTYSQL 570
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADYVAF--LYNGELVEWGSSNEI 239
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
370-549 |
6.12e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.53 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTG-FLPYDGSLLVN----GVELRDLDASRWHRL----LSWVGQN----PQLPA 436
Cdd:COG4778 31 SFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSILVRhdggWVDLAQASPREILALrrrtIGYVSQFlrviPRVSA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 437 ATLRENVLLAWPEASEAqlqlALDKA--WVSEFisQLPQgintpvgdqagRL--------SVGQAQRIAVARALLVPCRL 506
Cdd:COG4778 111 LDVVAEPLLERGVDREE----ARARAreLLARL--NLPE-----------RLwdlppatfSGGEQQRVNIARGFIADPPL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695777692 507 LLLDEPAASLDAHSEQRVMQALFNASSQQTT-LMVTHQLE---GIAD 549
Cdd:COG4778 174 LLLDEPTASLDAANRAVVVELIEEAKARGTAiIGIFHDEEvreAVAD 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
369-543 |
7.42e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASrWHRLLSWVGQNPQL-PAATLRENvlLA 446
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLArPDAGEVLWQGEPIRRQRDE-YHQDLLYLGHQPGIkTELTALEN--LR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 447 W-----PEASEAQLQLALDKAWVSEFiSQLPqgintpvgdqAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSe 521
Cdd:PRK13538 97 FyqrlhGPGDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG- 164
|
170 180
....*....|....*....|....
gi 695777692 522 QRVMQALFNASSQQ--TTLMVTHQ 543
Cdd:PRK13538 165 VARLEALLAQHAEQggMVILTTHQ 188
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
345-570 |
7.61e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.74 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 345 NEPIgLEARDaIVKS-PEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWH 422
Cdd:COG1129 1 AEPL-LEMRG-ISKSfGGVKALDG-VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDsGEILLDGEPVRFRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 423 RL-LSWVGQNPQL-PAATLRENVLLA----------WPEA-SEAQlqlaldkawvsEFISQLpqGINTPVGDQAGRLSVG 489
Cdd:COG1129 78 AAgIAIIHQELNLvPNLSVAENIFLGreprrgglidWRAMrRRAR-----------ELLARL--GLDIDPDTPVGDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 490 QAQRIAVARALLVPCRLLLLDEPAASLDAH-SEQ--RVMQALfnaSSQQTT-LMVTHQLE---GIAdwDAIWVMQDGQIV 562
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTEReVERlfRIIRRL---KAQGVAiIYISHRLDevfEIA--DRVTVLRDGRLV 219
|
....*...
gi 695777692 563 EQGTYSQL 570
Cdd:COG1129 220 GTGPVAEL 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
376-587 |
9.04e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.76 E-value: 9.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 376 GKRVVLVGQSGSGKSSLLNALTGFLP----YDGSLLVNGvelRDLDASRWHRLLSWVGQNPQ-LPAATLRENVLLawpea 450
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPkgvkGSGSVLLNG---MPIDAKEMRAISAYVQQDDLfIPTLTVREHLMF----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 451 sEAQLQLALD------KAWVSEFISQ--LPQGINTPVGdQAGR---LSVGQAQRIAVARALLVPCRLLLLDEPAASLDAH 519
Cdd:TIGR00955 123 -QAHLRMPRRvtkkekRERVDEVLQAlgLRKCANTRIG-VPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 520 SEQRVMQALFN-ASSQQTTLMVTHQ--LEGIADWDAIWVMQDGQIVEQGTYSQLAmangPFAALLAHRQEE 587
Cdd:TIGR00955 201 MAYSVVQVLKGlAQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQAV----PFFSDLGHPCPE 267
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
360-566 |
9.09e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.78 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 360 PEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHR-LLSWVGQNP--QLP 435
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKGKVLVSGIDTGDFSKLQGIRkLVGIVFQNPetQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 436 AATLRENV------LLAWPEASEAQLQLALDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLL 509
Cdd:PRK13644 92 GRTVEEDLafgpenLCLPPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 510 DEPAASLDAHSEQRVMQALFNASSQ-QTTLMVTHQLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
362-570 |
1.02e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 362 GKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQnpQLPAA--- 437
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQpPSEGEILLDAQPLESWSSKAFARKVAYLPQ--QLPAAegm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 438 TLRENVLLA-WPEASEAQLQLALDKAWVSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:PRK10575 101 TVRELVAIGrYPWHGALGRFGAADREKVEEAISLV--GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695777692 517 D-AHseQRVMQALFNASSQQ---TTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK10575 179 DiAH--QVDVLALVHRLSQErglTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAEL 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
369-561 |
1.27e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.08 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDL---------DAsrwhRLLSWvgqnpqlpaAT 438
Cdd:PRK11247 31 LDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGELLAGTAPLAEAredtrlmfqDA----RLLPW---------KK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 439 LRENVLLA----W-PEASEAQLQLAL-DKAwvsefisqlpqgintpvGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEP 512
Cdd:PRK11247 98 VIDNVGLGlkgqWrDAALQALAAVGLaDRA-----------------NEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695777692 513 AASLDAHSeqRV-MQALFNASSQQ---TTLMVTHQL-EGIADWDAIWVMQDGQI 561
Cdd:PRK11247 161 LGALDALT--RIeMQDLIESLWQQhgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
369-570 |
1.50e-11 |
|
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: 64.31 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVE-LRDLDASRwhRLLSWVGQNPQL-PAATLRENVLL 445
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRATVAGHDvVREPREVR--RRIGIVFQDLSVdDELTGWENLYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 446 awpeasEAQLQlALDKAWVSEFISQLPQGINtpVGDQAGRL----SVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSE 521
Cdd:cd03265 97 ------HARLY-GVPGAERRERIDELLDFVG--LLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695777692 522 Q---RVMQALfNASSQQTTLMVTHQLEGiADW--DAIWVMQDGQIVEQGTYSQL 570
Cdd:cd03265 168 AhvwEYIEKL-KEEFGMTILLTTHYMEE-AEQlcDRVAIIDHGRIIAEGTPEEL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
361-566 |
1.76e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.45 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 361 EGKILAGPL---NFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASR----WHRLLSWVGQ-N 431
Cdd:PRK11629 17 EGSVQTDVLhnvSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLSSAAkaelRNQKLGFIYQfH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 432 PQLPAATLRENV----LLAWPEASEAQlqlalDKAwvSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLL 507
Cdd:PRK11629 97 HLLPDFTALENVamplLIGKKKPAEIN-----SRA--LEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 508 LLDEPAASLDAHSEQRVMQALFNASSQQTT--LMVTHQLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
356-587 |
2.27e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.39 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 356 IVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTgFL--PYDGSLLVNGVELrdlDASR--------WHRLL 425
Cdd:PRK11264 9 LVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCIN-LLeqPEAGTIRVGDITI---DTARslsqqkglIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 426 SWVG---QNPQL-PAATLRENV----LLAWPEASEAQLQLA---LDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRI 494
Cdd:PRK11264 85 QHVGfvfQNFNLfPHRTVLENIiegpVIVKGEPKEEATARArelLAKVGLAGKETSYPR-----------RLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 495 AVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFN-ASSQQTTLMVTHQL---EGIADwDAIWvMQDGQIVEQgtysql 570
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMsfaRDVAD-RAIF-MDQGRIVEQ------ 225
|
250
....*....|....*..
gi 695777692 571 amanGPFAALLAHRQEE 587
Cdd:PRK11264 226 ----GPAKALFADPQQP 238
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
342-557 |
2.53e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.58 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 342 LSDNEPIgLEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASR 420
Cdd:PRK10247 1 MQENSPL-LQLQNVGYLAGDAKILNN-ISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLLFEGEDISTLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 421 WHRLLSWVGQNPQLPAATLRENVLLAW------PEasEAQLQLALDKAWVSEFIsqLPQGINTpvgdqagrLSVGQAQRI 494
Cdd:PRK10247 79 YRQQVSYCAQTPTLFGDTVYDNLIFPWqirnqqPD--PAIFLDDLERFALPDTI--LTKNIAE--------LSGGEKQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 495 AVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQ--TTLMVTHQLEGIADWDAIWVMQ 557
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITLQ 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
369-570 |
3.51e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.98 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNP--QLPAATLR----- 440
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLeAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVEddvaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 441 --ENVLLAWPEASEaQLQLALDKAWVSEFISQLPqgintpvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDA 518
Cdd:PRK13650 106 glENKGIPHEEMKE-RVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695777692 519 HSEQRVMQAL--FNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK13650 174 EGRLELIKTIkgIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
350-565 |
4.06e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.86 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDaIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDAsrWHRLLSWV 428
Cdd:PRK11607 20 LEIRN-LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDGVDLSHVPP--YQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 429 GQNPQL-PAATLRENVLLAWPEASEAQLQLA------LDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVARALL 501
Cdd:PRK11607 97 FQSYALfPHMTVEQNIAFGLKQDKLPKAEIAsrvnemLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 502 VPCRLLLLDEPAASLDAHSEQRVMQALFNASSQ--QTTLMVTH-QLEGIADWDAIWVMQDGQIVEQG 565
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
363-543 |
4.92e-11 |
|
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: 62.67 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 363 KILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD----GSLLVNGVElrdLDASRWHRLLSWVGQNPQL-PAA 437
Cdd:cd03234 21 RILND-VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttsGQILFNGQP---RKPDQFQKCVAYVRQDDILlPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 438 TLREN----VLLAWPE-ASEAQLQlaldKAWVSEFISQLPqgiNTPVGDQAGR-LSVGQAQRIAVARALLVPCRLLLLDE 511
Cdd:cd03234 97 TVRETltytAILRLPRkSSDAIRK----KRVEDVLLRDLA---LTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|...
gi 695777692 512 PAASLDAHSEQRVMQALFN-ASSQQTTLMVTHQ 543
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQlARRNRIVILTIHQ 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
350-549 |
5.04e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLD-ASRWHrllsW 427
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSG-LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLpPAAGTIKLDGGDIDDPDvAEACH----Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 428 VG-QNPQLPAATLRENvLLAW----------PEASEAQLQLALdkawvsefISQLPqgintpvgdqAGRLSVGQAQRIAV 496
Cdd:PRK13539 78 LGhRNAMKPALTVAEN-LEFWaaflggeeldIAAALEAVGLAP--------LAHLP----------FGYLSAGQKRRVAL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 497 ARALLVPCRLLLLDEPAASLDAHSeQRVMQALFNASSQQ--TTLMVTHQLEGIAD 549
Cdd:PRK13539 139 ARLLVSNRPIWILDEPTAALDAAA-VALFAELIRAHLAQggIVIAATHIPLGLPG 192
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
381-572 |
7.75e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.87 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 381 LVGQSGSGKSSLLNAL------------TGFLPYDG----SLLVNGVELRdldasrwhRLLSWVGQNPQLPAATLRENVL 444
Cdd:PRK14239 36 LIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGhniySPRTDTVDLR--------KEIGMVFQQPNPFPMSIYENVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 445 LAwpeaseaqLQLA--LDKAWVSEFISQLPQG------INTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:PRK14239 108 YG--------LRLKgiKDKQVLDEAVEKSLKGasiwdeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695777692 517 DAHSEQRVMQALFNASSQQTTLMVTH---QLEGIADWDAIWVmqDGQIVEQGTYSQLAM 572
Cdd:PRK14239 180 DPISAGKIEETLLGLKDDYTMLLVTRsmqQASRISDRTGFFL--DGDLIEYNDTKQMFM 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
336-566 |
1.09e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.03 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 336 TRGEKLLSDNEPIGLEARDA--------------------------IVK--SPEGKILAGPLNFTLPAGKRVVLVGQSGS 387
Cdd:TIGR01257 888 TREERALEKTEPLTEEMEDPehpegindsfferelpglvpgvcvknLVKifEPSGRPAVDRLNITFYENQITAFLGHNGA 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 388 GKSSLLNALTGFLP-YDGSLLVNGVELR-DLDASRWHrllswVGQNPQ----LPAATLRENVL----LAWPEASEAQLQL 457
Cdd:TIGR01257 968 GKTTTLSILTGLLPpTSGTVLVGGKDIEtNLDAVRQS-----LGMCPQhnilFHHLTVAEHILfyaqLKGRSWEEAQLEM 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 458 aldKAWVSEfisqlpQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTT 537
Cdd:TIGR01257 1043 ---EAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI 1113
|
250 260 270
....*....|....*....|....*....|.
gi 695777692 538 LMVTHQLEGiADW--DAIWVMQDGQIVEQGT 566
Cdd:TIGR01257 1114 IMSTHHMDE-ADLlgDRIAIISQGRLYCSGT 1143
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
363-570 |
1.13e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.36 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 363 KILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVNG-VEL-------RDLDASRWHRLLSWVGQNPQL 434
Cdd:PRK14258 21 KILEG-VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrVEFfnqniyeRRVNLNRLRRQVSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 435 PAATLRENV-----LLAWPEASEAQ--LQLALDKAwvsefisQLPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLL 507
Cdd:PRK14258 100 FPMSVYDNVaygvkIVGWRPKLEIDdiVESALKDA-------DLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 508 LLDEPAASLDAHSEQRVMQALFNAS--SQQTTLMVTH---QLEGIADWDAIWVMQD---GQIVEQGTYSQL 570
Cdd:PRK14258 173 LMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHnlhQVSRLSDFTAFFKGNEnriGQLVEFGLTKKI 243
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
358-566 |
1.21e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 62.76 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 358 KSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRD--LDASRWHRLLSWVGQNP-- 432
Cdd:PRK13637 15 GTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 433 QLPAATLRENVLLAwPEaseaqlQLALDKAWVSEFISQLPQGINTPVGDQAGR----LSVGQAQRIAVARALLVPCRLLL 508
Cdd:PRK13637 95 QLFEETIEKDIAFG-PI------NLGLSEEEIENRVKRAMNIVGLDYEDYKDKspfeLSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 509 LDEPAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGT 566
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGT 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
350-566 |
1.30e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.20 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIV--KSPEGKILA-GPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP----YDGSLLVNGVELRDLDASRWH 422
Cdd:PRK09473 13 LDVKDLRVtfSTPDGDVTAvNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangrIGGSATFNGREILNLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 423 RL----LSWVGQ------NPQLPAATLRENVLlawpeaseaQLQLALDKAWVSEFISQLPQGINTPVGDQAGRL-----S 487
Cdd:PRK09473 93 KLraeqISMIFQdpmtslNPYMRVGEQLMEVL---------MLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMyphefS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 488 VGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQAL------FNASsqqtTLMVTHQL---EGIAdwDAIWVMQD 558
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkreFNTA----IIMITHDLgvvAGIC--DKVLVMYA 237
|
....*...
gi 695777692 559 GQIVEQGT 566
Cdd:PRK09473 238 GRTMEYGN 245
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
369-566 |
1.50e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 62.32 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNP--QLPAATLR----- 440
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSGEIKIDGITISKENLKEIRKKIGIIFQNPdnQFIGATVEddiaf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 441 --ENVLLAWPEASEAQLQLAlDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDA 518
Cdd:PRK13632 108 glENKKVPPKKMKDIIDDLA-KKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695777692 519 HSEQRVMQALFNASSQ--QTTLMVTHQLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:PRK13632 176 KGKREIKKIMVDLRKTrkKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
361-570 |
1.68e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.07 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 361 EGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVEL------RDLDASRWHRLLswVGQNP- 432
Cdd:PRK13649 19 EGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPTQGSVRVDDTLItstsknKDIKQIRKKVGL--VFQFPe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 433 -QLPAATLRENVLLAwPE----ASEAQLQLALDK-AWVsefisqlpqGINTPVGDQAG-RLSVGQAQRIAVARALLVPCR 505
Cdd:PRK13649 96 sQLFEETVLKDVAFG-PQnfgvSQEEAEALAREKlALV---------GISESLFEKNPfELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 506 LLLLDEPAASLDAHSEQRVMQaLFNASSQQ--TTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMT-LFKKLHQSgmTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKPKDI 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
368-566 |
2.21e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 62.51 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 368 PLNFTLPAGKRVVLVGQSGSGKSSLL---NALTGflPYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQ----LPAATLR 440
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTLIrciNLLER--PTSGRVLVDGQDLTALSEKELRKARRQIGMIFQhfnlLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 441 ENVLLAwpeaseaqLQLA-LDKAWVSEFISQLPQgintPVG--DQAGR----LSVGQAQRIAVARALLVPCRLLLLDEPA 513
Cdd:PRK11153 101 DNVALP--------LELAgTPKAEIKARVTELLE----LVGlsDKADRypaqLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 514 ASLDAHSEQRVMQAL--FNASSQQTTLMVTHQLE---GIADWDAiwVMQDGQIVEQGT 566
Cdd:PRK11153 169 SALDPATTRSILELLkdINRELGLTIVLITHEMDvvkRICDRVA--VIDAGRLVEQGT 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
369-570 |
2.26e-10 |
|
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: 61.36 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDAS---RWHRLLSWVGQ------NPQlpaAT 438
Cdd:TIGR02769 30 VSLSIEEGETVGLLGRSGCGKSTLARLLLGLeKPAQGTVSFRGQDLYQLDRKqrrAFRRDVQLVFQdspsavNPR---MT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 439 LREnvLLAWPEASEAQLQLALDKAWVSEFISQLpqGINTPVGDQAGR-LSVGQAQRIAVARALLVPCRLLLLDEPAASLD 517
Cdd:TIGR02769 107 VRQ--IIGEPLRHLTSLDESEQKARIAELLDMV--GLRSEDADKLPRqLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 518 AHSEQRVMQAL--FNASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:TIGR02769 183 MVLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQL 238
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
368-566 |
2.35e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.34 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 368 PLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNP-----------QLP 435
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqrisQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 436 AATLRENVLLAwPEASEAQLQLALDKawvsefISQLPqgintpvgDQAG----RLSVGQAQRIAVARALLVPCRLLLLDE 511
Cdd:PRK15112 111 DFPLRLNTDLE-PEQREKQIIETLRQ------VGLLP--------DHASyyphMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 512 PAASLDAHSEQRVMQALFNASSQQ--TTLMVTHQL---EGIAdwDAIWVMQDGQIVEQGT 566
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLgmmKHIS--DQVLVMHQGEVVERGS 233
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
32-308 |
3.19e-10 |
|
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: 61.29 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 32 VISGLLIVGQAWLLARILHRMIMENIPaTALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVLDRLQQAGP 111
Cdd:cd18542 9 LLATALNLLIPLLIRRIIDSVIGGGLR-ELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 112 AWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFMALVGMGAaean 191
Cdd:cd18542 88 SFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKV---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 192 RRNFL----ALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVAVY 267
Cdd:cd18542 164 RPAFEeireQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 695777692 268 FGFSYL-GELNFGhygvgvTLMsGFLALILApeFFQPLRDLG 308
Cdd:cd18542 244 GGYLVInGEITLG------ELV-AFISYLWM--LIWPVRQLG 276
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
369-566 |
3.40e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.48 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGvelRdldasrwhrlLSW-----VGQNPQLpaaTLREN 442
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILePTSGRVEVNG---R----------VSAllelgAGFHPEL---TGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLLAwpeA-----SEAQLQLALDKawVSEFiSQLPQGINTPVgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLD 517
Cdd:COG1134 109 IYLN---GrllglSRKEIDEKFDE--IVEF-AELGDFIDQPV----KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695777692 518 AHSEQRVMQALFNASSQQTT-LMVTHQLEGIADW--DAIWvMQDGQIVEQGT 566
Cdd:COG1134 179 AAFQKKCLARIRELRESGRTvIFVSHSMGAVRRLcdRAIW-LEKGRLVMDGD 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
361-570 |
6.90e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.98 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 361 EGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTgFL--PYDGSLLVNGVELR-------DLDASRWHRL------L 425
Cdd:PRK10619 17 EHEVLKG-VSLQANAGDVISIIGSSGSGKSTFLRCIN-FLekPSEGSIVVNGQTINlvrdkdgQLKVADKNQLrllrtrL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 426 SWVGQNPQLPA-ATLRENVLlawpeasEAQLQ-LALDKAWVSE----FISQLpqGINTPV-GDQAGRLSVGQAQRIAVAR 498
Cdd:PRK10619 95 TMVFQHFNLWShMTVLENVM-------EAPIQvLGLSKQEAREravkYLAKV--GIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 499 ALLVPCRLLLLDEPAASLDAH---SEQRVMQALfnASSQQTTLMVTHQLEGIADWDA-IWVMQDGQIVEQGTYSQL 570
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPElvgEVLRIMQQL--AEEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQL 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
362-570 |
6.96e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.11 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 362 GKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNAL-------TGFlPYDGSLLVNGVELRDL-DASRWHRLLSWVGQNPQ 433
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGY-RYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 434 LPAATLRENVLlawpeASEAQLQLALDKAWVSEFISQLPQ-----GINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLL 508
Cdd:PRK14271 112 PFPMSIMDNVL-----AGVRAHKLVPRKEFRGVAQARLTEvglwdAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 509 LDEPAASLDAHSEQRVMQALFNASSQQTTLMVTHQLEG---IADWDAIWVmqDGQIVEQGTYSQL 570
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQaarISDRAALFF--DGRLVEEGPTEQL 249
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
369-545 |
7.62e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.71 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRwhrllSWVGQNPQ-LPAATLRENVLLA 446
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEGPGAER-----GVVFQNEGlLPWRNVQDNVAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 447 wpeaseaqLQLA-LDKAWVSEFISQLPQGINTPVGDQ--AGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQR 523
Cdd:PRK11248 95 --------LQLAgVEKMQRLEIAHQMLKKVGLEGAEKryIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*
gi 695777692 524 vMQALFNASSQQT---TLMVTHQLE 545
Cdd:PRK11248 167 -MQTLLLKLWQETgkqVLLITHDIE 190
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
48-311 |
7.67e-10 |
|
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: 60.17 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 48 ILHRMIMENIPA---TALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVLDRLQQAGPAWIQGKPAGSWAT 124
Cdd:cd18545 22 LIKIAIDEYIPNgdlSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 125 LVLEQIDDMHDYYARYLpqMTLAASVPLLIVITI--FPINWAAALILLGTAPLIPLFMALVGMGAAEANRRNFLALARLS 202
Cdd:cd18545 102 RVINDVNSLSDLLSNGL--INLIPDLLTLVGIVIimFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 203 GHFLDRLRGMETLRLFHRgeaETDNIRH---ASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVAVYFGFSYLGelnfG 279
Cdd:cd18545 180 AYLHESISGIRVIQSFAR---EDENEEIfdeLNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLG----G 252
|
250 260 270
....*....|....*....|....*....|..
gi 695777692 280 HYGVGVtlMSGFLALIlaPEFFQPLRDLGTFY 311
Cdd:cd18545 253 AITVGV--LVAFIGYV--GRFWQPIRNLSNFY 280
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
369-566 |
8.64e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 59.76 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNP--QLPAATLR----- 440
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPdnQFVGSIVKydvaf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 441 --ENVLLAWPEASEAqlqlaldkawVSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDA 518
Cdd:PRK13648 108 glENHAVPYDEMHRR----------VSEALKQV--DMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695777692 519 HSEQRVMQAL--FNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:PRK13648 176 DARQNLLDLVrkVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
347-565 |
8.90e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 347 PIGLEARDAIVKSPegKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP-----YDGSLLVNGVELrdLDASRW 421
Cdd:PRK10418 2 PQQIELRNIALQAA--QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrqTAGRVLLDGKPV--APCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 422 HRLLSWVGQNP-------QLPAATLRENVLLAWPEASEAQLQLALDKAWVSEfisqlPQGIntpVGDQAGRLSVGQAQRI 494
Cdd:PRK10418 78 GRKIATIMQNPrsafnplHTMHTHARETCLALGKPADDATLTAALEAVGLEN-----AARV---LKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 495 AVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQT--TLMVTHQLEGIADW-DAIWVMQDGQIVEQG 565
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLaDDVAVMSHGRIVEQG 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
369-566 |
9.91e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.81 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGS---LLVNGVELRDLDASRWHRLLSWVGQNP--QLPAATLREN 442
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLlPDDNPnskITVDGITLTAKTVWDIREKVGIVFQNPdnQFVGATVGDD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLLAWPEASEAQLQL------ALDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:PRK13640 106 VAFGLENRAVPRPEMikivrdVLADVGMLDYIDSEPA-----------NLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695777692 517 DAHSEQRVMQAL--FNASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:PRK13640 175 DPAGKEQILKLIrkLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
59-317 |
1.02e-09 |
|
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: 59.81 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 59 ATALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYA 138
Cdd:cd18546 35 LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 139 RYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLF 218
Cdd:cd18546 115 TGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 219 HRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVAVYFGFSYLGelnfGHYGVGVtLMSGFLALILap 298
Cdd:cd18546 195 RRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAA----GTLTVGV-LVAFLLYLRR-- 267
|
250
....*....|....*....
gi 695777692 299 eFFQPLRDLGTFYHAKAQA 317
Cdd:cd18546 268 -FFAPIQQLSQVFDSYQQA 285
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
369-570 |
1.10e-09 |
|
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: 60.85 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPY-----DGSLLVNGVELRDLDASRWHRL----LSWVGQ------NP- 432
Cdd:COG4172 29 VSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahpSGSILFDGQDLLGLSERELRRIrgnrIAMIFQepmtslNPl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 433 -----QLpAATLRENVLLAWPEASEAQLQLaLDKAwvsefisqlpqGINTPvgdqAGR-------LSVGQAQRIAVARAL 500
Cdd:COG4172 109 htigkQI-AEVLRLHRGLSGAAARARALEL-LERV-----------GIPDP----ERRldayphqLSGGQRQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 501 LVPCRLLLLDEPAASLDAHSEQRVMQALfnASSQQTT----LMVTHQL---EGIADWdaIWVMQDGQIVEQGTYSQL 570
Cdd:COG4172 172 ANEPDLLIADEPTTALDVTVQAQILDLL--KDLQRELgmalLLITHDLgvvRRFADR--VAVMRQGEIVEQGPTAEL 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
370-570 |
1.13e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.11 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP-YDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATL--RENV--L 444
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLnpRMTIgeI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 445 LA------WPEASEAQLqlaldKAWVSEFISQ---LPQGINT-PvgdqaGRLSVGQAQRIAVARALLVPCRLLLLDEPAA 514
Cdd:PRK15079 121 IAeplrtyHPKLSRQEV-----KDRVKAMMLKvglLPNLINRyP-----HEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695777692 515 SLDAHSEQRVMQALfnASSQQ----TTLMVTHQL---EGIAdwDAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK15079 191 ALDVSIQAQVVNLL--QQLQRemglSLIFIAHDLavvKHIS--DRVLVMYLGHAVELGTYDEV 249
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
370-566 |
1.77e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 59.71 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLL---NALTgfLPYDGSLLVNGVELRDLDASRWHRLLSWVG---QNPQL-PAATLREN 442
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIrciNLLE--RPTSGSVLVDGVDLTALSERELRAARRKIGmifQHFNLlSSRTVAEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VllAWPeaseaqLQLA-LDKAW----VSEFIsQLpqgintpVG--DQAGR----LSVGQAQRIAVARALLVPCRLLLLDE 511
Cdd:COG1135 103 V--ALP------LEIAgVPKAEirkrVAELL-EL-------VGlsDKADAypsqLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 512 PAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQLE---GIADWDAiwVMQDGQIVEQGT 566
Cdd:COG1135 167 ATSALDPETTRSILDLLkdINRELGLTIVLITHEMDvvrRICDRVA--VLENGRIVEQGP 224
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
58-317 |
1.78e-09 |
|
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: 59.50 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 58 PATALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYY 137
Cdd:cd18565 49 PRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 138 ARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIpLFMALVGMGAAE---ANRRNflALARLSGHFLDRLRGMET 214
Cdd:cd18565 129 DDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLI-IAGTYWFQRRIEpryRAVRE--AVGDLNARLENNLSGIAV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 215 LRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVAVYFGFSYLgelnFGHYGVGVTLMSGFLA- 293
Cdd:cd18565 206 IKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVL----DGPPLFTGTLTVGTLVt 281
|
250 260
....*....|....*....|....*....
gi 695777692 294 -LILAPEFFQPLRDLG----TFYHAKAQA 317
Cdd:cd18565 282 fLFYTQRLLWPLTRLGdlidQYQRAMASA 310
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
376-564 |
2.27e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.87 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 376 GKRVVLVGQSGSGKSSLLNALTGFlpYDGS---LLVNGVELRDLDASRWHRL----LSWVGQNPQL-PAATLRENVLLAW 447
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGL--DDGSsgeVSLVGQPLHQMDEEARAKLrakhVGFVFQSFMLiPTLNALENVELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASEAQLQlalDKAWVSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQA 527
Cdd:PRK10584 114 LLRGESSRQ---SRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 695777692 528 LF--NASSQQTTLMVTHQLEGIADWDAIWVMQDGQIVEQ 564
Cdd:PRK10584 189 LFslNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
354-573 |
2.29e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.28 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 354 DAIVKSPEGKILAGPLNFTLPaGKRVVLVGQSGSGKSSLLNALTGFLP---YDGSLLVNGVELrdldASRWHRLLSWVGQ 430
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASP-GEILAVLGPSGSGKSTLLNALAGRIQgnnFTGTILANNRKP----TKQILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 431 NPQL-PAATLRENV----LLAWPEASEAQLQLALDKAWVSEFisQLPQGINTPVGDQAGR-LSVGQAQRIAVARALLVPC 504
Cdd:PLN03211 148 DDILyPHLTVRETLvfcsLLRLPKSLTKQEKILVAESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695777692 505 RLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMVT-HQLEG--IADWDAIWVMQDGQIVEQGTYSQlAMA 573
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSrvYQMFDSVLVLSEGRCLFFGKGSD-AMA 296
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
371-583 |
2.29e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.74 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 371 FTLPAGKRVVLVGQSGSGKSSLLNALTGFLPY-DGSLLVNGVELRDldASRwHRLLSWVGQNPQLPAA--TLRENVLLAW 447
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLaSGKISILGQPTRQ--ALQ-KNLVAYVPQSEEVDWSfpVLVEDVVMMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASEAQLQLAL--DKAWVSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVM 525
Cdd:PRK15056 105 RYGHMGWLRRAKkrDRQIVTAALARV--DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695777692 526 QALFNASSQQTTLMV-THQLEGIADWDAIWVMQDGQIVEQG-TYSQLAMAN--GPFAALLAH 583
Cdd:PRK15056 183 SLLRELRDEGKTMLVsTHNLGSVTEFCDYTVMVKGTVLASGpTETTFTAENleLAFSGVLRH 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
350-560 |
2.53e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDaIVKSPEG-KILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP---YDGSLLVNGVEL-----RDLDA-- 418
Cdd:PRK13549 6 LEMKN-ITKTFGGvKALDN-VSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtYEGEIIFEGEELqasniRDTERag 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 419 -SRWHRLLSWVgqnPQLpaaTLRENVLLA----------WP----EASE--AQLQLALDkawvsefisqlpqgINTPVGD 481
Cdd:PRK13549 84 iAIIHQELALV---KEL---SVLENIFLGneitpggimdYDamylRAQKllAQLKLDIN--------------PATPVGN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 482 qagrLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAhSEQRVMQALFNASSQQ--TTLMVTHQLEGIAD-WDAIWVMQD 558
Cdd:PRK13549 144 ----LGLGQQQLVEIAKALNKQARLLILDEPTASLTE-SETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRD 218
|
..
gi 695777692 559 GQ 560
Cdd:PRK13549 219 GR 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
371-565 |
3.04e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 58.59 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 371 FTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRL---LSWVGQNPQ--L-PAATLREnv 443
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEePTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDPYasLnPRMTVGD-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAWP-----EASEAQLQlaldkAWVSEFISQlpqgintpVG---DQAGR----LSVGQAQRIAVARALLVPCRLLLLDE 511
Cdd:COG4608 117 IIAEPlrihgLASKAERR-----ERVAELLEL--------VGlrpEHADRypheFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 512 PAASLDahseqrV-MQA----LFnASSQQ----TTLMVTHQL---EGIAdwDAIWVMQDGQIVEQG 565
Cdd:COG4608 184 PVSALD------VsIQAqvlnLL-EDLQDelglTYLFISHDLsvvRHIS--DRVAVMYLGKIVEIA 240
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
369-571 |
4.61e-09 |
|
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: 57.30 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP-YDGSLLVNGVELRDLDASRWHRL-LSWVGQN----PQLpaaTLREN 442
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPpRSGSIRFDGEDITGLPPHRIARLgIGYVPEGrrifPSL---TVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLL-AWPEASEAQLQLALDKAW-----VSEFISQLpqgintpvgdqAGRLSVGQAQRIAVARALLVPCRLLLLDEPaasl 516
Cdd:COG0410 99 LLLgAYARRDRAEVRADLERVYelfprLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEP---- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 517 dahSE-------QRVMQALFNASSQQTT-LMV---THQLEGIADWdaIWVMQDGQIVEQGTYSQLA 571
Cdd:COG0410 164 ---SLglaplivEEIFEIIRRLNREGVTiLLVeqnARFALEIADR--AYVLERGRIVLEGTAAELL 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
369-565 |
6.33e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVNGVELRDLDASR---WHRLLSWVGQNPQlPAATLRENVLL 445
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPN-SSLNPRLNVLQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 446 AWPEASEAQlQLALDKAWVSEFISQLPQgintPVG-DQAGR------LSVGQAQRIAVARALLVPCRLLLLDEPAASLDa 518
Cdd:PRK15134 384 IIEEGLRVH-QPTLSAAQREQQVIAVME----EVGlDPETRhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLD- 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695777692 519 HSEQRVMQALFNASSQQTTL---MVTHQLEGI-ADWDAIWVMQDGQIVEQG 565
Cdd:PRK15134 458 KTVQAQILALLKSLQQKHQLaylFISHDLHVVrALCHQVIVLRQGEVVEQG 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
371-571 |
6.57e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 371 FTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELR------DLDASrwhrlLSWVGQNPQL-PAATLREN 442
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGNyQPDAGSILIDGQEMRfasttaALAAG-----VAIIYQELHLvPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLLAWPEASEAQLQLALDKAWVSEFISQLPQGI--NTPVGdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDA-H 519
Cdd:PRK11288 100 LYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIdpDTPLK----YLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 520 SEQ--RVMQALfnASSQQTTLMVTHQLEGI-ADWDAIWVMQDGQIVEqgTYSQLA 571
Cdd:PRK11288 176 IEQlfRVIREL--RAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDMA 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
369-548 |
1.49e-08 |
|
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: 55.80 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGveLRDLDASRWH-RLLSWV-GQNPQL-----PAATLR 440
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTSGEVRVAG--LVPWKRRKKFlRRIGVVfGQKTQLwwdlpVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 441 enVLLAWPEASEAQLQLALDKawVSEFIsQLPQGINTPVGdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHS 520
Cdd:cd03267 118 --LLAAIYDLPPARFKKRLDE--LSELL-DLEELLDTPVR----QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190
....*....|....*....|....*....|
gi 695777692 521 EQRVMQAL--FNASSQQTTLMVTHQLEGIA 548
Cdd:cd03267 189 QENIRNFLkeYNRERGTTVLLTSHYMKDIE 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
369-565 |
1.71e-08 |
|
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: 55.07 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVE-LRDLDASRwhRLLSWVGQNPQL-PAATLRENVLL 445
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATVDGFDvVKEPAEAR--RRLGFVSDSTGLyDRLTARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 446 AwpeASEAQLQLALDKAWVSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVM 525
Cdd:cd03266 102 F---AGLYGLKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695777692 526 QALFNASSQQTTLMV-THQLEGIADW-DAIWVMQDGQIVEQG 565
Cdd:cd03266 177 EFIRQLRALGKCILFsTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
370-565 |
2.76e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.32 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLL--VNGVELRDL----DASRwhRLLS---W--VGQNPqlpAA 437
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDaGEVHyrMRDGQLRDLyalsEAER--RRLLrteWgfVHQHP---RD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 438 TLRENV---------LLAWPEASEAQL-QLALDkaWVSEFisQLPQGintPVGDQAGRLSVGQAQRIAVARALLVPCRLL 507
Cdd:PRK11701 101 GLRMQVsaggnigerLMAVGARHYGDIrATAGD--WLERV--EIDAA---RIDDLPTTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695777692 508 LLDEPAASLDAHSEQRVMQALFNASSQQ--TTLMVTHQLeGIADW--DAIWVMQDGQIVEQG 565
Cdd:PRK11701 174 FMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDL-AVARLlaHRLLVMKQGRVVESG 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
363-573 |
2.85e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.38 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 363 KILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPA-ATLR 440
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 441 ENV----------LLAWPEASEAQLQLALDKAWVSEFISQlpqGINTpvgdqagrLSVGQAQRIAVARALLVPCRLLLLD 510
Cdd:PRK10253 100 ELVargryphqplFTRWRKEDEEAVTKAMQATGITHLADQ---SVDT--------LSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 511 EPAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQLEGIADWDA-IWVMQDGQIVEQGTYSQLAMA 573
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYAShLIALREGKIVAQGAPKEIVTA 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
363-543 |
3.27e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 363 KILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELrDLDASRWHRLLSWVGQNPQL-PAATLR 440
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPEKGEILFERQSI-KKDLCTYQKQLCFVGHRSGInPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 441 ENVLLAWPEASEAqlqLALDKAWVsefISQLPQGINTPvgdqAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHS 520
Cdd:PRK13540 93 ENCLYDIHFSPGA---VGITELCR---LFSLEHLIDYP----CGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....
gi 695777692 521 EQRVMQALFNASSQ-QTTLMVTHQ 543
Cdd:PRK13540 163 LLTIITKIQEHRAKgGAVLLTSHQ 186
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
373-545 |
4.82e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.40 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 373 LPAGKRVVLVGQSGSGKSSLL---NALTGFLP---YDGSLLVNGVEL--RDLDASRWHRLLSWVGQNPQLPAATLRENVL 444
Cdd:PRK14243 33 IPKNQITAFIGPSGCGKSTILrcfNRLNDLIPgfrVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 445 LA---------WPEASEAQL-QLALdkaWvSEFISQLPQgintpvgdQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAA 514
Cdd:PRK14243 113 YGaringykgdMDELVERSLrQAAL---W-DEVKDKLKQ--------SGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190
....*....|....*....|....*....|.
gi 695777692 515 SLDAHSEQRVMQALFNASSQQTTLMVTHQLE 545
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
327-570 |
5.08e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.42 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 327 FMEKPLAQEtrgekLLSDNEPIGLEARDAIVKSPEGKILagplnftlpagkrvVLVGQSGSGKSSLLNALTGFL-PYDGS 405
Cdd:PRK10070 24 YIEQGLSKE-----QILEKTGLSLGVKDASLAIEEGEIF--------------VIMGLSGSGKSTMVRLLNRLIePTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 406 LLVNGVELRDLDASRWHRL----LSWVGQNPQL-PAATLRENVL----LAWPEASEAQlQLALDKawvsefISQLpqGIN 476
Cdd:PRK10070 85 VLIDGVDIAKISDAELREVrrkkIAMVFQSFALmPHMTVLDNTAfgmeLAGINAEERR-EKALDA------LRQV--GLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 477 TPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQL-EGIADWDAI 553
Cdd:PRK10070 156 NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRI 235
|
250
....*....|....*..
gi 695777692 554 WVMQDGQIVEQGTYSQL 570
Cdd:PRK10070 236 AIMQNGEVVQVGTPDEI 252
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-545 |
5.93e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.84 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 321 ADSLKTFMEKPLAQETRGEKLLSDNEPIGLEARDAI-----VKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNA 395
Cdd:PRK13536 7 AEEAPRRLELSPIERKHQGISEAKASIPGSMSTVAIdlagvSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 396 LTGFLPYD-GSLLVNGVELRDldASRWHRllSWVGQNPQL----PAATLRENVLL--AWPEASEAQLQLALDKawVSEFi 468
Cdd:PRK13536 87 ILGMTSPDaGKITVLGVPVPA--RARLAR--ARIGVVPQFdnldLEFTVRENLLVfgRYFGMSTREIEAVIPS--LLEF- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 469 SQLPQGINTPVGDqagrLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQ-QTTLMVTHQLE 545
Cdd:PRK13536 160 ARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTHFME 233
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
278-543 |
6.16e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.53 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 278 FGHYGVGVTLMSGFLALILapEFFQPLRDLGTFyHAKAQAIGAADSLKTFMEKPLAQETRGEKLLSDNEpIGLEARDAIv 357
Cdd:TIGR00954 386 LMLAGRDMTRLAGFTARVD--TLLQVLDDVKSG-NFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNG-IKFENIPLV- 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 358 kSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVNGVELRdldasrwhrlLSWVGQNPQLPAA 437
Cdd:TIGR00954 461 -TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGK----------LFYVPQRPYMTLG 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 438 TLRENVLlaWPEASEAQLQLALDKAWVSEFIS--QLPQGINTPVGDQAGR-----LSVGQAQRIAVARALLVPCRLLLLD 510
Cdd:TIGR00954 530 TLRDQII--YPDSSEDMKRRGLSDKDLEQILDnvQLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILD 607
|
250 260 270
....*....|....*....|....*....|....*....
gi 695777692 511 EPAASLDAHSEQRVMQALFNAS------SQQTTLMVTHQ 543
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLCREFGitlfsvSHRKSLWKYHE 646
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
350-565 |
7.69e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.91 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPY---DGSLLVNGVELRDLDASRWHRL-- 424
Cdd:cd03217 1 LEIKDLHVSVGGKEILKG-VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevtEGEILFKGEDITDLPPEERARLgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 425 -LSWvgQNP-QLPAATlrenvllawpeaseaqlqlaldkawVSEFISQLPQGintpvgdqagrLSVGQAQRIAVARALLV 502
Cdd:cd03217 80 fLAF--QYPpEIPGVK-------------------------NADFLRYVNEG-----------FSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 503 PCRLLLLDEPAASLDAHSEQRVMQALFN-ASSQQTTLMVTHQLEgIADW---DAIWVMQDGQIVEQG 565
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVKSG 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
370-569 |
8.83e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.07 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGvELRdldasrwhrlLSWVGQNPQL-PAATLRENVLLAW 447
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELePDSGEVSIPK-GLR----------IGYLPQEPPLdDDLTVLDTVLDGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASE----------------------AQLQLALDK--AW-----VSEFISQLpqGINTPVGDQA-GRLSVGQAQRIAVA 497
Cdd:COG0488 87 AELRAleaeleeleaklaepdedlerlAELQEEFEAlgGWeaearAEEILSGL--GFPEEDLDRPvSELSGGWRRRVALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 498 RALLVPCRLLLLDEPAASLDAHS----EQrvmqalFNASSQQTTLMVTHQ---LEGIADWdaIWVMQDGQIVE-QGTYSQ 569
Cdd:COG0488 165 RALLSEPDLLLLDEPTNHLDLESiewlEE------FLKNYPGTVLVVSHDryfLDRVATR--ILELDRGKLTLyPGNYSA 236
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
350-563 |
9.34e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.98 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTG-FLPYDGSLLVNGVELRDLDASRWHRLLSWV 428
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 429 GQNPQLPAATLRenvllawPEASEAqlqlalDKAWVSEFISQLpqGINTPVGDQAGR-----LSVGQAQRIAVARALLVP 503
Cdd:PRK10522 403 FTDFHLFDQLLG-------PEGKPA------NPALVEKWLERL--KMAHKLELEDGRisnlkLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695777692 504 CRLLLLDEPAASLDAHSEQRVMQALFNASSQQ--TTLMVTHQLEGIADWDAIWVMQDGQIVE 563
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQVLLPLLQEMgkTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
372-563 |
9.38e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 372 TLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASRW---HRLLSWVGQNPqLPAATLRENVllAW 447
Cdd:PRK10419 34 SLKSGETVALLGRSGCGKSTLARLLVGLeSPSQGNVSWRGEPLAKLNRAQRkafRRDIQMVFQDS-ISAVNPRKTV--RE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PEASEAQLQLALDKAWVSEFISQLPQGINTPVGDQA---GRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRV 524
Cdd:PRK10419 111 IIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDkrpPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695777692 525 MQALFNASSQQTT--LMVTHQLEGIADWDA-IWVMQDGQIVE 563
Cdd:PRK10419 191 IRLLKKLQQQFGTacLFITHDLRLVERFCQrVMVMDNGQIVE 232
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
32-269 |
1.04e-07 |
|
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: 53.57 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 32 VISGLLIVGQAWLLARILHRMIMENIPATAL---VLPFIVL-VLIFVLR-AWVVWLrervgFYAGQHIRYEIRRQVLDRL 106
Cdd:cd18541 9 ILVDLLQLLIPRIIGRAIDALTAGTLTASQLlryALLILLLaLLIGIFRfLWRYLI-----FGASRRIEYDLRNDLFAHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 107 QQAGPAWIQGKPAG---SWATLVLEQIddmhdyyarylpQMTL---------AASVPLLIVITIFPINWAAALILLGTAP 174
Cdd:cd18541 84 LTLSPSFYQKNRTGdlmARATNDLNAV------------RMALgpgilylvdALFLGVLVLVMMFTISPKLTLIALLPLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 175 LIPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLE 254
Cdd:cd18541 152 LLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIG 231
|
250
....*....|....*
gi 695777692 255 FFTSLSIALVaVYFG 269
Cdd:cd18541 232 LLIGLSFLIV-LWYG 245
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
357-570 |
1.12e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 53.76 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 357 VKSPEGKILA-GPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-----GSLLVNGVELRDLDASRWHRLL----S 426
Cdd:COG4170 13 IDTPQGRVKAvDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtaDRFRWNGIDLLKLSPRERRKIIgreiA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 427 WVGQNPQL---PAATLRENVLLAWPEASeaqlqlaLDKAWVSEFISQLPQGINT--PVGDQAGR---------LSVGQAQ 492
Cdd:COG4170 93 MIFQEPSScldPSAKIGDQLIEAIPSWT-------FKGKWWQRFKWRKKRAIELlhRVGIKDHKdimnsypheLTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 493 RIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQ 569
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLarLNQLQGTSILLISHDLESISQWaDTITVLYCGQTVESGPTEQ 245
|
.
gi 695777692 570 L 570
Cdd:COG4170 246 I 246
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
369-565 |
1.27e-07 |
|
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: 52.28 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTG-FLPYDGSLLVNGvelRDLDASRWHRLlswvGQNPQ----LPAATLRENV 443
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPDSGEVLFDG---KPLDIAARNRI----GYLPEerglYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAwpeASEAQLQLALDKAWVSEFISQLPqgintpVGDQAGR----LSVGQAQRIAVARALLVPCRLLLLDEPAASLDAH 519
Cdd:cd03269 92 VYL---AQLKGLKKEEARRRIDEWLERLE------LSEYANKrveeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695777692 520 SEQRVMQALFNASSQQTT-LMVTHQLEGIADW-DAIWVMQDGQIVEQG 565
Cdd:cd03269 163 NVELLKDVIRELARAGKTvILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
370-566 |
1.36e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.47 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVEL-----RDLDASRWHRLLSWVGQNP--QLPAATLRE 441
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISEtGQTIVGDYAIpanlkKIKEVKRLRKEIGLVFQFPeyQLFQETIEK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 442 NVLLAwpeaseaQLQLALDKAWVSEFISQLPQGINTPvGDQAGR----LSVGQAQRIAVARALLVPCRLLLLDEPAASLD 517
Cdd:PRK13645 111 DIAFG-------PVNLGENKQEAYKKVPELLKLVQLP-EDYVKRspfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695777692 518 AHSEQRVMQAL--FNASSQQTTLMVTHQLEGIAD-WDAIWVMQDGQIVEQGT 566
Cdd:PRK13645 183 PKGEEDFINLFerLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
369-566 |
1.40e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.93 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVelrdlDASRWH---RLLSWVGQNPQL-PAATLRENV 443
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTsGHIRFHGT-----DVSRLHardRKVGFVFQHYALfRHMTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 ---LLAWPEASEaqlqlaLDKAWVSEFISQLPQGINtpVGDQAGR----LSVGQAQRIAVARALLVPCRLLLLDEPAASL 516
Cdd:PRK10851 96 afgLTVLPRRER------PNAAAIKAKVTQLLEMVQ--LAHLADRypaqLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695777692 517 DAHSEQRVMQALFNASSQQ--TTLMVTH-QLEGIADWDAIWVMQDGQIVEQGT 566
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
43-268 |
1.81e-07 |
|
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: 53.19 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 43 WLLARILHRMIMENIPATA-----LVLPFIVLVLIF-VLRAWVVWLRERVGFYAGQHIRYEIRRQVLDRLQQAGPAWIQG 116
Cdd:cd18554 20 LILKYIVDDVIQGSSLTLDekvykLFTIIGIMFFIFlILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYAN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 117 KPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVpLLIVITI-FPINWAAALILLGTAPLIPLFMALVGMGAAEANRRNF 195
Cdd:cd18554 100 NRSGEIISRVINDVEQTKDFITTGLMNIWLDMIT-IIIAICImLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERS 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 196 LALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLR---LAFLSSGVLEFFTSLSIALVAVYF 268
Cdd:cd18554 179 QALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRwnaKTFSAVNTITDLAPLLVIGFAAYL 254
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-566 |
2.13e-07 |
|
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: 53.65 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 354 DAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTG---FLPYDGSLLVN--------------------- 409
Cdd:TIGR03269 4 KNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqYEPTSGRIIYHvalcekcgyverpskvgepcp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 410 --GVELRDLDASRW-------HRLLSWVGQNPQLPAA-----TLRENVLLAWPEAsEAQLQLALDKAwvSEFISQLpqGI 475
Cdd:TIGR03269 84 vcGGTLEPEEVDFWnlsdklrRRIRKRIAIMLQRTFAlygddTVLDNVLEALEEI-GYEGKEAVGRA--VDLIEMV--QL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 476 NTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTTLMV--THQLEGIADWD-- 551
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVltSHWPEVIEDLSdk 238
|
250
....*....|....*
gi 695777692 552 AIWvMQDGQIVEQGT 566
Cdd:TIGR03269 239 AIW-LENGEIKEEGT 252
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
369-548 |
3.45e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.41 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASRWHRLLSWVGQNPQ----LPAATLRENV 443
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQdhhlLMDRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LL------AWPEASEAQLQLALDKawvsefISQLPQGINTPVgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASLD 517
Cdd:PRK10908 101 AIpliiagASGDDIRRRVSAALDK------VGLLDKAKNFPI-----QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190
....*....|....*....|....*....|...
gi 695777692 518 AHSEQRVMQaLFNASSQ--QTTLMVTHQLEGIA 548
Cdd:PRK10908 170 DALSEGILR-LFEEFNRvgVTVLMATHDIGLIS 201
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
350-563 |
3.73e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDaIVKS-PEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP---YDGSLLVNG--VELRDLDASR--- 420
Cdd:NF040905 2 LEMRG-ITKTfPGVKALDD-VNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgsYEGEILFDGevCRFKDIRDSEalg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 421 ---WHRLLSWVgqnPQLPAAtlrENVLLA----------WPEASEAQLQLaLDKAWVSEfisqLPQginTPVGDqagrLS 487
Cdd:NF040905 80 iviIHQELALI---PYLSIA---ENIFLGnerakrgvidWNETNRRAREL-LAKVGLDE----SPD---TLVTD----IG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 488 VGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQ-TTLMVTHQL---EGIAdwDAIWVMQDGQIVE 563
Cdd:NF040905 142 VGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIIISHKLneiRRVA--DSITVLRDGRTIE 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
356-585 |
5.74e-07 |
|
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: 52.13 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 356 IVKSPEG-KILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP---YDGSLLVNGVEL-----RDLDA---SRWHR 423
Cdd:TIGR02633 7 IVKTFGGvKALDG-IDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtWDGEIYWSGSPLkasniRDTERagiVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 424 LLSWV-----------GQNPQLPAATLRENVLLAWPEASEAQLQLALDkawvsefisqlpqgintPVGDQAGRLSVGQAQ 492
Cdd:TIGR02633 86 ELTLVpelsvaeniflGNEITLPGGRMAYNAMYLRAKNLLRELQLDAD-----------------NVTRPVGDYGGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 493 RIAVARALLVPCRLLLLDEPAASLDAhSEQRVMQALFNASSQQ--TTLMVTHQLEGI-ADWDAIWVMQDGQIVeqGTYSQ 569
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTE-KETEILLDIIRDLKAHgvACVYISHKLNEVkAVCDTICVIRDGQHV--ATKDM 225
|
250
....*....|....*.
gi 695777692 570 LAMANGPFAALLAHRQ 585
Cdd:TIGR02633 226 STMSEDDIITMMVGRE 241
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
58-317 |
7.80e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 50.97 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 58 PATALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYY 137
Cdd:cd18564 49 PLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 138 ARYLpqMTLAASVPLLIVITI--FPINWAAALILLGTAPLipLFMALVGMG-----AAEANRRNFLALARLSGhfldrlR 210
Cdd:cd18564 129 VSGV--LPLLTNLLTLVGMLGvmFWLDWQLALIALAVAPL--LLLAARRFSrrikeASREQRRREGALASVAQ------E 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 211 GMETLRL---FHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVaVYFGfSYL---GELNFGhygvG 284
Cdd:cd18564 199 SLSAIRVvqaFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALV-LWFG-AWLvlaGRLTPG----D 272
|
250 260 270
....*....|....*....|....*....|....*..
gi 695777692 285 VTLMSGFLALilapeFFQPLRDL----GTFYHAKAQA 317
Cdd:cd18564 273 LLVFLAYLKN-----LYKPVRDLakltGRIAKASASA 304
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
347-561 |
8.48e-07 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 49.35 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 347 PIGLEARDAIVKSPEGkilagPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWHRL- 424
Cdd:cd03215 2 EPVLEVRGLSVKGAVR-----DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAsGEITLDGKPVTRRSPRDAIRAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 425 LSWVGQNPQ----LPAATLRENVLLAWpeaseaqlqlaldkawvsefisqlpqgintpvgdqagRLSVGQAQRIAVARAL 500
Cdd:cd03215 77 IAYVPEDRKreglVLDLSVAENIALSS-------------------------------------LLSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 501 LVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTT-LMVTHQLE---GIAdwDAIWVMQDGQI 561
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAvLLISSELDellGLC--DRILVMYEGRI 182
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
369-566 |
1.00e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.60 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP---------YDGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAA-T 438
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAFAfS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 439 LRENVLLA-WPEASEAQLQLALDKAWVSEFISQlpQGINTPVGDQAGRLSVGQAQRIAVARA---------LLVPCRLLL 508
Cdd:PRK13547 100 AREIVLLGrYPHARRAGALTHRDGEIAWQALAL--AGATALVGRDVTTLSGGELARVQFARVlaqlwpphdAAQPPRYLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 509 LDEPAASLDAHSEQRVMQALFNASS--QQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGT 566
Cdd:PRK13547 178 LDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARHaDRIAMLADGAIVAHGA 238
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
370-566 |
1.03e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.37 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRWHRL-LSWVGQNPQL-PAATLRENVLLA 446
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTGGTILLRGQHIEGLPGHQIARMgVVRTFQHVRLfREMTVIENLLVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 447 WPEASEAQL--------------QLALDKA--WVsEFIsqlpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLD 510
Cdd:PRK11300 105 QHQQLKTGLfsgllktpafrraeSEALDRAatWL-ERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695777692 511 EPAASLDAHsEQRVMQALFNASSQQ---TTLMVTHQLE---GIAdwDAIWVMQDGQIVEQGT 566
Cdd:PRK11300 179 EPAAGLNPK-ETKELDELIAELRNEhnvTVLLIEHDMKlvmGIS--DRIYVVNQGTPLANGT 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
361-406 |
1.09e-06 |
|
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: 48.21 E-value: 1.09e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 695777692 361 EGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTG-FLPYDGSL 406
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEGIV 57
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
369-565 |
1.19e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.80 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPY-DGSLLVNGVELRDLDASRwhRLLSWVGQNPQL-PAATLRENVL-- 444
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDItSGDLFIGEKRMNDVPPAE--RGVGMVFQSYALyPHLSVAENMSfg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 445 --LAWPEASEAQ---------LQLA--LDKawvsefisqlpqgintpvgdQAGRLSVGQAQRIAVARALLVPCRLLLLDE 511
Cdd:PRK11000 100 lkLAGAKKEEINqrvnqvaevLQLAhlLDR--------------------KPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 512 PAASLDA--HSEQRVMQALFNASSQQTTLMVTH-QLEGIADWDAIWVMQDGQIVEQG 565
Cdd:PRK11000 160 PLSNLDAalRVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
375-398 |
1.77e-06 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 48.93 E-value: 1.77e-06
10 20
....*....|....*....|....
gi 695777692 375 AGKRVVLVGQSGSGKSSLLNALTG 398
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
369-565 |
2.11e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.26 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVELRDLDASRW----HRLLSWVGQNPQL-PAATLREN 442
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTrPQKGRIVLNGRVLFDAEKGIClppeKRRIGYVFQDARLfPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 vllawpeaseaqLQLALDKAWVSEF--ISQLpQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHS 520
Cdd:PRK11144 97 ------------LRYGMAKSMVAQFdkIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695777692 521 EQRVMQALFNASSQQTT--LMVTHQLEGI---AdwDAIWVMQDGQIVEQG 565
Cdd:PRK11144 164 KRELLPYLERLAREINIpiLYVSHSLDEIlrlA--DRVVVLEQGKVKAFG 211
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
24-307 |
2.13e-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: 49.71 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 24 LMISRALGVISGLLIVGQAWLLARILHRMIMENIPA-----TALVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEI 98
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGggvdfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 99 RRQVLDRLQQAGPAWIQGKPAG---SWATLVLEQIDDMhdyYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPL 175
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGdimSRVTNDVDNISQA---LSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 176 IPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEF 255
Cdd:cd18547 158 SLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNF 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 695777692 256 FTSLSIALVAVYFGFSYLgelnFGHYGVGVtlMSGFlaLILAPEFFQPLRDL 307
Cdd:cd18547 238 INNLGYVLVAVVGGLLVI----NGALTVGV--IQAF--LQYSRQFSQPINQI 281
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
381-565 |
2.13e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.62 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 381 LVGQSGSGKSSLLNALTGFL-PYDGSLLVNGVEL----RDLDASRwhRLLSWVGQNP--QLPAATLRENVLLAWPE--AS 451
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPLdyskRGLLALR--QQVATVFQDPeqQIFYTDIDSDIAFSLRNlgVP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 452 EAQLQLALDKAWvsefisqlpqginTPVGDQAGR------LSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVM 525
Cdd:PRK13638 110 EAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695777692 526 QALFNASSQQTTLMV-THQLEGIADW-DAIWVMQDGQIVEQG 565
Cdd:PRK13638 177 AIIRRIVAQGNHVIIsSHDIDLIYEIsDAVYVLRQGQILTHG 218
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
375-398 |
3.26e-06 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 49.34 E-value: 3.26e-06
10 20
....*....|....*....|....
gi 695777692 375 AGKRVVLVGQSGSGKSSLLNALTG 398
Cdd:COG1162 165 KGKTSVLVGQSGVGKSTLINALLP 188
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
369-570 |
3.33e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDG-----SLLVNGVELRDLDASRWHRLL-SWVGQNPQLPAATLREN 442
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaeKLEFNGQDLQRISEKERRNLVgAEVAMIFQDPMTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLLAWPEASEAQLQLALDKAWVSEFISQLPQGINTPvgDQAGRLSV-------GQAQRIAVARALLVPCRLLLLDEPAAS 515
Cdd:PRK11022 106 YTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIP--DPASRLDVyphqlsgGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 516 LDAHSEQRVMQALFNASSQQTT--LMVTHQLEGIAD-WDAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK11022 184 LDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
369-576 |
3.51e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.99 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWH---RLLSWVGQNPQL-PAATLRENV 443
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDhGEILFDGENIPAMSRSRLYtvrKRMSMLFQSGALfTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 llAWPEASEAQLQLALDKAWVSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQR 523
Cdd:PRK11831 106 --AYPLREHTQLPAPLLHSTVMMKLEAV--GLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695777692 524 VMQAL--FNASSQQTTLMVTH---QLEGIADWdaIWVMQDGQIVEQGTYSQLAMANGP 576
Cdd:PRK11831 182 LVKLIseLNSALGVTCVVVSHdvpEVLSIADH--AYIVADKKIVAHGSAQALQANPDP 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
350-568 |
3.94e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.68 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDaIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVNGVELRdldasrwhrlLSWVG 429
Cdd:COG0488 316 LELEG-LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK----------IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 430 QNP-QL-PAATLRENVLLAWPEASEAQlqlaldkawVSEFISQL---PQGINTPVGDqagrLSVGQAQRIAVARALLVPC 504
Cdd:COG0488 385 QHQeELdPDKTVLDELRDGAPGGTEQE---------VRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 505 RLLLLDEPAASLDAHSEQRVMQAL--FNAssqqTTLMVTHQ---LEGIAdwDAIWVMQDGQIVE-QGTYS 568
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALddFPG----TVLLVSHDryfLDRVA--TRILEFEDGGVREyPGGYD 515
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
370-562 |
7.10e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.87 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNG--VELRD-LDAsrwHRL-LSWVGQNPQL-PAATLRENV 443
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDsGEILIDGkpVRIRSpRDA---IALgIGMVHQHFMLvPNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAWPEASEAQLQLALDKAWVSEFISQLPQGIN--TPVGDqagrLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSE 521
Cdd:COG3845 102 VLGLEPTKGGRLDRKAARARIRELSERYGLDVDpdAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695777692 522 QRVMQALFNASSQQTT-LMVTHQLE---GIAdwDAIWVMQDGQIV 562
Cdd:COG3845 178 DELFEILRRLAAEGKSiIFITHKLRevmAIA--DRVTVLRRGKVV 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
354-561 |
8.88e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 354 DAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFL-PYDGSLLvngvelrdldasRWHRLLSWVGQNP 432
Cdd:PLN03073 513 DASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELqPSSGTVF------------RSAKVRMAVFSQH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 433 QLPAATLRENVLL----AWPEASEAQLQLALDKAWVSEFISQLPQGIntpvgdqagrLSVGQAQRIAVARALLVPCRLLL 508
Cdd:PLN03073 581 HVDGLDLSSNPLLymmrCFPGVPEQKLRAHLGSFGVTGNLALQPMYT----------LSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695777692 509 LDEPAASLDAHSEQRVMQALfnASSQQTTLMVTHQLEGIA-DWDAIWVMQDGQI 561
Cdd:PLN03073 651 LDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
355-566 |
1.12e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.92 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 355 AIVKSPEGKILA-GPLNFTLPAGKRVVLVGQSGSGKSSL------LNALTGFLPYDGSLLVNGVELRDLDasrwhrlLSW 427
Cdd:PRK11650 8 AVRKSYDGKTQViKGIDLDVADGEFIVLVGPSGCGKSTLlrmvagLERITSGEIWIGGRVVNELEPADRD-------IAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 428 VGQNPQL-PAATLRENvlLAWpeaseaqlqlALDKAWVSEfisqlpQGINTPVGDQAG-------------RLSVGQAQR 493
Cdd:PRK11650 81 VFQNYALyPHMSVREN--MAY----------GLKIRGMPK------AEIEERVAEAARileleplldrkprELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 494 IAVARALLVPCRLLLLDEPAASLDA------HSEQRVMQALFNAssqqTTLMVTH-QLEGIADWDAIWVMQDGQIvEQ-G 565
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAklrvqmRLEIQRLHRRLKT----TSLYVTHdQVEAMTLADRVVVMNGGVA-EQiG 217
|
.
gi 695777692 566 T 566
Cdd:PRK11650 218 T 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
486-571 |
1.14e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 486 LSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQ-QTTLMVTHQLEGIADW-DAIWVMQDGQIVE 563
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWtKRTIFFKDGKIIK 245
|
....*....
gi 695777692 564 QG-TYSQLA 571
Cdd:PRK13651 246 DGdTYDILS 254
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
144-269 |
1.24e-05 |
|
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: 47.39 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 144 MTLAASVPLLIV---ITIFPINWAAALILLGTAPLIPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHR 220
Cdd:cd18548 117 LRMLVRAPIMLIgaiIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNR 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 695777692 221 GEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVaVYFG 269
Cdd:cd18548 197 EDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI-LWFG 244
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
357-559 |
1.39e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 357 VKSPEGKILAGPLNFTLPaGKRVVLVGQSGSGKSSLLNAL----TGFLPYDGSLLVNGvelRDLDASrWHRLLSWVGQNP 432
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKP-GTLTALMGASGAGKTTLLNVLaervTTGVITGGDRLVNG---RPLDSS-FQRSIGYVQQQD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 433 -QLPAATLRENVLLAWPEASEAQLQLALDKAWVSEFIS--QLPQGINTPVGDQAGRLSVGQAQR--IAVARAlLVPCRLL 507
Cdd:TIGR00956 846 lHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKllEMESYADAVVGVPGEGLNVEQRKRltIGVELV-AKPKLLL 924
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 508 LLDEPAASLDAHSEQRVMQALFN-ASSQQTTLMVTHQLEGI--ADWDAIWVMQDG 559
Cdd:TIGR00956 925 FLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
363-545 |
2.15e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 46.72 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 363 KILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELrdldASRWHRLLSWVGQNPQL----PAA 437
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDAGSISLCGEPV----PSRARHARQRVGVVPQFdnldPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 438 TLRENVLL--AWPEASEAQLQLALDKawVSEFiSQLPQGINTPVGDqagrLSVGQAQRIAVARALLVPCRLLLLDEPAAS 515
Cdd:PRK13537 96 TVRENLLVfgRYFGLSAAAARALVPP--LLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190
....*....|....*....|....*....|.
gi 695777692 516 LDAHSEQRVMQALFN-ASSQQTTLMVTHQLE 545
Cdd:PRK13537 169 LDPQARHLMWERLRSlLARGKTILLTTHFME 199
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
345-571 |
2.16e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.17 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 345 NEPIgLEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD---GSLLVNGVELRDLDAS-R 420
Cdd:CHL00131 4 NKPI-LEIKNLHASVNENEILKG-LNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKileGDILFKGESILDLEPEeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 421 WHRLLSWVGQNP-QLPAATLRENVLLAWPEASEAQLQLALDKAWVSEFISQL-------PQGINTPVGDQagrLSVGQAQ 492
Cdd:CHL00131 82 AHLGIFLAFQYPiEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKlklvgmdPSFLSRNVNEG---FSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 493 RIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFN-ASSQQTTLMVTHQ---LEGIADwDAIWVMQDGQIVEQGTyS 568
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHYqrlLDYIKP-DYVHVMQNGKIIKTGD-A 236
|
...
gi 695777692 569 QLA 571
Cdd:CHL00131 237 ELA 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
350-498 |
2.35e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.33 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDAIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWHRL-LSW 427
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAsGSIRLDGEDITGLSPRERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 428 VGQNPQ----LPAATLRENVLLAWPEASEAQLQLALDKAWVSEFISQL-------PQGINTPvgdqAGRLSVGQAQRIAV 496
Cdd:COG3845 338 IPEDRLgrglVPDMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELieefdvrTPGPDTP----ARSLSGGNQQKVIL 413
|
..
gi 695777692 497 AR 498
Cdd:COG3845 414 AR 415
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
375-398 |
2.52e-05 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 44.84 E-value: 2.52e-05
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
369-570 |
2.58e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPY------DGSLLVNGVELRDLDASRWHRL----LSWVGQNPQL---P 435
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvypSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPMVslnP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 436 AATLrenvllawpeasEAQLQLALD-------KAWVSEFISQLPQ-GINTP---VGDQAGRLSVGQAQRIAVARALLVPC 504
Cdd:PRK15134 108 LHTL------------EKQLYEVLSlhrgmrrEAARGEILNCLDRvGIRQAakrLTDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 505 RLLLLDEPAASLDAHSEQRVMQaLFNASSQQ---TTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQ-LLRELQQElnmGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATL 244
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
24-322 |
3.43e-05 |
|
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: 45.89 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 24 LMISRALGVISGLLIVGQAWLLARILHRMIMENIPATALVLPFIVLVLIFVLRAWVVWLRERVGfyagQHIRYEIRRQVL 103
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTG----ERVVLDLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 104 DRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQM-----TLAASVPLLIVItifpiNWAAALILLGTAPLIPL 178
Cdd:cd18551 77 RRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLvtgvlTVVGAVVLMFLL-----DWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 179 FMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTS 258
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695777692 259 LSIALVavyfgfsylgeLNFGHYGV--GVTLMSGFLALILApeFFQ---PLRDLGTFYHAKAQAIGAAD 322
Cdd:cd18551 232 LALLVV-----------LGVGGARVasGALTVGTLVAFLLY--LFQlitPLSQLSSFFTQLQKALGALE 287
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
130-264 |
4.40e-05 |
|
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: 45.55 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 130 IDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLG----TAPLIPLFMALVGMGAAEANRRnflALARLSGHF 205
Cdd:cd18585 102 IDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAglllAGVVIPLLFYRLGKKIGQQLVQ---LRAELRTEL 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695777692 206 LDRLRGMETLRLFHRGEAETDNIRHASQDF--RQRTMEvlRLAFLSSGVLEFFTSLSIALV 264
Cdd:cd18585 179 VDGLQGMAELLIFGALERQRQQLEQLSDALikEQRRLA--RLSGLSQALMILLSGLTVWLV 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
369-570 |
4.57e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVNG-----------VELRDLDASRWHRL----LSWVGQ--- 430
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrsrqvIELSEQSAAQMRHVrgadMAMIFQepm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 431 ---NPQLP-----AATLRENVLLAWPEASeAQLQLALDKAWVSE---FISQLPQgintpvgdqagRLSVGQAQRIAVARA 499
Cdd:PRK10261 115 tslNPVFTvgeqiAESIRLHQGASREEAM-VEAKRMLDQVRIPEaqtILSRYPH-----------QLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 500 LLVPCRLLLLDEPAASLDAHSEQRVMQaLFNASSQQTTLMV---THQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMSMGVifiTHDMGVVAEIaDRVLVMYQGEAVETGSVEQI 256
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
378-398 |
6.75e-05 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 42.61 E-value: 6.75e-05
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
24-324 |
1.02e-04 |
|
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: 44.40 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 24 LMISRALGVISGLLIvGQawLLARILHRMIMENIPATALVLpfivlVLIFVLRAWVVWLRERVGFYAGQHIRYEIRRQVL 103
Cdd:cd18576 5 LLLSSAIGLVFPLLA-GQ--LIDAALGGGDTASLNQIALLL-----LGLFLLQAVFSFFRIYLFARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 104 DRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMtLAASVPLLI-VITIFPINWAAALILLGTAPLIPLFMAL 182
Cdd:cd18576 77 RHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEF-LRQILTLIGgVVLLFFISWKLTLLMLATVPVVVLVAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 183 VGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIA 262
Cdd:cd18576 156 FGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIV 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 263 LVaVYFGFSYL--GELNFGHYgVGVTLMSGFLAlilapeffQPLRDLGTFYHAKAQAIGAADSL 324
Cdd:cd18576 236 AV-LWYGGRLVlaGELTAGDL-VAFLLYTLFIA--------GSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
350-531 |
1.10e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 44.93 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDaIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLV-NGVELRDLDASRwhrllsw 427
Cdd:TIGR03719 323 IEAEN-LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQeQPDSGTIEIgETVKLAYVDQSR------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 428 vgqnpqlPAATLRENVllaWPEASEAQLQLALDK------AWVSEFisqlpqgiNTPVGDQ---AGRLSVGQAQRIAVAR 498
Cdd:TIGR03719 395 -------DALDPNKTV---WEEISGGLDIIKLGKreipsrAYVGRF--------NFKGSDQqkkVGQLSGGERNRVHLAK 456
|
170 180 190
....*....|....*....|....*....|...
gi 695777692 499 ALLVPCRLLLLDEPAASLDAHSeqrvMQALFNA 531
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVET----LRALEEA 485
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
327-565 |
1.37e-04 |
|
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: 44.79 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 327 FMEkpLAQETRGEKLLSDNEPIgLEARD----------AIVKSPEGkilagpLNFTLPAGKRVVLVGQSGSGKSSLLNAL 396
Cdd:TIGR03269 260 FME--GVSEVEKECEVEVGEPI-IKVRNvskryisvdrGVVKAVDN------VSLEVKEGEIFGIVGTSGAGKTTLSKII 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 397 TGFLPYD--------GSLLVNGVELRDLDASRWHRLLSWVGQNPQL-PAATLRENVllawPEASEAQL--QLALDKAW-- 463
Cdd:TIGR03269 331 AGVLEPTsgevnvrvGDEWVDMTKPGPDGRGRAKRYIGILHQEYDLyPHRTVLDNL----TEAIGLELpdELARMKAVit 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 464 --VSEFISQLPQGINTPVGDQagrLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQ--QTTLM 539
Cdd:TIGR03269 407 lkMVGFDEEKAEEILDKYPDE---LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFII 483
|
250 260
....*....|....*....|....*..
gi 695777692 540 VTHQLEGIAD-WDAIWVMQDGQIVEQG 565
Cdd:TIGR03269 484 VSHDMDFVLDvCDRAALMRDGKIVKIG 510
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
379-578 |
1.55e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 43.55 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 379 VVLVGQSGSGKSSLLNALTGFLPYDGsllvnGVELRDLDAsrwhrllswVGQNPQLPAA----TLREnvLLawpeaSEAQ 454
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDE-----GDIEIELDT---------VSYKPQYIKAdyegTVRD--LL-----SSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 455 LQLALDKAWVSEFISqlPQGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDahSEQRVMQA----LFN 530
Cdd:cd03237 87 KDFYTHPYFKTEIAK--PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMASkvirRFA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695777692 531 ASSQQTTLMVTHqlegiaDWDAIWVMQDGQIVEQGTYSQLAMANGPFA 578
Cdd:cd03237 163 ENNEKTAFVVEH------DIIMIDYLADRLIVFEGEPSVNGVANPPQS 204
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
358-570 |
1.99e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.64 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 358 KSPEGKILA-GPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVNGVELRDLD----ASRWHRLL-----SW 427
Cdd:PRK15093 14 KTSDGWVKAvDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDllrlSPRERRKLvghnvSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 428 VGQNPQL---PAATLRENVLLA---WPEASEAQLQLALDKAWVSEFISQLpqGINTP---VGDQAGRLSVGQAQRIAVAR 498
Cdd:PRK15093 94 IFQEPQScldPSERVGRQLMQNipgWTYKGRWWQRFGWRKRRAIELLHRV--GIKDHkdaMRSFPYELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 499 ALLVPCRLLLLDEPAASLDAHSEQRVMQAL--FNASSQQTTLMVTHQLEGIADW-DAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLtrLNQNNNTTILLISHDLQMLSQWaDKINVLYCGQTVETAPSKEL 246
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
369-569 |
2.01e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 44.16 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFtLPAGKRVVLvGQSGSGKSSLLNALTGF-LPYDG-SLLVNGVElrdldasrwhrllswVG---QNPQL-PAATLREN 442
Cdd:TIGR03719 26 LSF-FPGAKIGVL-GLNGAGKSTLLRIMAGVdKDFNGeARPQPGIK---------------VGylpQEPQLdPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 443 VLLAWPE--------------------------ASEAQLQLALD--KAWvsEFISQLPQGINT---PVGDQ-AGRLSVGQ 490
Cdd:TIGR03719 89 VEEGVAEikdaldrfneisakyaepdadfdklaAEQAELQEIIDaaDAW--DLDSQLEIAMDAlrcPPWDAdVTKLSGGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 491 AQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALfnASSQQTTLMVTHQ---LEGIADWdaIWVMQDGQ-IVEQGT 566
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL--QEYPGTVVAVTHDryfLDNVAGW--ILELDRGRgIPWEGN 242
|
...
gi 695777692 567 YSQ 569
Cdd:TIGR03719 243 YSS 245
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
375-396 |
2.08e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 43.65 E-value: 2.08e-04
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
350-571 |
2.10e-04 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 42.92 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 350 LEARDaIVKSPEGKILAGPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWHRLlsWV 428
Cdd:cd03218 1 LRAEN-LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDsGKILLDGQDITKLPMHKRARL--GI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 429 GQNPQLPAA----TLRENVLLAwpeaseaqLQLA-LDKAWVSEFISQLPQGIN-TPVGDQ-AGRLSVGQAQRIAVARALL 501
Cdd:cd03218 78 GYLPQEASIfrklTVEENILAV--------LEIRgLSKKEREEKLEELLEEFHiTHLRKSkASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 502 VPCRLLLLDEPAASLD--AHSE-QRVMQALfnaSSQQTTLMVT----HQLEGIAdwDAIWVMQDGQIVEQGTYSQLA 571
Cdd:cd03218 150 TNPKFLLLDEPFAGVDpiAVQDiQKIIKIL---KDRGIGVLITdhnvRETLSIT--DRAYIIYEGKVLAEGTPEEIA 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
369-550 |
2.14e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.02 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPydGSLLVNGVELRDLDASRWHRLLSWVGQNPQLPAATlrenVLLAWP 448
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK--GTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAV----ELLNAV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 449 EASEAQLQLALDKawvsefisqlpqgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQAL 528
Cdd:COG2401 123 GLSDAVLWLRRFK-----------------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL 179
|
170 180
....*....|....*....|....
gi 695777692 529 FNASSQQ--TTLMVTHQLEgIADW 550
Cdd:COG2401 180 QKLARRAgiTLVVATHHYD-VIDD 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
367-517 |
2.39e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.91 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 367 GPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELRDLDASRWhrlLSWVGQNPQLPA--ATLRENV 443
Cdd:PRK13543 28 GPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVEsGQIQIDGKTATRGDRSRF---MAYLGHLPGLKAdlSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 444 LLAWPEASEAQlqlaldkawvsefisQLPQGINTPVG-----DQAGR-LSVGQAQRIAVARALLVPCRLLLLDEPAASLD 517
Cdd:PRK13543 105 FLCGLHGRRAK---------------QMPGSALAIVGlagyeDTLVRqLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
376-398 |
2.52e-04 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 41.71 E-value: 2.52e-04
10 20
....*....|....*....|...
gi 695777692 376 GKRVVLVGQSGSGKSSLLNALTG 398
Cdd:cd04164 3 GIKVVIAGKPNVGKSSLLNALAG 25
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
328-565 |
3.14e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 328 MEKPLAQETRGE-KLLSDNEPIgLEARDAIVKSPegkILAGPLN-------------FTLPAGKRVVLVGQSGSGKSSLL 393
Cdd:PRK10261 292 LEHPAKQEPPIEqDTVVDGEPI-LQVRNLVTRFP---LRSGLLNrvtrevhavekvsFDLWPGETLSLVGESGSGKSTTG 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 394 NALTGFL-PYDGSLLVNGVELRDLDASRWH---RLLSWVGQNPQL---PAATLRENVL-------LAWPEASEAQLqlal 459
Cdd:PRK10261 368 RALLRLVeSQGGEIIFNGQRIDTLSPGKLQalrRDIQFIFQDPYAsldPRQTVGDSIMeplrvhgLLPGKAAAARV---- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 460 dkAWVSEFISQLPQgintpvgdQAGR----LSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQ 535
Cdd:PRK10261 444 --AWLLERVGLLPE--------HAWRypheFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDF 513
|
250 260 270
....*....|....*....|....*....|....*
gi 695777692 536 --TTLMVTHQL---EGIADWDAiwVMQDGQIVEQG 565
Cdd:PRK10261 514 giAYLFISHDMavvERISHRVA--VMYLGQIVEIG 546
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
369-561 |
3.22e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.50 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP-YDGSLLVNGVELRDLD-ASRWHRLLSWVGQNPQlpAATLRENVLLA 446
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPaRGGRIMLNGKEINALStAQRLARGLVYLPEDRQ--SSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 447 WPEASEAQ------LQLALDKAWVSEFISQLpqGINTPVGDQAGR-LSVGQAQRIAVARALLVPCRLLLLDEPAASLDAH 519
Cdd:PRK15439 360 WNVCALTHnrrgfwIKPARENAVLERYRRAL--NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695777692 520 SEQRVMQALFNASSQQTT-LMVT---HQLEGIAdwDAIWVMQDGQI 561
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAvLFISsdlEEIEQMA--DRVLVMHQGEI 481
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-270 |
5.36e-04 |
|
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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 42.08 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 24 LMISRALGVISGLLIVGQAWLLARILHRMIME-NIPATALVLPFIVLVLIF--VLRAWVVWLRERVGfyagQHIRYEIRR 100
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQgDLGLLVLLALGMVAVAVAsaLLGVVQTYLSARIG----QGVMYDLRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 101 QVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPLIPLFM 180
Cdd:cd18550 77 QLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 181 ALVGMGAAEANRRNFLALARLSGHFLDRLR--GMETLRLFHRGEAETDNIRHASQDFRQ---RTMEVLRLAFLssgVLEF 255
Cdd:cd18550 157 RRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDlgvRQALAGRWFFA---ALGL 233
|
250
....*....|....*
gi 695777692 256 FTSLSIALVAVYFGF 270
Cdd:cd18550 234 FTAIGPALVYWVGGL 248
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
378-398 |
1.20e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 41.29 E-value: 1.20e-03
|
| RecA-like_BCS1 |
cd19510 |
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ... |
381-431 |
1.72e-03 |
|
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410918 [Multi-domain] Cd Length: 153 Bit Score: 39.26 E-value: 1.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 695777692 381 LVGQSGSGKSSLLNALTGFLPYDGSLLvngvEL--RDLDASRWHRLLSWVGQN 431
Cdd:cd19510 28 LYGPPGTGKSSFIAALAGELDYDICDL----NLseVVLTDDRLNHLLNTAPKQ 76
|
|
| Dynamin_N |
pfam00350 |
Dynamin family; |
379-401 |
2.04e-03 |
|
Dynamin family;
Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 39.14 E-value: 2.04e-03
|
| PRK12288 |
PRK12288 |
small ribosomal subunit biogenesis GTPase RsgA; |
375-411 |
2.44e-03 |
|
small ribosomal subunit biogenesis GTPase RsgA;
Pssm-ID: 237039 [Multi-domain] Cd Length: 347 Bit Score: 40.22 E-value: 2.44e-03
10 20 30
....*....|....*....|....*....|....*..
gi 695777692 375 AGKRVVLVGQSGSGKSSLLNALtgfLPyDGSLLVNGV 411
Cdd:PRK12288 204 TGRISIFVGQSGVGKSSLINAL---LP-EAEILVGDV 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
370-571 |
2.50e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 370 NFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPydgslLVNGvELRdldaSRWHR--LLSWVGQNPQLPAATLRENVLLAW 447
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELP-----LLSG-ERQ----SQFSHitRLSFEQLQKLVSDEWQRNNTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 448 PE-------ASEAQLQLALDKAWVSEFISQLpqGINTPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHS 520
Cdd:PRK10938 93 PGeddtgrtTAEIIQDEVKDPARCEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695777692 521 EQRVMQALFNASSQQTTLM-VTHQLEGIADW-DAIWVMQDGQIVEQGT---------YSQLA 571
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVlVLNRFDEIPDFvQFAGVLADCTLAETGEreeilqqalVAQLA 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
376-543 |
3.88e-03 |
|
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: 38.76 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 376 GKRVVLVGQSGSGKSSLLNAL-----TGFLpyDGSLLVNGVELRDldasRWHRLLSWVGQNP-QLPAATLRENVLLAwpe 449
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLagrktAGVI--TGEILINGRPLDK----NFQRSTGYVEQQDvHSPNLTVREALRFS--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 450 aseaqlqlaldkAWVSEfisqlpqgintpvgdqagrLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALF 529
Cdd:cd03232 104 ------------ALLRG-------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
170
....*....|....*
gi 695777692 530 N-ASSQQTTLMVTHQ 543
Cdd:cd03232 153 KlADSGQAILCTIHQ 167
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
376-440 |
4.30e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.12 E-value: 4.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695777692 376 GKRVVLVGQSGSGKSSLLNALTGFLPYDGS--LLVNGVELRDLDASRWHRLLSWVGQNPQLPAATLR 440
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGgvIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLR 68
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
380-398 |
4.45e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 38.21 E-value: 4.45e-03
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
375-403 |
4.64e-03 |
|
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 38.29 E-value: 4.64e-03
10 20
....*....|....*....|....*....
gi 695777692 375 AGKRVVLVGQSGSGKSSLLNALTGFLPYD 403
Cdd:cd01130 11 ARKNILISGGTGSGKTTLLNALLSFIPPD 39
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
379-398 |
4.85e-03 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 38.26 E-value: 4.85e-03
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
365-573 |
4.98e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.60 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 365 LAGP----LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNGVELrdldasrwhrllswVGQNPQLPAA-- 437
Cdd:PRK10762 263 LSGPgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTsGYVTLDGHEV--------------VTRSPQDGLAng 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 438 -----------------TLRENV-LLAWPEASEA--QLQLALDKAWVSEFISQLpqGINTPVGDQA-GRLSVGQAQRIAV 496
Cdd:PRK10762 329 ivyisedrkrdglvlgmSVKENMsLTALRYFSRAggSLKHADEQQAVSDFIRLF--NIKTPSMEQAiGLLSGGNQQKVAI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 497 ARALLVPCRLLLLDEPAASLDAHSEQRVMQaLFNASSQQ--TTLMVTHQL-EGIADWDAIWVMQDGQI-----VEQGTYS 568
Cdd:PRK10762 407 ARGLMTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKAEglSIILVSSEMpEVLGMSDRILVMHEGRIsgeftREQATQE 485
|
....*
gi 695777692 569 QLaMA 573
Cdd:PRK10762 486 KL-MA 489
|
|
| DLP_1 |
cd08771 |
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ... |
371-401 |
5.28e-03 |
|
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206738 Cd Length: 278 Bit Score: 39.15 E-value: 5.28e-03
10 20 30
....*....|....*....|....*....|....
gi 695777692 371 FTLPagkRVVLVG-QSgSGKSSLLNALTG--FLP 401
Cdd:cd08771 1 IDLP---QIVVVGdQS-SGKSSVLEALVGrdFLP 30
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
21-307 |
5.99e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 39.00 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 21 RRWLMISRALGVISGLLIVGQAWLLARILHRMIMENIPATaLVLPFIVLVLIFVLRAWVVWLRERVGFYAGQHIRYEIRR 100
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDG-LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 101 QVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMTLAASVPLLIVITIFPINWAAALILLGTAPliplFM 180
Cdd:cd18540 80 KAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVP----VL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 181 ALVGMgaaeANRRNFLALAR--------LSGHFLDRLRGMETLRLFHRGEAETDNIRHASQDFRQRTMEVLRLAFLSSGV 252
Cdd:cd18540 156 AVVSI----YFQKKILKAYRkvrkinsrITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 695777692 253 LEFFTSLSIALVAVYFGFSYL-GELNFGhygvgvTLMSgFLALILapEFFQPLRDL 307
Cdd:cd18540 232 VLFLGSIATALVLWYGGILVLaGAITIG------TLVA-FISYAT--QFFEPIQQL 278
|
|
| FeoB_N |
pfam02421 |
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ... |
377-398 |
6.07e-03 |
|
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.
Pssm-ID: 460552 [Multi-domain] Cd Length: 156 Bit Score: 37.81 E-value: 6.07e-03
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
155-268 |
6.18e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). 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.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 39.08 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 155 VITIFPINWAAALILLGTAPLIPLFMALVGMGAAEANRRNFLALARLSGHFLDRLRGMETLRLFHRGEAETDNirhasqd 234
Cdd:cd18557 128 LIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRR------- 200
|
90 100 110
....*....|....*....|....*....|....*....
gi 695777692 235 FRQRTMEVLRLAF---LSSGVLEFFTSLSI--ALVAVYF 268
Cdd:cd18557 201 YSEALDRSYRLARkkaLANALFQGITSLLIylSLLLVLW 239
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
371-517 |
6.27e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.55 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 371 FTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYD-GSLLVNgvelRDLDASR----------------------------- 420
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDdGRIIYE----QDLIVARlqqdpprnvegtvydfvaegieeqaeylk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 421 -WHRLLSWVGQNPQlpaatlrENVLlawpeASEAQLQLALD--KAW-----VSEFISQLPQGINTPVGDqagrLSVGQAQ 492
Cdd:PRK11147 100 rYHDISHLVETDPS-------EKNL-----NELAKLQEQLDhhNLWqlenrINEVLAQLGLDPDAALSS----LSGGWLR 163
|
170 180
....*....|....*....|....*
gi 695777692 493 RIAVARALLVPCRLLLLDEPAASLD 517
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
362-570 |
6.44e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 38.71 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 362 GKILA-GPLNFTLPAGKRVVLVGQSGSGKSSLLNALTGF-LPYDGSLLVNGVELRDLDASRWHR-LLSWVGQNPQLPA-A 437
Cdd:PRK11614 16 GKIQAlHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDpRATSGRIVFDGKDITDWQTAKIMReAVAIVPEGRRVFSrM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 438 TLRENVLLAWPEASEAQLQLALdkAWVSEFISQLPQgintPVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLD 517
Cdd:PRK11614 96 TVEENLAMGGFFAERDQFQERI--KWVYELFPRLHE----RRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695777692 518 AHSEQRVMQALFNASSQQTTLMVTHQ--LEGIADWDAIWVMQDGQIVEQGTYSQL 570
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
376-398 |
7.03e-03 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 39.32 E-value: 7.03e-03
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
369-550 |
7.62e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 37.69 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALtgflpydgsllvngvelrdLDASRWHRLLSWVGQNPQLPAATLrenvllawp 448
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVNEG-------------------LYASGKARLISFLPKFSRNKLIFI--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 449 easeAQLQLALDkawvsefisqlpQGIN-TPVGDQAGRLSVGQAQRIAVAR--ALLVPCRLLLLDEPAASLDAHSEQRVM 525
Cdd:cd03238 66 ----DQLQFLID------------VGLGyLTLGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLL 129
|
170 180
....*....|....*....|....*...
gi 695777692 526 QALFNASSQQTTL-MVTHQLEGI--ADW 550
Cdd:cd03238 130 EVIKGLIDLGNTViLIEHNLDVLssADW 157
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
331-545 |
8.22e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.84 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 331 PLAQETRGEKLLSDNEPIgLEARDAIVKSPEGKILAGpLNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLP--YDGSLLV 408
Cdd:PRK10938 243 PEPDEPSARHALPANEPR-IVLNNGVVSYNDRPILHN-LSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgYSNDLTL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 409 NGVElRDLDASRW--HRLLSWVGQNPQLP---AATLReNVLLA--------WPEASEAQLQLAldkawvSEFISQLpqGI 475
Cdd:PRK10938 321 FGRR-RGSGETIWdiKKHIGYVSSSLHLDyrvSTSVR-NVILSgffdsigiYQAVSDRQQKLA------QQWLDIL--GI 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695777692 476 NTPVGDQAGR-LSVGQaQRIA-VARALLVPCRLLLLDEPAASLDAHSEQRVMQALFNASSQQTT--LMVTHQLE 545
Cdd:PRK10938 391 DKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSHHAE 463
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
376-398 |
8.80e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 8.80e-03
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
369-544 |
9.09e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 38.17 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 369 LNFTLPAGKRVVLVGQSGSGKSSLLNALTGFLPYDGSLLVNGVELRdldasrwhrlLSWVGQ----NPQLPAATLRenVL 444
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR----------IGYVPQklylDTTLPLTVNR--FL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695777692 445 LAWPEASEAQLQLALDKAWVSEFISQLPQgintpvgdqagRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEqrv 524
Cdd:PRK09544 91 RLRPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ--- 156
|
170 180
....*....|....*....|....*.
gi 695777692 525 mQALFNASSQQTT------LMVTHQL 544
Cdd:PRK09544 157 -VALYDLIDQLRReldcavLMVSHDL 181
|
|
| |
