|
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: 1092.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 1 MNKSRQKELTRWLKQQSVISQRWLNISRLLGFVSGILIIAQAWFMARILQHMIMENIPREALLLPFTLLVLTFVLRAWVV 80
Cdd:PRK11174 1 MDKSRQKELTRWLKQQSKPAKRWLNLSILLGFLSGLLLIAQAWLLATILQALIIENIPREALLPPFILLILLFVLRALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 81 WLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFP 160
Cdd:PRK11174 81 WLRERVGFKAGQHIRQQIRQQVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 161 SNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTM 240
Cdd:PRK11174 161 INWAAGLILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 241 EVLRLAFLSSGILEFFTSLSIALVAVYFGFSYLGELDFGHYDTGVTLAAGFLALILAPEFFQPLRDLGTFYHAKAQAVGA 320
Cdd:PRK11174 241 EVLRMAFLSSAVLEFFASISIALVAVYFGFSYLGELNFGHYGTGVTLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 321 ADSLKTFMETPLAHPQRGEAELALTDPLTIEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL 400
Cdd:PRK11174 321 AESLVTFLETPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 401 SYQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVG 480
Cdd:PRK11174 401 PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 481 DQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGR 560
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
570 580
....*....|....*....|....*...
gi 446966322 561 IIEQGRYAELSVAGGPFATLLAHRQEEI 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: 755.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 6 QKELTRWLKQQSVISQRWLNISRLLGFVSGILIIAQAWFMARILQHMIMENIPREALLLPFTLLVLTFVLRAWVVWLRER 85
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 86 VGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAA 165
Cdd:COG4988 81 AAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 166 ALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRL 245
Cdd:COG4988 161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 246 AFLSSGILEFFTSLSIALVAVYFGFSYLGeldfghydTGVTLAAGFLALILAPEFFQPLRDLGTFYHAKAQAVGAADSLK 325
Cdd:COG4988 241 AFLSSAVLEFFASLSIALVAVYIGFRLLG--------GSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 326 TFMETPLAHPQRGEAELALTDPLTIEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQG 404
Cdd:COG4988 313 ALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPpYSG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 405 SLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAA 484
Cdd:COG4988 393 SILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 485 RLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQ 564
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
570
....*....|.
gi 446966322 565 GRYAELSVAGG 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: 563.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 21 QRWLNISRLLGFVSGILIIAQAWFMARILQHMIMENIPREALLLPFTLLVLTFVLRAWVVWLRERVGYHAGQHIRFAIRR 100
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 101 QVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFM 180
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 181 ALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLS 260
Cdd:TIGR02857 162 ILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 261 IALVAVYFGFSYLGEldfghydtGVTLAAGFLALILAPEFFQPLRDLGTFYHAKAQAVGAADSLKTFMETPlAHPQRGEA 340
Cdd:TIGR02857 242 VALVAVYIGFRLLAG--------DLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAA-PRPLAGKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 341 ELALTDPLTIEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPE 419
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDpTEGSIAVNGVPLADADAD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 420 SWRKHLSWVGQNPQLPAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARA 499
Cdd:TIGR02857 393 SWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 500 LLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVM 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 |
1.85e-128 |
|
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: 378.29 E-value: 1.85e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 29 LLGFVSGILIIAQAWFMARILQHMIMENIPREALLLPFTLLVLTFVLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQ 108
Cdd:cd18584 3 LLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 109 AGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAA 188
Cdd:cd18584 83 LGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKAAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 189 DANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVAVYF 268
Cdd:cd18584 163 AASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAVYI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 269 GFSYLGEldfghydtGVTLAAGFLALILAPEFFQPLRDLGTFYHAKAQAVGAADSL 324
Cdd:cd18584 243 GFRLLGG--------SLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-587 |
5.31e-107 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 333.28 E-value: 5.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 1 MNKSRQKELtRWLKQQSVISQRWLNISRLLGFVSGILIIAQAWFMARILQHMImENIPREALLLPFTLLVLTFVLRAWVV 80
Cdd:COG1132 1 MSKSPRKLL-RRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-AGGDLSALLLLLLLLLGLALLRALLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 81 WLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFP 160
Cdd:COG1132 79 YLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 161 SNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTM 240
Cdd:COG1132 159 IDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 241 EVLRLAFLSSGILEFFTSLSIALVAVYFGFSYL-GELDFGhydtgvTLAAgFLALILApeFFQPLRDLGTFYHAKAQAVG 319
Cdd:COG1132 239 RAARLSALFFPLMELLGNLGLALVLLVGGLLVLsGSLTVG------DLVA-FILYLLR--LFGPLRQLANVLNQLQRALA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 320 AADSLKTFMETPLAHPQRGEAELALTDPLTIEAEDLFITSPEGK-TLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSG 398
Cdd:COG1132 310 SAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRpVLKD-ISLTIPPGETVALVGPSGSGKSTLVNLLLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 399 FLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDT 477
Cdd:COG1132 389 FYDPTsGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 478 PVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQ 557
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLD 548
|
570 580 590
....*....|....*....|....*....|
gi 446966322 558 DGRIIEQGRYAELSVAGGPFATLLAHRQEE 587
Cdd:COG1132 549 DGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
27-324 |
2.10e-106 |
|
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: 321.54 E-value: 2.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 27 SRLLGFVSGILIIAQAWFMARILQHMIMeNIPREALLLPFTLLVLTFVLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRL 106
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFA-GGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 107 QQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFMALVGMG 186
Cdd:cd18561 80 LKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 187 AADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVAV 266
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 267 YFGFSYLGeldfghydTGVTLAAGFLALILAPEFFQPLRDLGTFYHAKAQAVGAADSL 324
Cdd:cd18561 240 VGALRVLG--------GQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
98-583 |
2.85e-87 |
|
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: 281.65 E-value: 2.85e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 98 IRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILLG----TA 173
Cdd:COG4987 90 LRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALglllAG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 174 PLIPLFMALVGMGAADANRRnflALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGIL 253
Cdd:COG4987 170 LLLPLLAARLGRRAGRRLAA---ARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 254 EFFTSLSIALVAVYfgfsyLGELDFGHYDTGVTLAAGFLALILAPEFFQPLRDlgtFYHAKAQAVGAADSLKTFMETPLA 333
Cdd:COG4987 247 QLAAGLAVVAVLWL-----AAPLVAAGALSGPLLALLVLAALALFEALAPLPA---AAQHLGRVRAAARRLNELLDAPPA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 334 HPQRGEAElALTDPLTIEAEDL-FITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGI 411
Cdd:COG4987 319 VTEPAEPA-PAPGGPSLELEDVsFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQsGSITLGGV 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 412 ELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQA 491
Cdd:COG4987 398 DLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGER 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 492 QRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELS 571
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
490
....*....|..
gi 446966322 572 VAGGPFATLLAH 583
Cdd:COG4987 558 AQNGRYRQLYQR 569
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
72-580 |
9.21e-75 |
|
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: 252.06 E-value: 9.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 72 TFVLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLV--LEQIDDMhdyyaryLPQMALAVS 149
Cdd:COG2274 205 ALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFrdVESIREF-------LTGSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 150 VPLLIVV----AIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEI 225
Cdd:COG2274 278 LDLLFVLifliVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 226 ESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVaVYFGfSYL---GELDFGhydtgvTLAAgFLALILApeFFQ 302
Cdd:COG2274 358 RRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVAL-LWLG-AYLvidGQLTLG------QLIA-FNILSGR--FLA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 303 PLRDLGTFYHAKAQAVGAADSLKTFMETPLAHPQRGEAELALTDPLTIEAEDLFITSPEGKTLA-GPLNFTLPAGQRAVL 381
Cdd:COG2274 427 PVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVlDNISLTIKPGERVAI 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 382 VGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARPDASEQELQAALD 460
Cdd:COG2274 507 VGRSGSGKSTLLKLLLGLYEpTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAAR 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 461 NAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMV 540
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446966322 541 THQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATL 580
Cdd:COG2274 667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
84-544 |
2.60e-58 |
|
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: 203.75 E-value: 2.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 84 ER-VGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSN 162
Cdd:TIGR02868 73 ERlVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 163 WAAALILLGTAPLIPLFMALVgmgAADANRRNFLALARLSGHFLDR----LRGMETLRIFGRGEAEIESIRSASEDFRQR 238
Cdd:TIGR02868 153 VPAALILAAGLLLAGFVAPLV---SLRAARAAEQALARLRGELAAQltdaLDGAAELVASGALPAALAQVEEADRELTRA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 239 TMEVLRLAFLSSGILEFFTSLSIALVAVYFGFSYLGeldfgHYDTGVTLAAGFLALILAPEFFQPLRDlgtfyhAKAQAV 318
Cdd:TIGR02868 230 ERRAAAATALGAALTLLAAGLAVLGALWAGGPAVAD-----GRLAPVTLAVLVLLPLAAFEAFAALPA------AAQQLT 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 319 GAADSLKTFMETPLAHPQRGEAELALTDPL-----TIEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLL 393
Cdd:TIGR02868 299 RVRAAAERIVEVLDAAGPVAEGSAPAAGAVglgkpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 394 NALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLP 472
Cdd:TIGR02868 379 ATLAGLLDpLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALP 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446966322 473 QGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQL 544
Cdd:TIGR02868 459 DGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
358-585 |
1.68e-52 |
|
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: 179.66 E-value: 1.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 358 TSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFlsY---QGSLRINGIELRDLSPESWRKHLSWVGQNPQL 434
Cdd:cd03249 12 SRPDVPILKG-LSLTIPPGKTVALVGSSGCGKSTVVSLLERF--YdptSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 435 PAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAA 514
Cdd:cd03249 89 FDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446966322 515 SLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFAtLLAHRQ 585
Cdd:cd03249 169 ALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYA-KLVKAQ 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
350-580 |
2.15e-52 |
|
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: 179.35 E-value: 2.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDL-FITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSW 427
Cdd:cd03253 1 IEFENVtFAYDPGRPVLKD-VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSsGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 428 VGQNPQLPAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLL 507
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446966322 508 LLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATL 580
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
98-580 |
3.40e-51 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 185.31 E-value: 3.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 98 IRRQVLDRLQQAGPAWIQGKPAGSwatlVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFP----SNWAAALILLGTA 173
Cdd:TIGR02203 89 IRVRMFEKLLGLPVSFFDRQPTGT----LLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIvllyYSWQLTLIVVVML 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 174 PLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGIL 253
Cdd:TIGR02203 165 PVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPIT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 254 EFFTSLSIALVAVYFGFSYLgeldfghydTGVTLAAGFLALILAP-EFFQPLRDLGTFYHAKAQAVGAADSLKTFMETPL 332
Cdd:TIGR02203 245 QLIASLALAVVLFIALFQAQ---------AGSLTAGDFTAFITAMiALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 333 A------HPQRGEAElaltdpltIEAEDLFITSP--EGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-Q 403
Cdd:TIGR02203 316 EkdtgtrAIERARGD--------VEFRNVTFRYPgrDRPALDS-ISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPdS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 404 GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARP-DASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQ 482
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGEN 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 483 AARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRII 562
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
490
....*....|....*...
gi 446966322 563 EQGRYAELSVAGGPFATL 580
Cdd:TIGR02203 547 ERGTHNELLARNGLYAQL 564
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
350-560 |
3.90e-50 |
|
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: 170.64 E-value: 3.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDL-FITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSW 427
Cdd:cd03228 1 IEFKNVsFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDpTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 428 VGQNPQLPAATLRDNVllarpdaseqelqaaldnawvseflpllpqgvdtpvgdqaarLSVGQAQRVAVARALLNPCSLL 507
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446966322 508 LLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGR 560
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
369-580 |
1.53e-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: 1.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLAR 447
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 PDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEA 527
Cdd:cd03251 101 PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446966322 528 LNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATL 580
Cdd:cd03251 181 LERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
361-565 |
2.37e-48 |
|
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: 167.77 E-value: 2.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 361 EGKTLAGPlNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATL 439
Cdd:cd03245 16 EIPALDNV-SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTsGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 440 RDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAH 519
Cdd:cd03245 95 RDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446966322 520 SEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:cd03245 175 SEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
369-575 |
6.46e-46 |
|
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: 161.62 E-value: 6.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLAR 447
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 PDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEA 527
Cdd:cd03254 102 PNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446966322 528 LNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGG 575
Cdd:cd03254 182 LEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
369-587 |
7.32e-45 |
|
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: 168.07 E-value: 7.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFlsY---QGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLL 445
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRF--YdvtSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAY 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 446 ARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVM 525
Cdd:COG5265 455 GRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQ 534
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446966322 526 EALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLLAHRQEE 587
Cdd:COG5265 535 AALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEE 596
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
152-584 |
1.19e-44 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 167.12 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 152 LLIVvaIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSA 231
Cdd:PRK11176 156 LFIM--MFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 232 SEDFRQRTMEVLRLAFLSSGILEFFTSLsiALVAVYFGFSYLGELDfghydtgvTLAAGFLALILAPEF--FQPLRDLgT 309
Cdd:PRK11176 234 SNRMRQQGMKMVSASSISDPIIQLIASL--ALAFVLYAASFPSVMD--------TLTAGTITVVFSSMIalMRPLKSL-T 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 310 FYHAKAQ-AVGAADSLKTF--METPLAHPQRgEAELALTDpltIEAEDLFITSPEGKTLA-GPLNFTLPAGQRAVLVGRS 385
Cdd:PRK11176 303 NVNAQFQrGMAACQTLFAIldLEQEKDEGKR-VIERAKGD---IEFRNVTFTYPGKEVPAlRNINFKIPAGKTVALVGRS 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 386 GSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARPDA-SEQELQAALDNAW 463
Cdd:PRK11176 379 GSGKSTIANLLTRFYDiDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAY 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 464 VSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQ 543
Cdd:PRK11176 459 AMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446966322 544 LEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLlaHR 584
Cdd:PRK11176 539 LSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL--HK 577
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
24-292 |
1.94e-44 |
|
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: 158.96 E-value: 1.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 24 LNISRLLGFVSGILIIAQAWFMARILQHMIMENIPR-EALLLPFTLLVLTFVLRAWVVWLRERVGYHAGQHIRFAIRRQV 102
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 103 LDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFMAL 182
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 183 VGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIA 262
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|..
gi 446966322 263 LVAvYFGFSYL--GELDFGHYDTGVTLAAGFL 292
Cdd:pfam00664 241 LAL-WFGAYLVisGELSVGDLVAFLSLFAQLF 271
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
316-565 |
2.52e-44 |
|
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: 167.74 E-value: 2.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 316 QAVGAADSLKTFMETPLAHPqrGEAELALTDPLT--IEAEDLFITSPEGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSL 392
Cdd:TIGR03375 430 QAKTALQSLDELMQLPVERP--EGTRFLHRPRLQgeIEFRNVSFAYPGQETPAlDNVSLTIRPGEKVAIIGRIGSGKSTL 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 393 LNALSGFlsYQ---GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARPDASEQELQAALDNAWVSEFLP 469
Cdd:TIGR03375 508 LKLLLGL--YQpteGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVR 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 470 LLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAE 549
Cdd:TIGR03375 586 RHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDL 665
|
250
....*....|....*.
gi 446966322 550 WDVIWVMQDGRIIEQG 565
Cdd:TIGR03375 666 VDRIIVMDNGRIVADG 681
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
145-581 |
2.74e-41 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 157.82 E-value: 2.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 145 ALAVSVPLLIVVAIFpSNWAAALILLGTAPLIPLFMALV------GMGAADANRRNflalarLSGHFLDRLRGMETLRIF 218
Cdd:PRK13657 139 ATLVALVVLLPLALF-MNWRLSLVLVVLGIVYTLITTLVmrktkdGQAAVEEHYHD------LFAHVSDAIGNVSVVQSY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 219 GRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEffTSLSIALVAVYFGFSYL---GELDFGHYDTGVTLAAgflALI 295
Cdd:PRK13657 212 NRIEAETQALRDIADNLLAAQMPVLSWWALASVLNR--AASTITMLAILVLGAALvqkGQLRVGEVVAFVGFAT---LLI 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 296 lapeffQPLRDLGTFYHakaQAVGAADSLKTFMETPLAHPQRGEAELAlTDPL----TIEAEDLFITSPEGKTLAGPLNF 371
Cdd:PRK13657 287 ------GRLDQVVAFIN---QVFMAAPKLEEFFEVEDAVPDVRDPPGA-IDLGrvkgAVEFDDVSFSYDNSRQGVEDVSF 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 372 TLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARPDA 450
Cdd:PRK13657 357 EAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQsGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDA 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 451 SEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNA 530
Cdd:PRK13657 437 TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446966322 531 ASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLL 581
Cdd:PRK13657 517 LMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
154-575 |
2.36e-40 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 155.26 E-value: 2.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 154 IVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFgRGEAEI-ESIRSAS 232
Cdd:PRK10790 156 MLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF-RQQARFgERMGEAS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 233 EDFRQRTMEVLRL-AFLSSGILEFFTSLSIALVAVYFGFSYLGELdfghydtGVTLAAGFLALIlaPEFFQPLRDLGTFY 311
Cdd:PRK10790 235 RSHYMARMQTLRLdGFLLRPLLSLFSALILCGLLMLFGFSASGTI-------EVGVLYAFISYL--GRLNEPLIELTTQQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 312 HAKAQAVGAADSLKTFMETPlaHPQRGEAELALTDPlTIEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSS 391
Cdd:PRK10790 306 SMLQQAVVAGERVFELMDGP--RQQYGNDDRPLQSG-RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKST 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 392 LLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARpDASEQELQAALDNAWVSEFLPL 470
Cdd:PRK10790 383 LASLLMGYYPLTeGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARS 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 471 LPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALnAASLRQTTLMV-THQLEDLAE 549
Cdd:PRK10790 462 LPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVViAHRLSTIVE 540
|
410 420
....*....|....*....|....*.
gi 446966322 550 WDVIWVMQDGRIIEQGRYAELSVAGG 575
Cdd:PRK10790 541 ADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
130-583 |
5.00e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 153.83 E-value: 5.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 130 IDDMHDYYARYLPQMALAVSVplLIVVAIFPS--NWAAALILLGTAPLIPLFMALVGMGAADANRRNFLAL-ARLSGHFL 206
Cdd:PRK11160 127 VDTLDHLYLRLISPLVAALVV--ILVLTIGLSffDLTLALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLrAQYRVQLT 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 207 DRLRGMETLRIFGRGEAEIESIRSASEDF--RQRTMEvlRLAFLSSGILEFFTSLSIALVaVYFGFSYLGeldfGHYDTG 284
Cdd:PRK11160 205 EWLQGQAELTLFGAEDRYRQQLEQTEQQWlaAQRRQA--NLTGLSQALMILANGLTVVLM-LWLAAGGVG----GNAQPG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 285 VTLAAGFLALILAPEFFQPLRdlGTFYHAkAQAVGAADSLKTFME-TPLahPQRGEAELALTDPLTIEAEDLFITSPEGK 363
Cdd:PRK11160 278 ALIALFVFAALAAFEALMPVA--GAFQHL-GQVIASARRINEITEqKPE--VTFPTTSTAAADQVSLTLNNVSFTYPDQP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 364 TLA-GPLNFTLPAGQRAVLVGRSGSGKSSLLNALS-GFLSYQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRD 441
Cdd:PRK11160 353 QPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRD 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 442 NVLLARPDASEQELQAALDNAWVSEFLPLlPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSE 521
Cdd:PRK11160 433 NLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE 511
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446966322 522 QRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLLAH 583
Cdd:PRK11160 512 RQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQR 573
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
369-565 |
5.36e-37 |
|
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: 136.85 E-value: 5.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVllar 447
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVElSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 pD----ASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQR 523
Cdd:cd03244 99 -DpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDAL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446966322 524 VMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:cd03244 178 IQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
350-561 |
1.75e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.33 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITsPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSPESWRKHLSWV 428
Cdd:COG4619 1 LELEGLSFR-VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 429 GQNPQLPAATLRDNvlLARP-DASEQELQAALDNAWVSEFLplLPQGV-DTPVgdqaARLSVGQAQRVAVARALLNPCSL 506
Cdd:COG4619 80 PQEPALWGGTVRDN--LPFPfQLRERKFDRERALELLERLG--LPPDIlDKPV----ERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 507 LLLDEPAASLDAHSEQRVMEALN--AASLRQTTLMVTH---QLEDLAewDVIWVMQDGRI 561
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLReyLAEEGRAVLWVSHdpeQIERVA--DRVLTLEAGRL 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
197-581 |
3.37e-36 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 144.09 E-value: 3.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 197 ALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQ--RTMEVLRLAFLSsgILEFFTSLSIALVAVYFGFSYL- 273
Cdd:TIGR00958 335 AVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQlnKRKALAYAGYLW--TTSVLGMLIQVLVLYYGGQLVLt 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 274 GELDFGhydtgvtlaaGFLALILAPEFF-QPLRDLGTFYHAKAQAVGAADSLKTFMETPLAHPQRGEaeLA-LTDPLTIE 351
Cdd:TIGR00958 413 GKVSSG----------NLVSFLLYQEQLgEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGT--LApLNLEGLIE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 352 AEDL---FITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFlsYQ---GSLRINGIELRDLSPESWRKHL 425
Cdd:TIGR00958 481 FQDVsfsYPNRPDVPVLKG-LTFTLHPGEVVALVGPSGSGKSTVAALLQNL--YQptgGQVLLDGVPLVQYDHHYLHRQV 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 426 SWVGQNPQLPAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCS 505
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 506 LLLLDEPAASLDAHSEQRVMEALNAASLrqTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLL 581
Cdd:TIGR00958 638 VLILDEATSALDAECEQLLQESRSRASR--TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
356-580 |
1.11e-35 |
|
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: 133.77 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 356 FITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGF-LSYQGSLRINGIELRDLSPESWRKHLSWVGQNPQL 434
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 435 PAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAA 514
Cdd:cd03252 88 FNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 515 SLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATL 580
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
29-322 |
8.99e-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: 133.05 E-value: 8.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 29 LLGFVSGILIIAQAWFMARILQHMIMENIPREALLLPFTLLVLTFVLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQ 108
Cdd:cd18781 3 LLQWISLLANIAFVFSIANLLQKLLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 109 AGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAA 188
Cdd:cd18781 83 LGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKIAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 189 DANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFF----TSLSIALV 264
Cdd:cd18781 163 KLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVayggAALGIILA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 265 AVYFgfsYLGELdfghydtgvTLAAGFLALILAPEFFQPLRDLGTFYHAKAQAVGAAD 322
Cdd:cd18781 243 LLQF---ANGSI---------SLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAASD 288
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
358-561 |
1.02e-33 |
|
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: 127.97 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 358 TSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNPQLPA 436
Cdd:cd03248 23 TRPDTLVLQD-VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 437 ATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASL 516
Cdd:cd03248 102 RSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446966322 517 DAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRI 561
Cdd:cd03248 182 DAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
350-566 |
1.29e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 127.85 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKT----LAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSPESW--- 421
Cdd:COG1136 5 LELRNLTKSYGTGEGevtaLRG-VSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 422 -RKHLSWVGQNPQL-PAATLRDNVLLA------RPDASEQELQAALDNAWVSEFLPLLPqgvdtpvgdqaARLSVGQAQR 493
Cdd:COG1136 84 rRRHIGFVFQFFNLlPELTALENVALPlllagvSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 494 VAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALN--AASLRQTTLMVTHQlEDLAEW-DVIWVMQDGRIIEQGR 566
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHD-PELAARaDRVIRLRDGRIVSDER 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
368-514 |
1.60e-33 |
|
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: 125.07 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 368 PLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWVGQNPQL-PAATLRDNVLL 445
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLfPRLTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446966322 446 ArpdASEQELQAALDNAWVSEFLPLLPQG--VDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAA 514
Cdd:pfam00005 83 G---LLLKGLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
369-583 |
9.53e-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: 133.71 E-value: 9.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLL-A 446
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARsGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgA 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 RPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVME 526
Cdd:TIGR01193 573 KENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVN 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 527 alNAASLRQTTLM-VTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLLAH 583
Cdd:TIGR01193 653 --NLLNLQDKTIIfVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
29-322 |
1.75e-32 |
|
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: 126.51 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 29 LLGFVSGILIIAQAWFMARILQHMIMENIP---REALLLPFTLLVLTFVLRAWVVWLRERVGYHAGQHIRFAIRRQVLDR 105
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPagdLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 106 LQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFMALVGM 185
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 186 GAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVA 265
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 266 VYFGFSYL-GELDFGhydtgvTLAAgFLALIlaPEFFQPLRDLGTFYHAKAQAVGAAD 322
Cdd:cd07346 242 LYGGYLVLqGSLTIG------ELVA-FLAYL--GMLFGPIQRLANLYNQLQQALASLE 290
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
369-587 |
4.41e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 127.52 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALS-GFLSYQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLAR 447
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQrHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 PDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEA 527
Cdd:PRK10789 414 PDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 528 LNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLLAHRQEE 587
Cdd:PRK10789 494 LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLE 553
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
316-565 |
6.00e-31 |
|
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: 127.17 E-value: 6.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 316 QAVGAADSLKTFMETPLAHPQRgeaeLALTDPL-TIEAEDLFITSPEGK--TLAGpLNFTLPAGQRAVLVGRSGSGKSSL 392
Cdd:COG4618 300 SARQAYRRLNELLAAVPAEPER----MPLPRPKgRLSVENLTVVPPGSKrpILRG-VSFSLEPGEVLGVIGPSGSGKSTL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 393 LNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVllAR-PDASEQELQAALDNAWVSEFLPL 470
Cdd:COG4618 375 ARLLVGVWPpTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 471 LPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTT-LMVTHQLEDLAE 549
Cdd:COG4618 453 LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATvVVITHRPSLLAA 532
|
250
....*....|....*.
gi 446966322 550 WDVIWVMQDGRIIEQG 565
Cdd:COG4618 533 VDKLLVLRDGRVQAFG 548
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
350-561 |
1.19e-30 |
|
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: 119.13 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKT----LAGPlNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSPESW--- 421
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqaLKGV-SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVDGTDISKLSEKELaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 422 -RKHLSWVGQNPQL-PAATLRDNVLLA------RPDASEQELQAALDNAWVSEFLPLLPqgvdtpvgdqaARLSVGQAQR 493
Cdd:cd03255 80 rRRHIGFVFQSFNLlPDLTALENVELPlllagvPKKERRERAEELLERVGLGDRLNHYP-----------SELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446966322 494 VAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALN--AASLRQTTLMVTHQlEDLAEW-DVIWVMQDGRI 561
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHD-PELAEYaDRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
350-570 |
2.49e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 116.68 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFItSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWV 428
Cdd:COG1120 2 LEAENLSV-GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 429 GQNPQLPAA-TLRDNVLLAR---------PDASEQEL-QAALDNAWVSEFLpllpqgvDTPVGdqaaRLSVGQAQRVAVA 497
Cdd:COG1120 81 PQEPPAPFGlTVRELVALGRyphlglfgrPSAEDREAvEEALERTGLEHLA-------DRPVD----ELSGGERQRVLIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 498 RALLNPCSLLLLDEPAASLDAHSEQRVMEALN--AASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRrlARERGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
369-560 |
3.32e-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: 114.87 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSPESWRKHLSWVGQNP--QLPAATLRDNVLL 445
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQFFGPTVEEEVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 446 ARPDA--SEQELQAALDNAWvsEFLPLLPQgVDTPVgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQR 523
Cdd:cd03225 100 GLENLglPEEEIEERVEEAL--ELVGLEGL-RDRSP----FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRE 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 446966322 524 VMEALNA-ASLRQTTLMVTHQLEDLAEW-DVIWVMQDGR 560
Cdd:cd03225 173 LLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
350-570 |
1.45e-28 |
|
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: 119.62 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL----SYQGSLRINGIELRDLSPESWRKH 424
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAvDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 425 LSWVGQNP--QLPAATLRDNVL--LARPDASEQELQAAldnawVSEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARAL 500
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDQIAeaLENLGLSRAEARAR-----VLELLEAV--GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446966322 501 LNPCSLLLLDEPAASLDAHSEQRVMEALN--AASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEI 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
369-560 |
4.90e-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: 111.41 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGielrdlspeswrkHLSWVGQNPQLPAATLRDNVLLAR 447
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEkLSGSVSVPG-------------SIAYVSQEPWIQNGTIRENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 P-DasEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVME 526
Cdd:cd03250 91 PfD--EERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFE 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 446966322 527 A--LNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGR 560
Cdd:cd03250 169 NciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
362-560 |
1.76e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 108.49 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 362 GKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSPESWRKHLSWVGQnpqlpaatlr 440
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 441 dnvllarpdaseqelqaaldnawvseflpllpqgvdtpvgdqaarLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHS 520
Cdd:cd00267 81 ---------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446966322 521 EQRVMEALNAASLRQTT-LMVTHQLEDLAEW-DVIWVMQDGR 560
Cdd:cd00267 116 RERLLELLRELAEEGRTvIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
350-557 |
3.65e-26 |
|
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: 106.02 E-value: 3.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFItSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDlSPESWRKHLSWV 428
Cdd:COG4133 3 LEAENLSC-RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 429 GQNPQLPAA-TLRDNVLLAR----PDASEQELQAALdnawvsEFLPLLPQGvDTPVGdqaaRLSVGQAQRVAVARALLNP 503
Cdd:COG4133 81 GHADGLKPElTVRENLRFWAalygLRADREAIDEAL------EAVGLAGLA-DLPVR----QLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 504 CSLLLLDEPAASLDAHSEQRVMEALNA-ASLRQTTLMVTHQLEDLAEWDVIWVMQ 557
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
350-561 |
5.52e-26 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 104.61 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGK--TLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLS 426
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRN-VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 427 WVGQNPQLPAATLRDNVLlarpdaseqelqaaldnawvseflpllpqgvdtpvgdqaarlSVGQAQRVAVARALLNPCSL 506
Cdd:cd03246 80 YLPQDDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 507 LLLDEPAASLDAHSEQRVMEALNAASLRQTT-LMVTHQLEDLAEWDVIWVMQDGRI 561
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATrIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
350-565 |
1.37e-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: 105.28 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGK---TLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPE---SWR 422
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGKDLLKLSRRlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 423 KHLSWVGQNPQL---PAATLRDNV----LLARPDASEQELQAALDNAWV-----SEFLPLLPqgvdtpvgdqaARLSVGQ 490
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQIaeplRIHGKLSKKEARKEAVLLLLVgvglpEEVLNRYP-----------HELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 491 AQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEAL-NAASLRQTT-LMVTHQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLkKLQEELGLTlLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
362-565 |
4.22e-25 |
|
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: 103.37 E-value: 4.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 362 GKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPEswRKHLSWVGQNPQL-PAATL 439
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALfPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 440 RDNVL--LARPDASEQELQAAldnawVSEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:cd03259 90 AENIAfgLKLRGVPKAEIRAR-----VRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446966322 518 AHSEQRVMEALNA--ASLRQTTLMVTHQLED-LAEWDVIWVMQDGRIIEQG 565
Cdd:cd03259 163 AKLREELREELKElqRELGITTIYVTHDQEEaLALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
350-570 |
7.86e-25 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 103.73 E-value: 7.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDL---FITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHL 425
Cdd:COG1124 2 LEVRNLsvsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERpWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 426 SWVGQNPQL---PAATLRDnvLLARP------DASEQELQAALDNawV---SEFLPLLPqgvdtpvgdqaARLSVGQAQR 493
Cdd:COG1124 82 QMVFQDPYAslhPRHTVDR--ILAEPlrihglPDREERIAELLEQ--VglpPSFLDRYP-----------HQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 494 VAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAasLRQ----TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYA 568
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKD--LREerglTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVA 224
|
..
gi 446966322 569 EL 570
Cdd:COG1124 225 DL 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
350-565 |
1.44e-24 |
|
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: 100.85 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSpESWRKHLSW 427
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLkPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 428 VGQNPQLPAATLRDNVllarpdaseqelqaaldnawvseflpllpqgvdtpvgdqAARLSVGQAQRVAVARALLNPCSLL 507
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 508 LLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
351-565 |
1.73e-24 |
|
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: 100.59 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 351 EAEDLFItSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWVG 429
Cdd:cd03214 1 EVENLSV-GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 430 QnpqlpaatlrdnvLLARPDASEqelqaaldnawvseflpLLPQGVDTpvgdqaarLSVGQAQRVAVARALLNPCSLLLL 509
Cdd:cd03214 80 Q-------------ALELLGLAH-----------------LADRPFNE--------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 510 DEPAASLDAHSEQRVMEALN--AASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRrlARERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
350-563 |
1.89e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.86 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDL---FITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPEswrkhL 425
Cdd:COG1116 8 LELRGVskrFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKpTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 426 SWVGQNPQL-PAATLRDNVLLA------RPDASEQELQAALD--------NAWVSEflpllpqgvdtpvgdqaarLSVGQ 490
Cdd:COG1116 83 GVVFQEPALlPWLTVLDNVALGlelrgvPKAERRERARELLElvglagfeDAYPHQ-------------------LSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 491 AQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNA--ASLRQTTLMVTHQLED---LAewDVIWVMQD--GRIIE 563
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHDVDEavfLA--DRVVVLSArpGRIVE 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
209-581 |
3.41e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 108.14 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 209 LRGMETLRIFgrgeAEIESIRSASEDFRQRTMEVLRLAFLSSGILEF-FTSLSIALVAVYFG-FSYLGeldfghydTGVT 286
Cdd:PLN03232 486 LASMDTVKCY----AWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFiLNSIPVVVTLVSFGvFVLLG--------GDLT 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 287 LAAGFLALILapefFQPLR-DLGTFYHAKAQAVGAADSLKTFMETPLAHpqrgEAELALTDPL-------TIEAEDLFIT 358
Cdd:PLN03232 554 PARAFTSLSL----FAVLRsPLNMLPNLLSQVVNANVSLQRIEELLLSE----ERILAQNPPLqpgapaiSIKNGYFSWD 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 359 SPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQgslringielrDLSPESWRKHLSWVGQNPQLPAAT 438
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA-----------ETSSVVIRGSVAYVPQVSWIFNAT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 439 LRDNVLLARPDASEQELQAaLDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDA 518
Cdd:PLN03232 695 VRENILFGSDFESERYWRA-IDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446966322 519 HSEQRVMEALNAASLR-QTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLL 581
Cdd:PLN03232 774 HVAHQVFDSCMKDELKgKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
227-588 |
4.29e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 107.90 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 227 SIRSASEDFRQRTMEVLRLAFLSSGILEF-FTSLSIALVAVYFG-FSYLGeldfghydTGVTLAAGFLALILapefFQPL 304
Cdd:PLN03130 500 SFQSKVQTVRDDELSWFRKAQLLSAFNSFiLNSIPVLVTVVSFGvFTLLG--------GDLTPARAFTSLSL----FAVL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 305 R-DLGTFYHAKAQAVGAADSLKTFMETPLAHpqrgeaELALTDPLTIEAEDLFITSPEG----------KTLAGpLNFTL 373
Cdd:PLN03130 568 RfPLFMLPNLITQAVNANVSLKRLEELLLAE------ERVLLPNPPLEPGLPAISIKNGyfswdskaerPTLSN-INLDV 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 374 PAGQRAVLVGRSGSGKSSLLNALSGflsyqgslringiELRDLSPESW--RKHLSWVGQNPQLPAATLRDNVLLARP-DA 450
Cdd:PLN03130 641 PVGSLVAIVGSTGEGKTSLISAMLG-------------ELPPRSDASVviRGTVAYVPQVSWIFNATVRDNILFGSPfDP 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 451 SEQElqAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNA 530
Cdd:PLN03130 708 ERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK 785
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446966322 531 ASLRQTT-LMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLL--AHRQEEI 588
Cdd:PLN03130 786 DELRGKTrVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMenAGKMEEY 846
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
370-570 |
8.37e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.21 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPEswRKHLSWVGQNPQL-PAATLRDNVLLA- 446
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPpDSGRILWNGQDLTALPPA--ERPVSMLFQENNLfPHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 ----RPDASEQE-LQAALDNAWVSEFLPLLPqgvdtpvgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSE 521
Cdd:COG3840 97 rpglKLTAEQRAqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446966322 522 QRVMEALN--AASLRQTTLMVTHQLED---LAEWdVIWVmQDGRIIEQGRYAEL 570
Cdd:COG3840 166 QEMLDLVDelCRERGLTVLMVTHDPEDaarIADR-VLLV-ADGRIAADGPTAAL 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
364-581 |
3.51e-23 |
|
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: 105.03 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 364 TLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGielrdlspeswrkHLSWVGQNPQLPAATLRDN 442
Cdd:TIGR00957 653 TLNG-ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDkVEGHVHMKG-------------SVAYVPQQAWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 443 VLLARPdASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQ 522
Cdd:TIGR00957 719 ILFGKA-LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446966322 523 RVMEAL---NAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLL 581
Cdd:TIGR00957 798 HIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
350-570 |
4.55e-23 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 98.41 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSPE---SWRKHL 425
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVePTSGSVLIDGTDINKLKGKalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 426 SWVGQNPQL-PAATLRDNVLLARPDA-----------SEQELQAALDnawvseflpLLPQ-GVDTPVGDQAARLSVGQAQ 492
Cdd:cd03256 81 GMIFQQFNLiERLSVLENVLSGRLGRrstwrslfglfPKEEKQRALA---------ALERvGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 493 RVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEAL--NAASLRQTTLMVTHQLeDLAE--WDVIWVMQDGRIIEQGRYA 568
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQV-DLAReyADRIVGLKDGRIVFDGPPA 230
|
..
gi 446966322 569 EL 570
Cdd:cd03256 231 EL 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
350-565 |
5.54e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.93 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSG-FLSYQGSLRINGIELrdlSPES-W--RKH 424
Cdd:PRK13635 6 IRVEHISFRYPDAATYAlKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlLLPEAGTITVGGMVL---SEETvWdvRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 425 LSWVGQNP--QLPAATLRDNVLLA-------RPDASEQeLQAALDNAWVSEFLPLLPqgvdtpvgdqaARLSVGQAQRVA 495
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGlenigvpREEMVER-VDQALRQVGMEDFLNREP-----------HRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446966322 496 VARALLNPCSLLLLDEPAASLDAHSEQRVMEALN--AASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
369-570 |
6.18e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.83 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPEsWRKHLSWVGQNPQL-PAATLRDNVLLA 446
Cdd:COG1131 19 VSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRpTSGEVRVLGEDVARDPAE-VRRRIGYVPQEPALyPDLTVRENLRFF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 RP--DASEQELQAALDnaWVSEFLPLLPQGvDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRV 524
Cdd:COG1131 98 ARlyGLPRKEARERID--ELLELFGLTDAA-DRKVGT----LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARREL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446966322 525 MEALNAASLRQTT-LMVTHQLEDLAE-WDVIWVMQDGRIIEQGRYAEL 570
Cdd:COG1131 171 WELLRELAAEGKTvLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDEL 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
350-565 |
7.60e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.65 E-value: 7.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEG-KTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSG-FLSYQGSLRINGIELRDlSPESW-RKHLS 426
Cdd:PRK13647 5 IEVEDLHFRYKDGtKALKG-LSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGRVKVMGREVNA-ENEKWvRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 427 WVGQNP--QLPAATLRDNVLLA------RPDASEQELQAALDNAWVSEFLPLLPQgvdtpvgdqaaRLSVGQAQRVAVAR 498
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 499 ALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMV-THQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVaTHDVDLAAEWaDQVIVLKEGRVLAEG 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
369-559 |
2.92e-22 |
|
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: 95.48 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSPESW----RKHLSWVGQNPQLPAATLRDNV 443
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMqTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LLARPdASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQR 523
Cdd:cd03290 100 TFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 446966322 524 VMEALNAASLR---QTTLMVTHQLEDLAEWDVIWVMQDG 559
Cdd:cd03290 179 LMQEGILKFLQddkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
350-564 |
7.86e-22 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 94.08 E-value: 7.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDL---FITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPeswrkHL 425
Cdd:cd03293 1 LEVRNVsktYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 426 SWVGQNPQL-PAATLRDNVLLA-----RPDASEQEL-QAALDNAWVSEFLPLLPqgvdtpvgdqaARLSVGQAQRVAVAR 498
Cdd:cd03293 76 GYVFQQDALlPWLTVLDNVALGlelqgVPKAEARERaEELLELVGLSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446966322 499 ALLNPCSLLLLDEPAASLDAHSEQRVMEALNA--ASLRQTTLMVTHQLED---LAewDVIWVM--QDGRIIEQ 564
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEavfLA--DRVVVLsaRPGRIVAE 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-570 |
1.24e-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: 98.44 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 333 AHPQRGEAELALTDPLtIEAEDL---FITSPEGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLR 407
Cdd:COG1123 245 AARGRAAPAAAAAEPL-LEVRNLskrYPVRGKGGVRAvDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRpTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 408 INGIELRDLSPESWRKHLSWVG---QNP--QL-PAATLRDNV---LLARPDASEQELQAAldnawVSEFLPLlpqgvdtp 478
Cdd:COG1123 324 FDGKDLTKLSRRSLRELRRRVQmvfQDPysSLnPRMTVGDIIaepLRLHGLLSRAERRER-----VAELLER-------- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 479 VG---DQAAR----LSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALnaASLRQ----TTLMVTHQLEDL 547
Cdd:COG1123 391 VGlppDLADRypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLL--RDLQRelglTYLFISHDLAVV 468
|
250 260
....*....|....*....|....
gi 446966322 548 AEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:COG1123 469 RYIaDRVAVMYDGRIVEDGPTEEV 492
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
370-570 |
1.68e-21 |
|
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: 96.32 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRD------LSPEswRKHLSWVGQNPQL-PAATLRD 441
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERpDSGRIRLGGEVLQDsargifLPPH--RRRIGYVFQEARLfPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 442 NVLLARPDASEQELQAALDNawVSEFL---PLLPQGVdtpvgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDA 518
Cdd:COG4148 97 NLLYGRKRAPRAERRISFDE--VVELLgigHLLDRRP--------ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 519 HSEQRVMEALnaASLRQTT----LMVTHQLED---LAewDVIWVMQDGRIIEQGRYAEL 570
Cdd:COG4148 167 ARKAEILPYL--ERLRDELdipiLYVSHSLDEvarLA--DHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
369-565 |
2.11e-21 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 92.74 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPaGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRD------LSPEswRKHLSWVGQNPQL-PAATLR 440
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKpDGGTIVLNGTVLFDsrkkinLPPQ--QRKIGLVFQQYALfPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 441 DNVLLARPDASEQELQAAldnawVSEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHS 520
Cdd:cd03297 94 ENLAFGLKRKRNREDRIS-----VDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446966322 521 EQRVMEALN--AASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:cd03297 167 RLQLLPELKqiKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
350-565 |
2.24e-21 |
|
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: 93.01 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQGSLRING--------IELRDLSPESW 421
Cdd:cd03260 1 IELRDLNVYYGDKHALKD-ISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGevlldgkdIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 422 RKHLSWVGQNPQLPAATLRDNVLLA-------RPDASEQELQAALDNAWvseflplLPQGVDTPVGdqAARLSVGQAQRV 494
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAA-------LWDEVKDRLH--ALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446966322 495 AVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTH---QLEDLAewDVIWVMQDGRIIEQG 565
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqQAARVA--DRTAFLLNGRLVEFG 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
345-566 |
2.33e-21 |
|
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: 93.27 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 345 TDPLtIEAEDLFITSPEGktlAGPL------NFTLPAGQRAVLVGRSGSGKSSLLNALSGF-LSYQGSLRINGIELRDLS 417
Cdd:COG4181 5 SAPI-IELRGLTKTVGTG---AGELtilkgiSLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 418 PESW----RKHLSWVGQNPQL-PAATLRDNVLL-----ARPDAsEQELQAALDNAWVSEFLPLLPqgvdtpvgdqaARLS 487
Cdd:COG4181 81 EDARarlrARHVGFVFQSFQLlPTLTALENVMLplelaGRRDA-RARARALLERVGLGHRLDHYP-----------AQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 488 VGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVME---ALNAAslRQTTL-MVTHQLEDLAEWDVIWVMQDGRIIE 563
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDllfELNRE--RGTTLvLVTHDPALAARCDRVLRLRAGRLVE 226
|
...
gi 446966322 564 QGR 566
Cdd:COG4181 227 DTA 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
350-570 |
2.98e-21 |
|
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: 93.13 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLL---NALsgFLSYQGSLRINGIELRDLSPESWRKHLS 426
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMkmiNRL--IEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 427 WVGQNPQL-PAATLRDNV-----LLARPDASEQELqaaldnawVSEFLPLlpqgVDTPVGDQAAR----LSVGQAQRVAV 496
Cdd:cd03295 79 YVIQQIGLfPHMTVEENIalvpkLLKWPKEKIRER--------ADELLAL----VGLDPAEFADRypheLSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 497 ARALLNPCSLLLLDEPAASLDA---HSEQRVMEALNAAsLRQTTLMVTHQLED---LAewDVIWVMQDGRIIEQGRYAEL 570
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPitrDQLQEEFKRLQQE-LGKTIVFVTHDIDEafrLA--DRIAIMKNGEIVQVGTPDEI 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
243-543 |
5.47e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.80 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 243 LRLAFLSSGILEFFTSLSIALVAVYFgFSylGELDFGhydtGVTLAAG-FLALILAPEFF-QPLRDLGTFyhakaQAVga 320
Cdd:COG4178 266 RNLTFFTTGYGQLAVIFPILVAAPRY-FA--GEITLG----GLMQAASaFGQVQGALSWFvDNYQSLAEW-----RAT-- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 321 ADSLKTFME--TPLAHPQRGEAELALTDPLTIEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSG 398
Cdd:COG4178 332 VDRLAGFEEalEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 399 FLSY-QGSLRIngielrdlsPESWRkhLSWVGQNPQLPAATLRDnvLLARPDA----SEQELQAALDNAwvseFLPLLPQ 473
Cdd:COG4178 412 LWPYgSGRIAR---------PAGAR--VLFLPQRPYLPLGTLRE--ALLYPATaeafSDAELREALEAV----GLGHLAE 474
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446966322 474 GVDTpVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAAsLRQTTLM-VTHQ 543
Cdd:COG4178 475 RLDE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE-LPGTTVIsVGHR 543
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
369-561 |
1.05e-20 |
|
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: 89.38 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDlSPESWRKHLSWVGQNPQLPAA-TLRDNVlla 446
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTVRENL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 rpdaseqelqaaldnawvseflpllpqgvdtpvgdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVME 526
Cdd:cd03230 95 --------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 446966322 527 ALNAASLRQTT-LMVTHQLEDLAEW-DVIWVMQDGRI 561
Cdd:cd03230 137 LLRELKKEGKTiLLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
351-562 |
1.41e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 90.01 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 351 EAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGielRDLSPESWRKHLSWVG 429
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 430 QNP--QLPAATLRDNVLLARPDASEQELQAA--LDNAWVSEFLPLLPQGvdtpvgdqaarLSVGQAQRVAVARALLNPCS 505
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGNEQAEtvLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 506 LLLLDEPAASLDAHSEQRVMEALNAASLRQTT-LMVTHQLEDLAEW-DVIWVMQDGRII 562
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAvIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
351-569 |
1.69e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 96.39 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 351 EAEDLFITSPegKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQgslringielrdlSPESW-RKHLSWVG 429
Cdd:PTZ00243 663 KTDDFFELEP--KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS-------------EGRVWaERSIAYVP 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 430 QNPQLPAATLRDNVLLARPDaSEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLL 509
Cdd:PTZ00243 728 QQAWIMNATVRGNILFFDEE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446966322 510 DEPAASLDAHSEQRVMEALNAASLR-QTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAE 569
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEECFLGALAgKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD 867
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
369-570 |
1.92e-20 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 90.33 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSPES---WRKHLSWVGQNPQLPAA-TLRDNV 443
Cdd:cd03258 24 VSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPtSGSVLVDGTDLTLLSGKElrkARRRIGMIFQHFNLLSSrTVFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LL----ARPDASEQELQaaldnawVSEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAH 519
Cdd:cd03258 104 ALpleiAGVPKAEIEER-------VLELLELV--GLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 520 SEQRVMEAL---NaASLRQTTLMVTHQLE---DLAewDVIWVMQDGRIIEQGRYAEL 570
Cdd:cd03258 175 TTQSILALLrdiN-RELGLTIVLITHEMEvvkRIC--DRVAVMEKGEVVEEGTVEEV 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
369-585 |
1.93e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 93.25 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRD------LSPEswRKHLSWVGQNPQL-PAATLR 440
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRpDEGEIVLNGRTLFDsrkgifLPPE--KRRIGYVFQEARLfPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 441 DNVLLARPDASEQELQAALDNawVSEFLpllpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHS 520
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISFER--VIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 521 EQRVMEALN--AASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAElsVAGGPFATLLAHRQ 585
Cdd:TIGR02142 167 KYEILPYLErlHAEFGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAE--VWASPDLPWLARED 232
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
335-566 |
2.40e-20 |
|
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: 89.39 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 335 PQRGEaelaltdpltIEAEDLFIT-SPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIE 412
Cdd:cd03369 2 PEHGE----------IEVENLSVRyAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAeEGKIEIDGID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 413 LRDLSPESWRKHLSWVGQNPQLPAATLRDNvlLARPDA-SEQELQAALDnawVSEflpllpqgvdtpvgdQAARLSVGQA 491
Cdd:cd03369 72 ISTIPLEDLRSSLTIIPQDPTLFSGTIRSN--LDPFDEySDEEIYGALR---VSE---------------GGLNLSQGQR 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 492 QRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGR 566
Cdd:cd03369 132 QLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
350-542 |
3.90e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 89.00 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGF-LSYQGSLRINGIELRDLSPES---WRKHL 425
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 426 SWVGQNPQL-PAATLRDNVLLARP--DASEQELQAAldnawVSEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLN 502
Cdd:cd03292 81 GVVFQDFRLlPDRNVYENVAFALEvtGVPPREIRKR-----VPAALELV--GLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446966322 503 PCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTT-LMVTH 542
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTvVVATH 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
368-565 |
9.97e-20 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 87.93 E-value: 9.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 368 PLNF--TLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPEswRKHLSWVGQ-NPQLPAATLRDNV 443
Cdd:cd03298 14 PMHFdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLINGVDVTAAPPA--DRPVSMLFQeNNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LLARP------DASEQELQAALDNAWVSEFLPLLPQgvdtpvgdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:cd03298 92 GLGLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446966322 518 AHSEQRvMEALNAASLRQ---TTLMVTHQLEDLAE-WDVIWVMQDGRIIEQG 565
Cdd:cd03298 161 PALRAE-MLDLVLDLHAEtkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
376-581 |
1.08e-19 |
|
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: 88.81 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 376 GQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNvLLARPDASEQE 454
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN-LDPECKCTDDR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 455 LQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLR 534
Cdd:cd03288 126 LWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446966322 535 QTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAEL-SVAGGPFATLL 581
Cdd:cd03288 206 RTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLlAQEDGVFASLV 253
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
369-560 |
1.09e-19 |
|
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: 86.86 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPES--WRKHLSWVGQNPQL-PAATLRDNVL 444
Cdd:cd03229 19 VSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILIDGEDLTDLEDELppLRRRIGMVFQDFALfPHLTVLENIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 LArpdaseqelqaaldnawvseflpllpqgvdtpvgdqaarLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRV 524
Cdd:cd03229 99 LG---------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 446966322 525 MEALNA--ASLRQTTLMVTHQLEDLAEW-DVIWVMQDGR 560
Cdd:cd03229 140 RALLKSlqAQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
369-577 |
1.24e-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: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNvLLAR 447
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINeSAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN-LDPF 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 PDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEA 527
Cdd:TIGR00957 1384 SQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 1463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446966322 528 LNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPF 577
Cdd:TIGR00957 1464 IRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
369-545 |
1.65e-19 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 87.30 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIE---LRDLSPESWRKHLSWVGQNPQL-PAATLRDNV 443
Cdd:TIGR02673 21 VSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTpSRGQVRIAGEDvnrLRGRQLPLLRRRIGVVFQDFRLlPDRTVYENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LLA------RPDASEQELQAALDnaWVSeflplLPQGVDTPvgdqAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:TIGR02673 101 ALPlevrgkKEREIQRRVGAALR--QVG-----LEHKADAF----PEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLD 169
|
170 180
....*....|....*....|....*....
gi 446966322 518 AHSEQRVMEALNAASLRQTT-LMVTHQLE 545
Cdd:TIGR02673 170 PDLSERILDLLKRLNKRGTTvIVATHDLS 198
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
350-566 |
1.75e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.42 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKT-LAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPES---WRKH 424
Cdd:COG2884 2 IRFENVSKRYPGGREaLSD-VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERpTSGQVLVNGQDLSRLKRREipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 425 LSWVGQNPQL-PAATLRDNVLLA------RPDASEQELQAALDnaWV--SEFLPLLPqgvdtpvgdqaARLSVGQAQRVA 495
Cdd:COG2884 81 IGVVFQDFRLlPDRTVYENVALPlrvtgkSRKEIRRRVREVLD--LVglSDKAKALP-----------HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446966322 496 VARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTT-LMVTHQLE--DLAEWDVIwVMQDGRIIEQGR 566
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTvLIATHDLElvDRMPKRVL-ELEDGRLVRDEA 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
368-581 |
2.75e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 368 PLNFTL--PAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPEswRKHLSWVGQ-NPQLPAATLRDNV 443
Cdd:PRK10771 15 PMRFDLtvERGERVAILGPSGAGKSTLLNLIAGFLTpASGSLTLNGQDHTTTPPS--RRPVSMLFQeNNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LLA-----RPDASEQE-LQAALDNAWVSEFLPLLPqgvdtpvgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:PRK10771 93 GLGlnpglKLNAAQREkLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 518 AHSEQRVMEALN-AASLRQTT-LMVTHQLED---LAEWDViwVMQDGRIIEQGRYAELSVAGGPFATLL 581
Cdd:PRK10771 162 PALRQEMLTLVSqVCQERQLTlLMVSHSLEDaarIAPRSL--VVADGRIAWDGPTDELLSGKASASALL 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
130-549 |
4.09e-19 |
|
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: 91.90 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 130 IDDMhdyyaryLPQMALAVSVPLLIVV-AIFPSNWAAALILLGTAPLIPLFMALvgmgaadanRRNFL------------ 196
Cdd:TIGR01271 995 IDDM-------LPLTLFDFIQLTLIVLgAIFVVSVLQPYIFIAAIPVAVIFIML---------RAYFLrtsqqlkqlese 1058
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 197 ALARLSGHFLDRLRGMETLRIFGRgeaeiesiRSASEDFRQRTMEvLRLA--FLSSGILEFFtSLSIALVAVYF----GF 270
Cdd:TIGR01271 1059 ARSPIFSHLITSLKGLWTIRAFGR--------QSYFETLFHKALN-LHTAnwFLYLSTLRWF-QMRIDIIFVFFfiavTF 1128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 271 SYLGELDFGHYDTGVTLAagfLALILapeffqplrdLGTFYHAKAQAVgAADSL-----KTF----METPLAHPQRGEAE 341
Cdd:TIGR01271 1129 IAIGTNQDGEGEVGIILT---LAMNI----------LSTLQWAVNSSI-DVDGLmrsvsRVFkfidLPQEEPRPSGGGGK 1194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 342 LALTDPLTIE---------------AEDLFITSPE-GKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQGS 405
Cdd:TIGR01271 1195 YQLSTVLVIEnphaqkcwpsggqmdVQGLTAKYTEaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE 1274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 406 LRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNvLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAAR 485
Cdd:TIGR01271 1275 IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN-LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYV 1353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446966322 486 LSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAE 549
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLE 1417
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
73-321 |
5.81e-19 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 87.59 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 73 FVLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQmaLAVSVPL 152
Cdd:cd18778 50 YLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQ--GITNVLT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 153 LIVVAI--FPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRS 230
Cdd:cd18778 128 LVGVAIilFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 231 ASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVaVYFG--FSYLGELDFGhydtgvTLAAGFLALILapeFFQPLRDLG 308
Cdd:cd18778 208 LSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLV-LGFGgrLVLAGELTIG------DLVAFLLYLGL---FYEPITSLH 277
|
250
....*....|...
gi 446966322 309 TFYHAKAQAVGAA 321
Cdd:cd18778 278 GLNEMLQRALAGA 290
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
347-565 |
6.34e-19 |
|
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: 84.91 E-value: 6.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 347 PLTIEAEDLFITSPEG-----KTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY---QGSLRINGielRDLSP 418
Cdd:cd03213 1 GVTLSFRNLTVTVKSSpsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgvSGEVLING---RPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 419 ESWRKHLSWVGQNPQL-PAATLRDNVLLArpdaseqelqAALdnawvseflpllpQGvdtpvgdqaarLSVGQAQRVAVA 497
Cdd:cd03213 78 RSFRKIIGYVPQDDILhPTLTVRETLMFA----------AKL-------------RG-----------LSGGERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446966322 498 RALLNPCSLLLLDEPAASLDAHSEQRVMEALNA-ASLRQTTLMVTHQL--EDLAEWDVIWVMQDGRIIEQG 565
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
369-565 |
7.57e-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: 85.38 E-value: 7.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSPEswRKHLSWVGQNPQL-PAATLRDNVL-- 444
Cdd:cd03301 19 LNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYIGGRDVTDLPPK--DRDIAMVFQNYALyPHMTVYDNIAfg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 LARPDASEQELQAALDnaWVSEFLpllpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRV 524
Cdd:cd03301 97 LKLRKVPKDEIDERVR--EVAELL-----QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446966322 525 MEALNA--ASLRQTTLMVTH-QLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:cd03301 170 RAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
369-565 |
9.76e-19 |
|
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: 85.47 E-value: 9.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPEswRKHLSWVGQNPQL-PAATLRDNV--- 443
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKpDSGKILLNGKDITNLPPE--KRDISYVPQNYALfPHMTVYKNIayg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 ----LLARPDASEQELQaaldnawVSEFLpllpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAH 519
Cdd:cd03299 96 lkkrKVDKKEIERKVLE-------IAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446966322 520 SEQRVMEALNAA--SLRQTTLMVTHQLEDlAEW--DVIWVMQDGRIIEQG 565
Cdd:cd03299 164 TKEKLREELKKIrkEFGVTVLHVTHDFEE-AWAlaDKVAIMLNGKLIQVG 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
362-569 |
1.13e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.84 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 362 GKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL----SYQGSLRINGIELRDLSPEswRKHLSWVGQNPQL-PA 436
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLspafSASGEVLLNGRRLTALPAE--QRRIGILFQDDLLfPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 437 ATLRDNVLLARPD-----ASEQELQAALDNAWVSEFLPLLPqgvdtpvgdqaARLSVGQAQRVAVARALLNPCSLLLLDE 511
Cdd:COG4136 91 LSVGENLAFALPPtigraQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 512 PAASLDAHSEQRVME-ALNAASLRQT-TLMVTHQLEDlaewdviwVMQDGRIIEQGRYAE 569
Cdd:COG4136 160 PFSKLDAALRAQFREfVFEQIRQRGIpALLVTHDEED--------APAAGRVLDLGNWQH 211
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
362-561 |
1.30e-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: 86.06 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 362 GKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRD 441
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 442 NvLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSE 521
Cdd:cd03289 96 N-LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446966322 522 QRVMEALNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRI 561
Cdd:cd03289 175 QVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
350-570 |
1.62e-18 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 85.04 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSPE---SWRKHL 425
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVePSSGSILLEGTDITKLRGKklrKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 426 SWVGQNPQL-PAATLRDNVLLARPDA-----------SEQELQAALDNawvseflpLLPQGVDTPVGDQAARLSVGQAQR 493
Cdd:TIGR02315 82 GMIFQHYNLiERLTVLENVLHGRLGYkptwrsllgrfSEEDKERALSA--------LERVGLADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 494 VAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALN--AASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKriNKEDGITVIINLHQVDLAKKYaDRIVGLKAGEIVFDGAPSEL 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
370-565 |
2.96e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 84.28 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELrDLSPESWRKHLSWVG---QNPQL-PAATLRDNVL 444
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTITVDGEDL-TDSKKDINKLRRKVGmvfQQFNLfPHLTVLENVT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 LA--------RPDASEQelqaALDnawvseflpLLPQgvdtpVG--DQA----ARLSVGQAQRVAVARALLNPCSLLLLD 510
Cdd:COG1126 100 LApikvkkmsKAEAEER----AME---------LLER-----VGlaDKAdaypAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446966322 511 EPAASLDAhsE-----QRVMEALnaASLRQTTLMVTHQLE---DLAewDVIWVMQDGRIIEQG 565
Cdd:COG1126 162 EPTSALDP--ElvgevLDVMRDL--AKEGMTMVVVTHEMGfarEVA--DRVVFMDGGRIVEEG 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
369-570 |
4.66e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.92 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPEswRKHLSWVGQNPQL-PAATLRDNV--- 443
Cdd:COG3842 24 VSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETpDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALfPHLTVAENVafg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 L-LARPDASEQElqaaldnAWVSEFLPLlpqgvdtpVG--DQAAR----LSVGQAQRVAVARAllnpcsllllDEPAASL 516
Cdd:COG3842 102 LrMRGVPKAEIR-------ARVAELLEL--------VGleGLADRyphqLSGGQQQRVALARAlapeprvlllDEPLSAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 517 DAHSEQRVMEALnAASLRQ---TTLMVTHQLED---LAewDVIWVMQDGRIIEQGRYAEL 570
Cdd:COG3842 167 DAKLREEMREEL-RRLQRElgiTFIYVTHDQEEalaLA--DRIAVMNDGRIEQVGTPEEI 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
361-570 |
6.40e-18 |
|
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: 83.60 E-value: 6.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 361 EGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL--SYQGSLRINGIELRDLSPESWRKHLSWVgqNPQL---- 434
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLppTYGNDVRLFGERRGGEDVWELRKRIGLV--SPALqlrf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 435 -PAATLRDNVLLAR-------PDASEQELQAALDnaWVSEFlpllpqGV----DTPVGdqaaRLSVGQAQRVAVARALLN 502
Cdd:COG1119 92 pRDETVLDVVLSGFfdsiglyREPTDEQRERARE--LLELL------GLahlaDRPFG----TLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446966322 503 PCSLLLLDEPAASLDAHSEQRVMEALN--AASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDklAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEV 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
369-549 |
6.52e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 83.21 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGielrdLSPESWRKHLSWVGQ----NPQLPAaTLRDNV 443
Cdd:COG1121 25 VSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFG-----KPPRRARRRIGYVPQraevDWDFPI-TVRDVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 ---------LLARPDASEQEL-QAALDNAWVSEFLpllpqgvDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLDEPA 513
Cdd:COG1121 99 lmgrygrrgLFRRPSRADREAvDEALERVGLEDLA-------DRPIGE----LSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 446966322 514 ASLDAHSEQRVMEALnaASLRQ---TTLMVTHQLEDLAE 549
Cdd:COG1121 168 AGVDAATEEALYELL--RELRRegkTILVVTHDLGAVRE 204
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
368-570 |
6.66e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 85.51 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 368 PLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSPEswRKHLSWVGQNPQL-PAATLRDNVL- 444
Cdd:COG3839 21 DIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPtSGEILIGGRDVTDLPPK--DRNIAMVFQSYALyPHMTVYENIAf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 ---LARPDASEQE---LQAA--LDnawVSEFLPLLPqgvdtpvgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPAASL 516
Cdd:COG3839 99 plkLRKVPKAEIDrrvREAAelLG---LEDLLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 517 DAHSeqRV-MEA----LNAAsLRQTTLMVTH-QLEDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:COG3839 165 DAKL--RVeMRAeikrLHRR-LGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
369-545 |
7.28e-18 |
|
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: 82.58 E-value: 7.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLspeswRKHLSWVGQ----NPQLPAaTLRDNV 443
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGKPLEKE-----RKRIGYVPQrrsiDRDFPI-SVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LLAR----------PDASEQELQAALDNAWVSEFLpllpqgvDTPVGdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPA 513
Cdd:cd03235 92 LMGLyghkglfrrlSKADKAKVDEALERVGLSELA-------DRQIG----ELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190
....*....|....*....|....*....|....*
gi 446966322 514 ASLDAHSEQRVMEALNaaSLRQ---TTLMVTHQLE 545
Cdd:cd03235 161 AGVDPKTQEDIYELLR--ELRRegmTILVVTHDLG 193
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
90-307 |
8.69e-18 |
|
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: 83.98 E-value: 8.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 90 AGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLV---LEQIDDMhdyYARYLPQMALAVSVPLLIVVAIFPSNWAAA 166
Cdd:cd18544 68 LGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVtndTEALNEL---FTSGLVTLIGDLLLLIGILIAMFLLNWRLA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 167 LILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLA 246
Cdd:cd18544 145 LISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLF 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446966322 247 FLSSGILEFFTSLSIALVAVYFGFSYL-GELDFGhydtgvTLAAgFLALILapEFFQPLRDL 307
Cdd:cd18544 225 ALFRPLVELLSSLALALVLWYGGGQVLsGAVTLG------VLYA-FIQYIQ--RFFRPIRDL 277
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
369-570 |
1.01e-17 |
|
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: 82.10 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSPES-WRKHLSWVGQNPQL-PAATLRDNVLL 445
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIfPELTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 446 ARPDASEQELQAALDnaWVSEFLPLLPQGVDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVM 525
Cdd:cd03224 99 GAYARRRAKRKARLE--RVYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446966322 526 EALNA-ASLRQTTLMVTHQLE---DLAewDVIWVMQDGRIIEQGRYAEL 570
Cdd:cd03224 173 EAIRElRDEGVTILLVEQNARfalEIA--DRAYVLERGRVVLEGTAAEL 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
369-562 |
1.77e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.44 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSG-FLSYQGSLRINGIELRDLSPESWRKHLSWVGQNPQL---PAATLRDNVL 444
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGsLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSMTIEENLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 LA------RPdaseqeLQAALDNAWVSEF---LPLLPQG----VDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLDE 511
Cdd:COG1101 105 LAyrrgkrRG------LRRGLTKKRRELFrelLATLGLGlenrLDTKVGL----LSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446966322 512 PAASLDAHSEQRVMEALN--AASLRQTTLMVTHQLED-LAEWDVIWVMQDGRII 562
Cdd:COG1101 175 HTAALDPKTAALVLELTEkiVEENNLTTLMVTHNMEQaLDYGNRLIMMHEGRII 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
369-570 |
4.09e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 85.41 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNvLLAR 447
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFN-IDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 PDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEA 527
Cdd:PLN03232 1334 SEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446966322 528 LNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:PLN03232 1414 IREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
370-570 |
5.89e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.60 E-value: 5.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRI------NGIELRDLSPesWRKHLSWVGQNP--QLPAATLR 440
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVTIgervitAGKKNKKLKP--LRKKVGIVFQFPehQLFEETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 441 DNVLLARPD--ASEQElqaALDNAwvSEFLPLLpqGVDTPVGDQAA-RLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:PRK13634 105 KDICFGPMNfgVSEED---AKQKA--REMIELV--GLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 518 AHSEQRVMEALnaASLRQ----TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK13634 178 PKGRKEMMEMF--YKLHKekglTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
369-569 |
6.87e-17 |
|
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: 80.17 E-value: 6.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSP-ESWRKHLSWVGQNPQL-PAATLRDNVLL 445
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRpTSGSVLFDGEDITGLPPhEIARLGIGRTFQIPRLfPELTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 446 A---------RPDASEQELQAALDNAW-VSEFLPLLPQGvDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLDEPAAS 515
Cdd:cd03219 99 AaqartgsglLLARARREEREARERAEeLLERVGLADLA-DRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 516 LDAHSEQRVMEALNAASLRQTT-LMVTHQLE---DLAewDVIWVMQDGRIIEQGRYAE 569
Cdd:cd03219 174 LNPEETEELAELIRELRERGITvLLVEHDMDvvmSLA--DRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
350-570 |
7.57e-17 |
|
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: 80.24 E-value: 7.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPE---SWRKHL 425
Cdd:cd03261 1 IELRGLTKSFGGRTVLKG-VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDISGLSEAelyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 426 SWVGQNPQL-PAATLRDNV---LLARPDASEQELQAAldnawVSEFLPL--LPQGVDT-PvgdqaARLSVGQAQRVAVAR 498
Cdd:cd03261 80 GMLFQSGALfDSLTVFENVafpLREHTRLSEEEIREI-----VLEKLEAvgLRGAEDLyP-----AELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 499 ALLNPCSLLLLDEPAASLD---AHSEQRVMEALNAAsLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKE-LGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
369-561 |
8.24e-17 |
|
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: 79.50 E-value: 8.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELrDLSPESW---RKHLSWVGQNPQL-PAATLRDNV 443
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTIIIDGLKL-TDDKKNInelRQKVGMVFQQFNLfPHLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LLA------RPDASEQELqaALDnawvseflpLLPQgvdtpVG--DQA----ARLSVGQAQRVAVARALLNPCSLLLLDE 511
Cdd:cd03262 98 TLApikvkgMSKAEAEER--ALE---------LLEK-----VGlaDKAdaypAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 512 PAASLD---AHSEQRVMEALnaASLRQTTLMVTHQL---EDLAewDVIWVMQDGRI 561
Cdd:cd03262 162 PTSALDpelVGEVLDVMKDL--AEEGMTMVVVTHEMgfaREVA--DRVIFMDDGRI 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
349-569 |
1.30e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.82 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 349 TIEAEDLFItSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSW 427
Cdd:PRK13548 2 MLEARNLSV-RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSpDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 428 VGQNPQLPAA-TLRDNVLLAR------PDASEQELQAALDNAWVSEFlpllpqgvdtpvgdqAAR----LSVGQAQRVAV 496
Cdd:PRK13548 81 LPQHSSLSFPfTVEEVVAMGRaphglsRAEDDALVAAALAQVDLAHL---------------AGRdypqLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 497 ARALLNPCSLLLL------DEPAASLDAHSEQRVMEALNAASLRQ--TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRY 567
Cdd:PRK13548 146 ARVLAQLWEPDGPprwlllDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNLAARYaDRIVLLHQGRLVADGTP 225
|
..
gi 446966322 568 AE 569
Cdd:PRK13548 226 AE 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
369-570 |
3.62e-16 |
|
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: 78.10 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPE---SWRKHLSWVGQNpqlpAA-----TL 439
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpDSGEILVDGQDITGLSEKelyELRRRIGMLFQG----GAlfdslTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 440 RDNV---LLARPDASEQELQA----ALDNAWVSEFLPLLPqgvdtpvgdqaARLSVGQAQRVAVARALLNPCSLLLLDEP 512
Cdd:COG1127 100 FENVafpLREHTDLSEAEIRElvleKLELVGLPGAADKMP-----------SELSGGMRKRVALARALALDPEILLYDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446966322 513 AASLDAHSEQRVME---ALNAAsLRQTTLMVTHQLEDL---AEWdvIWVMQDGRIIEQGRYAEL 570
Cdd:COG1127 169 TAGLDPITSAVIDElirELRDE-LGLTSVVVTHDLDSAfaiADR--VAVLADGKIIAEGTPEEL 229
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
369-563 |
5.65e-16 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 76.89 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDL----SPESWRKHLSWVGQNPQL-PAATLRDN 442
Cdd:TIGR03608 17 LNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFdSGQVYLNGQETPPLnskkASKFRREKLGYLFQNFALiENETVEEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 443 VLLA-----RPDASEQELQ-AALDNAWVSEflpLLPQGVDTpvgdqaarLSVGQAQRVAVARALLNPCSLLLLDEPAASL 516
Cdd:TIGR03608 97 LDLGlkykkLSKKEKREKKkEALEKVGLNL---KLKQKIYE--------LSGGEQQRVALARAILKPPPLILADEPTGSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446966322 517 DAHSEQRVMEALNA-ASLRQTTLMVTHQLEdlaewdvIWVMQDgRIIE 563
Cdd:TIGR03608 166 DPKNRDEVLDLLLElNDEGKTIIIVTHDPE-------VAKQAD-RVIE 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
369-546 |
1.39e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 76.35 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGF-LSYQGSLRINGIELRDLSPESWRkhlswVGQNPQL-PAATLRDNVLLA 446
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEGKQITEPGPDRMV-----VFQNYSLlPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 ----RPDASEQELQAALDnawvsEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHS-- 520
Cdd:TIGR01184 79 vdrvLPDLSKSERRAIVE-----EHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTrg 151
|
170 180
....*....|....*....|....*...
gi 446966322 521 --EQRVMEALNAAslRQTTLMVTHQLED 546
Cdd:TIGR01184 152 nlQEELMQIWEEH--RVTVLMVTHDVDE 177
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
350-550 |
1.42e-15 |
|
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: 74.50 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGfL--SYQGSLRIngielrdlsPEswRKHLSW 427
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LwpWGSGRIGM---------PE--GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 428 VGQNPQLPAATLRDnvLLARPdaseqelqaaldnaWVSEflpllpqgvdtpvgdqaarLSVGQAQRVAVARALLNPCSLL 507
Cdd:cd03223 69 LPQRPYLPLGTLRE--QLIYP--------------WDDV-------------------LSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446966322 508 LLDEPAASLDAHSEQRVMEALNAASLrqTTLMVTHQ--LEDLAEW 550
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKELGI--TVISVGHRpsLWKFHDR 156
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
369-570 |
1.75e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.06 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSG-FLSYQGSLRINGIELRDLSPESWRKHLSWVGQNP--QLPAATLRDNVLL 445
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGlFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 446 ARPDAS--EQELQAALDNAWVSefLPLLPQGVDTPvgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQR 523
Cdd:PRK13642 106 GMENQGipREEMIKRVDEALLA--VNMLDFKTREP-----ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446966322 524 VMEALNAASLRQ--TTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK13642 179 IMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
350-570 |
2.22e-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: 76.18 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLL------NALSGFLSYQGSLRINGIELRD--LSPESW 421
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKN-INLDIPKNQVTALIGPSGCGKSTLLrslnrmNDLVPGVRIEGKVLFDGQDIYDkkIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 422 RKHLSWVGQNPQLPAATLRDNVLLArPDASEQELQAALDNAwVSEFL--PLLPQGVDTPVGDQAARLSVGQAQRVAVARA 499
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYG-PRLHGIKDKKELDEI-VEESLkkAALWDEVKDRLHDSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446966322 500 LLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARIsDRTAFFYDGELVEYGPTEQI 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
350-543 |
2.46e-15 |
|
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: 74.84 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLfITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPeSWRKHLSWV 428
Cdd:cd03231 1 LEADEL-TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPpLAGRVLLNGGPLDFQRD-SIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 429 GQNPQLPAA-TLRDNVLLARPDASEQELQAALDNAWVSEFlpllpqgVDTPVgdqaARLSVGQAQRVAVARALLNPCSLL 507
Cdd:cd03231 79 GHAPGIKTTlSVLENLRFWHADHSDEQVEEALARVGLNGF-------EDRPV----AQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 446966322 508 LLDEPAASLDAHSEQRVMEALNAASLR-QTTLMVTHQ 543
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMAGHCARgGMVVLTTHQ 184
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
368-570 |
2.49e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 75.74 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 368 PLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPesWRKHLSWVGQNPQL-PAATLRDNVL- 444
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETpTSGEILLDGKDITNLPP--HKRPVNTVFQNYALfPHLTVFENIAf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 -LARPDASEQELQAAldnawVSEFLPLlpqgvdTPVGDQAAR----LSVGQAQRVAVARALLNPCSLLLLDEPAASLDAH 519
Cdd:cd03300 96 gLRLKKLPKAEIKER-----VAEALDL------VQLEGYANRkpsqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446966322 520 SEQRVMEALNA--ASLRQTTLMVTH-QLEDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:cd03300 165 LRKDMQLELKRlqKELGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
364-570 |
6.63e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 76.34 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 364 TLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELR-DLSPEswRKHLSWVGQNPQL-PAATLR 440
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpDSGRIVLNGRDLFtNLPPR--ERRVGFVFQHYALfPHMTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 441 DNV---LLARPdASEQELQAAldnawVSEFLPLlpqgVD-TPVGDQ-AARLSVGQAQRVAVARALLNPCSLLLLDEPAAS 515
Cdd:COG1118 94 ENIafgLRVRP-PSKAEIRAR-----VEELLEL----VQlEGLADRyPSQLSGGQRQRVALARALAVEPEVLLLDEPFGA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 516 LDAH--SEQRvmealnaASLRQ-------TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:COG1118 164 LDAKvrKELR-------RWLRRlhdelggTTVFVTHDQEEALELaDRVVVMNQGRIEQVGTPDEV 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
369-569 |
6.80e-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: 74.69 E-value: 6.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSP-ESWRKHLSWVGQNPQL-PAATLRDNVLL 445
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRpTSGRILFDGRDITGLPPhRIARLGIARTFQNPRLfPELTVLENVLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 446 A--------------RPDASEQELQAALDNAW-VSEFLPLLPQGvDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLD 510
Cdd:COG0411 103 AaharlgrgllaallRLPRARREEREARERAEeLLERVGLADRA-DEPAGN----LSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 511 EPAASLDAHSEQRVMEALnaASLRQ----TTLMVTHQLE---DLAEWdvIWVMQDGRIIEQGRYAE 569
Cdd:COG0411 178 EPAAGLNPEETEELAELI--RRLRDergiTILLIEHDMDlvmGLADR--IVVLDFGRVIAEGTPAE 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
369-570 |
7.45e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.20 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHL-SWVGQNPQLPAATL-RDNV-- 443
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITITHKTKDKYIRPVrKRIGMVFQFPESQLfEDTVer 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 -LLARPDASEQELQAALDNAwvseFLPLLPQGVDTPVGDQAA-RLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSE 521
Cdd:PRK13646 106 eIIFGPKNFKMNLDEVKNYA----HRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446966322 522 QRVMEALNAASLRQ--TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK13646 182 RQVMRLLKSLQTDEnkTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKEL 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
363-565 |
8.68e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.67 E-value: 8.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 363 KTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAA-TLR 440
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 441 DNVLLARP----------DASEQELQAALDNAWVSEFlpllpqgVDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLD 510
Cdd:PRK11231 95 ELVAYGRSpwlslwgrlsAEDNARVNQAMEQTRINHL-------ADRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 511 EPAASLDAhSEQ----RVMEALNAASlrQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:PRK11231 164 EPTTYLDI-NHQvelmRLMRELNTQG--KTVVTVLHDLNQASRYcDHLVVLANGHVMAQG 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
333-565 |
9.83e-15 |
|
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: 77.03 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 333 AHPQRGEAELALTDPLTIEAEDLFITSPEGKTLAGP----------LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY 402
Cdd:COG4172 259 AEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGLFRRtvghvkavdgVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 403 QGSLRINGIELRDLSPE---SWRKHLSWVGQ------NPQLP-AATLRDNVLLARPDASEQELQAAldnawVSEFLpllp 472
Cdd:COG4172 339 EGEIRFDGQDLDGLSRRalrPLRRRMQVVFQdpfgslSPRMTvGQIIAEGLRVHGPGLSAAERRAR-----VAEAL---- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 473 qgvdTPVG-DQAAR------LSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALnaASLRQ----TTLMVT 541
Cdd:COG4172 410 ----EEVGlDPAARhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLL--RDLQRehglAYLFIS 483
|
250 260 270
....*....|....*....|....*....|.
gi 446966322 542 HqleDLAewdVIW-------VMQDGRIIEQG 565
Cdd:COG4172 484 H---DLA---VVRalahrvmVMKDGKVVEQG 508
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
384-577 |
1.13e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.76 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 384 RSGSGKSSLLnalsgfLSYQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLARPDASEQELQAALDNAW 463
Cdd:PTZ00265 1263 EGGSGEDSTV------FKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAA 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 464 VSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLR--QTTLMVT 541
Cdd:PTZ00265 1337 IDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKadKTIITIA 1416
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446966322 542 HQLEDLAEWDVIWVMQD----GRIIE-QGRYAE-LSVAGGPF 577
Cdd:PTZ00265 1417 HRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEElLSVQDGVY 1458
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
369-565 |
2.44e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 72.74 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNAL-------SGFLSYQG-----SLRINGIELRDLspeswRKHLSWVGQNPQL-P 435
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGhqfdfSQKPSEKAIRLL-----RQKVGMVFQQYNLwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 436 AATLRDNVL--------LARPDASE--QELQAALDNAWVSEFLPLlpqgvdtpvgdqaaRLSVGQAQRVAVARALLNPCS 505
Cdd:COG4161 96 HLTVMENLIeapckvlgLSKEQAREkaMKLLARLRLTDKADRFPL--------------HLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 506 LLLLDEPAASLDAHSEQRVMEALNaaSLRQ---TTLMVTHQLEdLAE---WDVIWvMQDGRIIEQG 565
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIR--ELSQtgiTQVIVTHEVE-FARkvaSQVVY-MEKGRIIEQG 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
369-558 |
3.05e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.22 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIE-LRDLSPESWRKHLSWVGQNPQLPAATLRDNV--- 443
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIINDSHnLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 ------LLARPDASEQELQAALDNA------------------------------------------------WVSEFLP 469
Cdd:PTZ00265 484 lyslkdLEALSNYYNEDGNDSQENKnkrnscrakcagdlndmsnttdsneliemrknyqtikdsevvdvskkvLIHDFVS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 470 LLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALN--AASLRQTTLMVTHQLEDL 547
Cdd:PTZ00265 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
250
....*....|.
gi 446966322 548 AEWDVIWVMQD 558
Cdd:PTZ00265 644 RYANTIFVLSN 654
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
369-558 |
3.10e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.05 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLA- 446
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTsGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIFPw 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 -----RPDasEQELQAALDnawvsEF-LP--LLPQGVdtpvgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDA 518
Cdd:PRK10247 106 qirnqQPD--PAIFLDDLE-----RFaLPdtILTKNI--------AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446966322 519 HSEQRVMEalnaaslrqttlmVTHQLEDLAEWDVIWVMQD 558
Cdd:PRK10247 171 SNKHNVNE-------------IIHRYVREQNIAVLWVTHD 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
370-573 |
3.22e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.44 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSP-ESWRKHLSWVGQNPQL-PAATLRDNVLLA 446
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPdSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLvPNLSVAENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 RP-------DASEQELQAAldnawvsEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAH 519
Cdd:COG1129 104 REprrggliDWRAMRRRAR-------ELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTER 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 520 SEQRVMEALNaaSLRQ---TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAELSVA 573
Cdd:COG1129 175 EVERLFRIIR--RLKAqgvAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAELTED 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
350-570 |
3.25e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.64 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQGSLRINGIELRD------LSPESWRK 423
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDG-VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDgqdifkMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 424 HLSWVGQNPQ-LPAATLRDNVLLA----RPDASEQELQAALdnAWVSEFLPLLPQgVDTPVGDQAARLSVGQAQRVAVAR 498
Cdd:PRK14247 83 RVQMVFQIPNpIPNLSIFENVALGlklnRLVKSKKELQERV--RWALEKAQLWDE-VKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 499 ALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTH---QLEDLAEWdvIWVMQDGRIIEQGRYAEL 570
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDY--VAFLYKGQIVEWGPTREV 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
350-570 |
3.99e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.72 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSW 427
Cdd:PRK13632 8 IKVENVSFSYPNSENNAlKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQsGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 428 VGQNP--QLPAATLRDNVL--LARPDASEQELQAALDNAW----VSEFLPLLPQgvdtpvgdqaaRLSVGQAQRVAVARA 499
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAfgLENKKVPPKKMKDIIDDLAkkvgMEDYLDKEPQ-----------NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 500 LLNPCSLLLLDEPAASLDAHSEQRVMEALNaaSLRQT---TLM-VTHQLEDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMV--DLRKTrkkTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
369-565 |
4.46e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.97 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNAL-------SGFLSYQG-----SLRINGIELRDLspeswRKHLSWVGQNPQL-P 435
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGnhfdfSKTPSDKAIREL-----RRNVGMVFQQYNLwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 436 AATLRDNVL--------LARPDASEQELQAaLDNAWVSEFLPLLPQgvdtpvgdqaaRLSVGQAQRVAVARALLNPCSLL 507
Cdd:PRK11124 96 HLTVQQNLIeapcrvlgLSKDQALARAEKL-LERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446966322 508 LLDEPAASLDAHSEQRVMEALNaaSLRQ---TTLMVTHQLE---DLAEwDVIWvMQDGRIIEQG 565
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIR--ELAEtgiTQVIVTHEVEvarKTAS-RVVY-MENGHIVEQG 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
348-563 |
5.84e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.55 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 348 LTIEAEDL-FITSP----EGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGielRDLSPESW 421
Cdd:PRK13641 1 MSIKFENVdYIYSPgtpmEKKGLDN-ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpSSGTITIAG---YHITPETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 422 RKHLS----WVGQNPQLPAATLRDNVLLARPD-------ASEQELQ-AALDnaWVSEFlpllpqGVDTPVGDQAA-RLSV 488
Cdd:PRK13641 77 NKNLKklrkKVSLVFQFPEAQLFENTVLKDVEfgpknfgFSEDEAKeKALK--WLKKV------GLSEDLISKSPfELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 489 GQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEA-LNAASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIE 563
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEYaDDVLVLEHGKLIK 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
369-570 |
6.59e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRDNvLLAR 447
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELErGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN-LDPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 PDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSeqrvmEA 527
Cdd:PLN03130 1337 NEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT-----DA 1411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446966322 528 LNAASLRQ-----TTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:PLN03130 1412 LIQKTIREefkscTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
369-565 |
8.45e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.04 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSL---LNALsgFLSYQGSLRINGIELRDLSpESW--RKHLSWVGQNP--QLPAATLRD 441
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIakhMNAL--LIPSEGKVYVDGLDTSDEE-NLWdiRNKAGMVFQNPdnQIVATIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 442 NV------LLARPDASEQELQAALDNAWVSEFLPLLPQgvdtpvgdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPAAS 515
Cdd:PRK13633 106 DVafgpenLGIPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446966322 516 LDAHSEQRVMEALNAASLRQ--TTLMVTHQLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
369-581 |
9.94e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 74.56 E-value: 9.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGielrdlspeswrkHLSWVGQNPQLPAATLRDNVLLAR 447
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEpSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFGL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 pDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEA 527
Cdd:TIGR01271 512 -SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 528 -LNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLL 581
Cdd:TIGR01271 591 cLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
369-570 |
1.84e-13 |
|
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: 70.06 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSPEswRKHLSWVGQNPQL-PAATLRDNV--- 443
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGGEDATDVPVQ--ERNVGFVFQHYALfRHMTVFDNVafg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LLARPDA---SEQELQAAldnawVSEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAhs 520
Cdd:cd03296 99 LRVKPRSerpPEAEIRAK-----VHELLKLV--QLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA-- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 521 eqRVMEALNAAsLRQ-------TTLMVTH-QLEDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:cd03296 170 --KVRKELRRW-LRRlhdelhvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
370-570 |
2.39e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 71.26 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLL---NAL----SGflsyqgSLRINGIELRDLSPES---WRKHLSWVGQNPQL-PAAT 438
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIrciNLLerptSG------SVLVDGVDLTALSERElraARRKIGMIFQHFNLlSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 439 LRDNVllARP------DASEQElqaaldnAWVSEFLPLlpqgvdtpVG--DQA----ARLSVGQAQRVAVARALLNPCSL 506
Cdd:COG1135 99 VAENV--ALPleiagvPKAEIR-------KRVAELLEL--------VGlsDKAdaypSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446966322 507 LLLDEPAASLDAHSEQRVMEALnaASLRQ----TTLMVTHQLE---DLAewDVIWVMQDGRIIEQGRYAEL 570
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLL--KDINRelglTIVLITHEMDvvrRIC--DRVAVLENGRIVEQGPVLDV 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
369-565 |
2.54e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.03 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGI--------ELRDLSPES--------WRKHLSWVGQN 431
Cdd:PRK13631 45 ISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkSKYGTIQVGDIyigdkknnHELITNPYSkkiknfkeLRRRVSMVFQF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 432 P--QLPAATLRDNVLLArPDASEQELQAALDNAwvSEFLPLLpqGVDTPVGDQAA-RLSVGQAQRVAVARALLNPCSLLL 508
Cdd:PRK13631 125 PeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLA--KFYLNKM--GLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 509 LDEPAASLDAHSEQRVME-ALNAASLRQTTLMVTHQLEDLAE-WDVIWVMQDGRIIEQG 565
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQlILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTG 258
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
371-570 |
3.64e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.89 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 371 FTLPAGQRAVLVGRSGSGKSSLLnalsgfLSYQ-------GSLRINGIE-----LRDLspeswRKHLSWVGQNPQLPAAT 438
Cdd:PTZ00243 1331 FRIAPREKVGIVGRTGSGKSTLL------LTFMrmvevcgGEIRVNGREigaygLREL-----RRQFSMIPQDPVLFDGT 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 439 LRDNVllaRP--DASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSL-LLLDEPAAS 515
Cdd:PTZ00243 1400 VRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGfILMDEATAN 1476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 516 ----LDAHSEQRVMEALNAaslrQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:PTZ00243 1477 idpaLDRQIQATVMSAFSA----YTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
350-570 |
3.77e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.26 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELrDLSPE---SWRKHL 425
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGKPI-DYSRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 426 SWVGQNP--QLPAATLRDNVLLARPDAS--EQELQAALDNAwvseflpLLPQGVdTPVGDQAAR-LSVGQAQRVAVARAL 500
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNA-------LKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446966322 501 LNPCSLLLLDEPAASLDAHSEQRVMEAL--NAASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLveMQKELGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEV 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
369-564 |
4.31e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.51 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRdlSPESWRkhlSWVGQNPQL-PAATLRDNVL-- 444
Cdd:COG4525 26 VSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPsSGEITLDGVPVT--GPGADR---GVVFQKDALlPWLNVLDNVAfg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 --LARPDASEQELQAAldnawvsEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQ 522
Cdd:COG4525 101 lrLRGVPKAERRARAE-------ELLALV--GLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446966322 523 RVMEAL--NAASLRQTTLMVTHQLED---LAEwdVIWVMQD--GRIIEQ 564
Cdd:COG4525 172 QMQELLldVWQRTGKGVFLITHSVEEalfLAT--RLVVMSPgpGRIVER 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
348-566 |
4.65e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.77 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 348 LTIEAEDLFITSPEGKTLAGP----LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSP---- 418
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFEGRalfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVpTQGSVRVDDTLITSTSKnkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 419 ESWRKHLSWVGQNP--QLPAATLRDNVLLARPD--ASEQELQAAldnawVSEFLPLLpqGVDTPVGDQAA-RLSVGQAQR 493
Cdd:PRK13649 81 KQIRKKVGLVFQFPesQLFEETVLKDVAFGPQNfgVSQEEAEAL-----AREKLALV--GISESLFEKNPfELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 494 VAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNaaSLRQ---TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGR 566
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFK--KLHQsgmTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
369-565 |
4.80e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 69.76 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHL-SWVGQNPQLPAATLRDNVLLA 446
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSSTSKQKEIKPVrKKVGVVFQFPESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 RPDASEQELQAALDNA--WVSEFLPLLpqGVDTPVGDQAA-RLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQR 523
Cdd:PRK13643 105 DVAFGPQNFGIPKEKAekIAAEKLEMV--GLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446966322 524 VMEALNAA-SLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:PRK13643 183 MMQLFESIhQSGQTVVLVTHLMDDVADYaDYVYLLEKGHIISCG 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
350-565 |
4.87e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.63 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSP-ESWRKHLSW 427
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 428 VGQNP--QLPAATLRDNVLLARPDA--SEQELQAALDNAwvseflpLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNP 503
Cdd:PRK13644 82 VFQNPetQFVGRTVEEDLAFGPENLclPPIEIRKRVDRA-------LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446966322 504 CSLLLLDEPAASLDAHSEQRVMEALNAASLR-QTTLMVTHQLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEG 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
350-565 |
7.35e-13 |
|
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: 67.99 E-value: 7.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLaGPLNFTLPAGQRAvLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDlSPESWRKHLSWV 428
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPpSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 429 GQNPQL-PAATLRDNV----LLARPDASE--QELQAALDNAWVSEFLpllpqgvDTPVGDqaarLSVGQAQRVAVARALL 501
Cdd:cd03264 78 PQEFGVyPNFTVREFLdyiaWLKGIPSKEvkARVDEVLELVNLGDRA-------KKKIGS----LSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 502 NPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAE-WDVIWVMQDGRIIEQG 565
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
369-569 |
8.74e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.92 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRD--LSPESWRKHLSWVGQNP--QLPAATLRDNV 443
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPeyQLFEETIEKDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LLA--RPDASEQELqaaldNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSE 521
Cdd:PRK13637 106 AFGpiNLGLSEEEI-----ENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446966322 522 QRVMEALNaaSLRQ----TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAE 569
Cdd:PRK13637 181 DEILNKIK--ELHKeynmTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPRE 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
369-562 |
9.00e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.91 E-value: 9.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALsGFLS--YQGSLRINGIELRDLSPESW----RKHLSWV------------GQ 430
Cdd:PRK10535 27 ISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDkpTSGTYRVAGQDVATLDADALaqlrREHFGFIfqryhllshltaAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 431 NPQLPA--ATLRDNVLLARPDASEQELqaaldnawvseflpllpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLL 508
Cdd:PRK10535 106 NVEVPAvyAGLERKQRLLRAQELLQRL------------------GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 509 LDEPAASLDAHSEQRVMEALNaaSLRQ---TTLMVTHQLEDLAEWDVIWVMQDGRII 562
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILH--QLRDrghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
74-322 |
9.01e-13 |
|
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: 69.08 E-value: 9.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 74 VLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLL 153
Cdd:cd18563 54 VLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 154 IVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASE 233
Cdd:cd18563 134 IGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 234 DFRQRTMEVLRLAFLSSGILEFFTSLSIALVaVYFGFSYL--GELDFGhydtgvTLAAgFLALILapEFFQPLRDLGTFY 311
Cdd:cd18563 214 ELLDANIRAEKLWATFFPLLTFLTSLGTLIV-WYFGGRQVlsGTMTLG------TLVA-FLSYLG--MFYGPLQWLSRLN 283
|
250
....*....|.
gi 446966322 312 HAKAQAVGAAD 322
Cdd:cd18563 284 NWITRALTSAE 294
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
350-565 |
1.11e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.67 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL----SYQGSLRINGIELRDLSPESWRKH 424
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPAlNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 425 LSWVGQNP--QLPAATLRDNVL--LARPDASEQELQAALDNAwvseflpLLPQGVDTPVGDQAARLSVGQAQRVAVARAL 500
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAfgLENRAVPRPEMIKIVRDV-------LADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 501 LNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQ--TTLMVTHQLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
361-565 |
1.12e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.59 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 361 EGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSPEswRKHLSWVGQNPQL-PAAT 438
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPdSGRIMLDGQDITHVPAE--NRHVNTVFQSYALfPHMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 439 LRDNVL--LARPDASEQELQA----ALDNAWVSEFLPLLPQgvdtpvgdqaaRLSVGQAQRVAVARALLNPCSLLLLDEP 512
Cdd:PRK09452 103 VFENVAfgLRMQKTPAAEITPrvmeALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 513 AASLDaHSEQRVMEALNAASLRQ---TTLMVTH-QLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:PRK09452 172 LSALD-YKLRKQMQNELKALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
370-562 |
1.28e-12 |
|
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: 65.91 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSP-ESWRKHLSWVGQnpqlpaatlrdnvllar 447
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVDGKEVSFASPrDARRAGIAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 pdaseqelqaaldnawvseflpllpqgvdtpvgdqaarLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEA 527
Cdd:cd03216 83 --------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 446966322 528 LnaASLRQ---TTLMVTHQLEDLAEW-DVIWVMQDGRII 562
Cdd:cd03216 125 I--RRLRAqgvAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
357-570 |
1.58e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.98 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 357 ITSPEGK-TLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPEswRKHLSWVGQNPQL 434
Cdd:PRK11432 12 ITKRFGSnTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 435 -PAATLRDNV-----LLARPDASEQELqaaldnawVSEFLPLLP-QGVDTPVGDQaarLSVGQAQRVAVARALLNPCSLL 507
Cdd:PRK11432 90 fPHMSLGENVgyglkMLGVPKEERKQR--------VKEALELVDlAGFEDRYVDQ---ISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 508 LLDEPAASLDAHSEQRVMEALNaaSLRQ----TTLMVTH-QLEDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIR--ELQQqfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
350-570 |
1.76e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.91 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWV 428
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKpTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 429 GQNP--QLPAATLRDNV------LLARPDASEQELQAALDNAWVSEFLPLLPQgvdtpvgdqaaRLSVGQAQRVAVARAL 500
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIafgpinLGLDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446966322 501 LNPCSLLLLDEPAASLDAHSEQRVMEALNAASLR--QTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
349-587 |
1.78e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.47 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 349 TIEAEDLfITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSgFLSY--QGSLRINGIEL---RDLSPE---- 419
Cdd:PRK11264 3 AIEVKNL-VKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCIN-LLEQpeAGTIRVGDITIdtaRSLSQQkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 420 -SWRKHLSWVGQNPQL-PAATLRDNV----LLARPDASEQELQAALDnawvseflpLLPQ-GVDTPVGDQAARLSVGQAQ 492
Cdd:PRK11264 81 rQLRQHVGFVFQNFNLfPHRTVLENIiegpVIVKGEPKEEATARARE---------LLAKvGLAGKETSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 493 RVAVARALLNPCSLLLLDEPAASLDAhseQRVMEALNA----ASLRQTTLMVTHQL---EDLAewDVIWVMQDGRIIEQg 565
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDP---ELVGEVLNTirqlAQEKRTMVIVTHEMsfaRDVA--DRAIFMDQGRIVEQ- 225
|
250 260
....*....|....*....|..
gi 446966322 566 ryaelsvagGPFATLLAHRQEE 587
Cdd:PRK11264 226 ---------GPAKALFADPQQP 238
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
369-565 |
2.21e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.47 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ------GSLRINGIELRDLspeswRKHLSWVGQNP--QLPAATLR 440
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsgeifyNNQAITDDNFEKL-----RKHIGIVFQNPdnQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 441 DNVLLArpdaseqelqaaLDNAWVS--EFLPLLPQGV-DTPVGDQA----ARLSVGQAQRVAVARALLNPCSLLLLDEPA 513
Cdd:PRK13648 103 YDVAFG------------LENHAVPydEMHRRVSEALkQVDMLERAdyepNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446966322 514 ASLDAHSEQRVMEALNAASLRQ--TTLMVTHQLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
369-570 |
2.44e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.04 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLL---NALSGFLSyqGSLRINGIELRD--LSPESWRKHLSWVGQNPQL-PAATLRDN 442
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLrciNKLEEITS--GDLIVDGLKVNDpkVDERLIRQEAGMVFQQFYLfPHLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 443 VLLA----RPDASEQELQAALDnawvseflpLLPQ-GVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:PRK09493 98 VMFGplrvRGASKEEAEKQARE---------LLAKvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 518 A---HSEQRVMEALnaASLRQTTLMVTHQLEdLAEwDV---IWVMQDGRIIEQGRYAEL 570
Cdd:PRK09493 169 PelrHEVLKVMQDL--AEEGMTMVIVTHEIG-FAE-KVasrLIFIDKGRIAEDGDPQVL 223
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
29-324 |
3.27e-12 |
|
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: 67.45 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 29 LLGFVSGILIIAQAWFMARILQHMIMENiPREALLLPFTLLVLTFVLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQ 108
Cdd:cd18552 6 LGMILVAATTAALAWLLKPLLDDIFVEK-DLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 109 AGPAWIQGKPAGSWATLVL---EQIddmhdyyarylpQMALAVSV------PLLIVVAI---FPSNWAAALILLGTAPLI 176
Cdd:cd18552 85 LPLSFFDRNSSGDLISRITndvNQV------------QNALTSALtvlvrdPLTVIGLLgvlFYLDWKLTLIALVVLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 177 PLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFF 256
Cdd:cd18552 153 ALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 257 TSLSIALVAVYFGFSYL-GELDFGhydtgvTLAAGFLALILApefFQPLRDLGTFYHAKAQAVGAADSL 324
Cdd:cd18552 233 GAIAIALVLWYGGYQVIsGELTPG------EFISFITALLLL---YQPIKRLSNVNANLQRGLAAAERI 292
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
347-570 |
3.54e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.65 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 347 PLTIEAEDLFITSPegKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-----SYQGSLRINGIELrdlSPESW 421
Cdd:PRK10418 2 PQQIELRNIALQAA--QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrQTAGRVLLDGKPV---APCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 422 R-KHLSWVGQNPQL---PAATLRDNVL-----LARPdASEQELQAALDNAWVSEflpllpqgVDTPVGDQAARLSVGQAQ 492
Cdd:PRK10418 77 RgRKIATIMQNPRSafnPLHTMHTHARetclaLGKP-ADDATLTAALEAVGLEN--------AARVLKLYPFEMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 493 RVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALnaASLRQT----TLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRY 567
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLL--ESIVQKralgMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDV 225
|
...
gi 446966322 568 AEL 570
Cdd:PRK10418 226 ETL 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
369-570 |
3.91e-12 |
|
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: 67.39 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ----GSLRINGIELRDLSPESWR----KHLSWVGQNPQ--L-PAA 437
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitsGEILFDGEDLLKLSEKELRkirgREIQMIFQDPMtsLnPVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 438 TLRDNV---LLARPDASEQELQAAldnawVSEFLPLLpqGVDTPVgDQAAR----LSVGQAQRVAVARALLNPCSLLLLD 510
Cdd:COG0444 104 TVGDQIaepLRIHGGLSKAEARER-----AIELLERV--GLPDPE-RRLDRypheLSGGMRQRVMIARALALEPKLLIAD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 511 EPAASLDAHSEQRVMEALnaASLRQ----TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:COG0444 176 EPTTALDVTIQAQILNLL--KDLQRelglAILFITHDLGVVAEIaDRVAVMYAGRIVEEGPVEEL 238
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
370-560 |
4.71e-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: 65.92 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSG-FLSYQGSLRIN----GIELRDLSPESW----RKHLSWVGQnpqlpaatlr 440
Cdd:COG4778 31 SFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSILVRhdggWVDLAQASPREIlalrRRTIGYVSQ---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 441 dnVLLARPDaseqelQAALDnaWVSEflPLLPQGVDTPVG-DQAARL------------------SVGQAQRVAVARALL 501
Cdd:COG4778 101 --FLRVIPR------VSALD--VVAE--PLLERGVDREEArARARELlarlnlperlwdlppatfSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446966322 502 NPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTT-LMVTHQLED---LAewDVIWVMQDGR 560
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAiIGIFHDEEVreaVA--DRVVDVTPFS 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
349-574 |
5.05e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.94 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 349 TIEAEDLFITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSW 427
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDG-VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTpTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 428 VGQNPQLPAA-TLRDNVLLARP----------DASEQELQAALDNAWVSEFlpllpqgVDTPVgdqaARLSVGQAQRVAV 496
Cdd:PRK09536 82 VPQDTSLSFEfDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQF-------ADRPV----TSLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 497 ARALLNPCSLLLLDEPAASLDAHSEQRVME-ALNAASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAELSVAG 574
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLElVRRLVDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
362-570 |
5.54e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 362 GKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNAL-------SGFlSYQGSLRING---IELRDLSpeSWRKHLSWVGQN 431
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGY-RYSGDVLLGGrsiFNYRDVL--EFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 432 PQLPAATLRDNVLL---ARPDASEQELQAaLDNAWVSEFLplLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLL 508
Cdd:PRK14271 110 PNPFPMSIMDNVLAgvrAHKLVPRKEFRG-VAQARLTEVG--LWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446966322 509 LDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
367-569 |
5.99e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 367 GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQGSLRINGIELRDLSPESWRKHLSWVGQNpQLPAATLrdNVL-- 444
Cdd:PRK03695 13 GPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQ-QTPPFAM--PVFqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 --LARPD-ASEQELQAALDNawVSEFLPLLPQgVDTPVGdqaaRLSVGQAQRVAVA-------RALLNPCSLLLLDEPAA 514
Cdd:PRK03695 90 ltLHQPDkTRTEAVASALNE--VAEALGLDDK-LGRSVN----QLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 515 SLDAhSEQRVMEALNAASLRQ--TTLMVTHQL-EDLAEWDVIWVMQDGRIIEQGRYAE 569
Cdd:PRK03695 163 SLDV-AQQAALDRLLSELCQQgiAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
349-565 |
9.12e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 9.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 349 TIEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRdlspESWRKHL-S 426
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLaSGKISILGQPTR----QALQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 427 WVGQNPQLPAA--TLRDNV----------LLARPDASEQE-LQAALDNAWVSEFLpllpqgvdtpvGDQAARLSVGQAQR 493
Cdd:PRK15056 82 YVPQSEEVDWSfpVLVEDVvmmgryghmgWLRRAKKRDRQiVTAALARVDMVEFR-----------HRQIGELSGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 494 VAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNaaSLR---QTTLMVTHQLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLR--ELRdegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
369-565 |
1.79e-11 |
|
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: 64.28 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPEsWRKHLSWV-GQNPQL-----PAATLRd 441
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVRVAGLVPWKRRKK-FLRRIGVVfGQKTQLwwdlpVIDSFY- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 442 nvLLARP-DASEQELQAALDNawVSEFLPLLPQgVDTPVgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHS 520
Cdd:cd03267 118 --LLAAIyDLPPARFKKRLDE--LSELLDLEEL-LDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446966322 521 EQRVMEALNAAS-LRQTTLMVT-HQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:cd03267 189 QENIRNFLKEYNrERGTTVLLTsHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
369-565 |
1.80e-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: 64.21 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQGSLR----INGIELrdlSPESWRKHLSWVGQNPQL-PAATLRD-- 441
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSgqilFNGQPR---KPDQFQKCVAYVRQDDILlPGLTVREtl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 442 ----NVLLARPDASEQELQAALDNawvseflpLLPQGVDTPVGDQAAR-LSVGQAQRVAVARALLNPCSLLLLDEPAASL 516
Cdd:cd03234 103 tytaILRLPRKSSDAIRKKRVEDV--------LLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446966322 517 DAHSEQRVMEALNAASLRQTTLMVT-HQ-LEDLAE-WDVIWVMQDGRIIEQG 565
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTiHQpRSDLFRlFDRILLLSSGEIVYSG 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
369-581 |
1.88e-11 |
|
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: 64.88 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGielrdlsPESWRKHLSWVgqnpqLPAaTLRDNVLLAR 447
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELePSEGKIKHSG-------RISFSSQFSWI-----MPG-TIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 pDASEQELQAALDNAWVSEFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEA 527
Cdd:cd03291 123 -SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 528 -LNAASLRQTTLMVTHQLEDLAEWDVIWVMQDGRIIEQGRYAELSVAGGPFATLL 581
Cdd:cd03291 202 cVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
369-564 |
2.34e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 65.49 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGielRDLSPESWR-KHLSWVGQNPQL-PAATLRDNVLL 445
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQtSGHIRFHG---TDVSRLHARdRKVGFVFQHYALfRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 446 A--------RPDASE--QELQAALDNAWVSEFLPLLPqgvdtpvgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPAAS 515
Cdd:PRK10851 98 GltvlprreRPNAAAikAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446966322 516 LDAHSEQRVMEALNA--ASLRQTTLMVTHQLEDLAE-WDVIWVMQDGrIIEQ 564
Cdd:PRK10851 167 LDAQVRKELRRWLRQlhEELKFTSVFVTHDQEEAMEvADRVVVMSQG-NIEQ 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
369-561 |
2.84e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.37 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKHLSWVGQNP--QLPAATLRDNVL- 444
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVEDDVAf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 -LARPDASEQELQAALDNAwvsefLPLlpqgvdtpVGDQA------ARLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:PRK13650 106 gLENKGIPHEEMKERVNEA-----LEL--------VGMQDfkerepARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446966322 518 AHSEQRVMEALNaaSLRQ----TTLMVTHQLEDLAEWDVIWVMQDGRI 561
Cdd:PRK13650 173 PEGRLELIKTIK--GIRDdyqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
369-571 |
3.26e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSPESWRKH-LSWVGQNPQL-PAATLRDNVL- 444
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVpPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLfPNLSVKENILf 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 -LARPDASEQELQAaldnawvseflpLLPQ-GVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQ 522
Cdd:PRK15439 110 gLPKRQASMQKMKQ------------LLAAlGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 523 RVMEALNAasLRQT---TLMVTHQLED---LAEWdvIWVMQDGRIIEQGRYAELS 571
Cdd:PRK15439 178 RLFSRIRE--LLAQgvgIVFISHKLPEirqLADR--ISVMRDGTIALSGKTADLS 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
370-565 |
3.57e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQG---SLRINGIELRDLS--PESWRKHLS---W--VGQNPqlpAATL 439
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAgevHYRMRDGQLRDLYalSEAERRRLLrteWgfVHQHP---RDGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 440 RDNV---------LLARPDASEQEL-QAALDnaWVSEfLPLLPQGVDtpvgDQAARLSVGQAQRVAVARALLNPCSLLLL 509
Cdd:PRK11701 103 RMQVsaggnigerLMAVGARHYGDIrATAGD--WLER-VEIDAARID----DLPTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446966322 510 DEPAASLDAHSEQRVMEALNA--ASLRQTTLMVTHqleDLAEW----DVIWVMQDGRIIEQG 565
Cdd:PRK11701 176 DEPTGGLDVSVQARLLDLLRGlvRELGLAVVIVTH---DLAVArllaHRLLVMKQGRVVESG 234
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
369-570 |
3.71e-11 |
|
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: 63.46 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPES-WRKHLSWVGQN----PQLpaaTLRDN 442
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPpRSGSIRFDGEDITGLPPHRiARLGIGYVPEGrrifPSL---TVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 443 VLL-ARPDASEQELQAALDnaWVSEFLPLLPQGVDTPvgdqAARLSVGQAQRVAVARALLNPCSLLLLDEPaasldahSE 521
Cdd:COG0410 99 LLLgAYARRDRAEVRADLE--RVYELFPRLKERRRQR----AGTLSGGEQQMLAIGRALMSRPKLLLLDEP-------SL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446966322 522 -------QRVMEALnaASLRQ---TTLMV---THQLEDLAewDVIWVMQDGRIIEQGRYAEL 570
Cdd:COG0410 166 glaplivEEIFEII--RRLNRegvTILLVeqnARFALEIA--DRAYVLERGRIVLEGTAAEL 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
368-569 |
4.22e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.44 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 368 PLNFTLPAGQRAVLVGRSGSGKSSLL---NAL---SGflsyqGSLRINGIELRDLSPESWRKHLSWVGQNPQ----LPAA 437
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTLIrciNLLerpTS-----GRVLVDGQDLTALSEKELRKARRQIGMIFQhfnlLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 438 TLRDNVLLARPDA--SEQELQAAldnawVSEFLPLlpqgvdtpVG--DQA----ARLSVGQAQRVAVARALLNPCSLLLL 509
Cdd:PRK11153 98 TVFDNVALPLELAgtPKAEIKAR-----VTELLEL--------VGlsDKAdrypAQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 510 DEPAASLDAHSEQRVMEAL---NaASLRQTTLMVTHQLedlaewDVI-------WVMQDGRIIEQGRYAE 569
Cdd:PRK11153 165 DEATSALDPATTRSILELLkdiN-RELGLTIVLITHEM------DVVkricdrvAVIDAGRLVEQGTVSE 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
350-565 |
4.93e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.32 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY------QGSLRING--IELRDLSPESW 421
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKG-VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearvEGEVRLFGrnIYSPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 422 RKHLSWVGQNPQ-LPAATLRDNV--------LLARPDASEQELQAALDNAwvseflpLLPQGVDTPVGDQAARLSVGQAQ 492
Cdd:PRK14267 84 RREVGMVFQYPNpFPHLTIYDNVaigvklngLVKSKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 493 RVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTH---QLEDLAEWDVIWVMqdGRIIEQG 565
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLYL--GKLIEVG 230
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
74-317 |
5.58e-11 |
|
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: 63.66 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 74 VLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLL 153
Cdd:cd18546 50 LAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 154 IVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASE 233
Cdd:cd18546 130 IAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 234 DFRQRTMEVLRLAFLSSGILEFFTSLSIALVAVYFGFSYL-GELDFGhydtgvTLAAGFLALILapeFFQPLRDLGTFYH 312
Cdd:cd18546 210 DYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAaGTLTVG------VLVAFLLYLRR---FFAPIQQLSQVFD 280
|
....*
gi 446966322 313 AKAQA 317
Cdd:cd18546 281 SYQQA 285
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
348-570 |
6.04e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.16 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 348 LTIEaedlfITSPEGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-----GSLRINGIELRDLSPESW 421
Cdd:COG4170 9 LTIE-----IDTPQGRVKAvDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtaDRFRWNGIDLLKLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 422 RK----HLSWVGQNPQL---PAATLRDNVLLARPDASeqelqaaLDNAWVSEF-------LPLLPQgvdtpVGDQAAR-- 485
Cdd:COG4170 84 RKiigrEIAMIFQEPSScldPSAKIGDQLIEAIPSWT-------FKGKWWQRFkwrkkraIELLHR-----VGIKDHKdi 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 486 -------LSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSE-Q--RVMEALNaaSLRQTT-LMVTHQLEDLAEW-DVI 553
Cdd:COG4170 152 mnsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQaQifRLLARLN--QLQGTSiLLISHDLESISQWaDTI 229
|
250
....*....|....*..
gi 446966322 554 WVMQDGRIIEQGRYAEL 570
Cdd:COG4170 230 TVLYCGQTVESGPTEQI 246
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
362-561 |
7.13e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.77 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 362 GKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGF-LSYQGSLRINGIELRDLspeswRKHLSWVGQNPQL-PAATL 439
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGELLAGTAPLAEA-----REDTRLMFQDARLlPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 440 RDNVLLA-RPDASEQELQAaldnawvseflpLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDA 518
Cdd:PRK11247 99 IDNVGLGlKGQWRDAALQA------------LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446966322 519 HSeqRV-MEALNAASLRQ---TTLMVTHQL-EDLAEWDVIWVMQDGRI 561
Cdd:PRK11247 167 LT--RIeMQDLIESLWQQhgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
328-570 |
8.51e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.09 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 328 METPLAHPQrGEAELALTdPLtIEAEDLfITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGF-LSYQGSL 406
Cdd:PRK11607 1 MNDAIPRPQ-AKTRKALT-PL-LEIRNL-TKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 407 RINGIELRDLSPesWRKHLSWVGQNPQL-PAATLRDNVLLArpdASEQELQAALDNAWVSEFLPLLpqGVDTPVGDQAAR 485
Cdd:PRK11607 77 MLDGVDLSHVPP--YQRPINMMFQSYALfPHMTVEQNIAFG---LKQDKLPKAEIASRVNEMLGLV--HMQEFAKRKPHQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 486 LSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQR----VMEALNAASLrqTTLMVTH-QLEDLAEWDVIWVMQDGR 560
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERVGV--TCVMVTHdQEEAMTMAGRIAIMNRGK 227
|
250
....*....|
gi 446966322 561 IIEQGRYAEL 570
Cdd:PRK11607 228 FVQIGEPEEI 237
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
369-549 |
8.73e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPeswRKHLSWVG-QNPQLPAATLRDNVLLA 446
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPpAAGTIKLDGGDIDDPDV---AEACHYLGhRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 RP--DASEQELQAALdnawvsEFLPLlpQGV-DTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSeQR 523
Cdd:PRK13539 98 AAflGGEELDIAAAL------EAVGL--APLaHLPFGY----LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA-VA 164
|
170 180
....*....|....*....|....*...
gi 446966322 524 VMEALNAASLRQ--TTLMVTHQLEDLAE 549
Cdd:PRK13539 165 LFAELIRAHLAQggIVIAATHIPLGLPG 192
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
350-565 |
9.16e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.79 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELR--DLSPESWRKHLS 426
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLIKGEPIKydKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 427 WVGQNP--QLPAATLRDNV------LLARPDASEQELQAALDNAWVSEFLPLLPQgvdtpvgdqaaRLSVGQAQRVAVAR 498
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVafgplnLGLSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 499 ALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMV-THQLeDLAEW--DVIWVMQDGRIIEQG 565
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIsTHDV-DLVPVyaDKVYVMSDGKIIKEG 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
369-575 |
1.08e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.14 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSP----ESWRKHLSWVGQ-NPQLPAATLRDN 442
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTpTSGDVIFNGQPMSKLSSaakaELRNQKLGFIYQfHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 443 V---LLARPDASEQELQAALDNawvseflpLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAH 519
Cdd:PRK11629 108 VampLLIGKKKPAEINSRALEM--------LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 520 SEQRVMEALNAASLRQTT--LMVTHQLEDLAEWDVIWVMQDGRIieqgrYAELSVAGG 575
Cdd:PRK11629 180 NADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDGRL-----TAELSLMGA 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
350-570 |
1.12e-10 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 61.62 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLfiTSPEGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIE-LRDlsPESWRKHLS 426
Cdd:cd03265 1 IEVENL--VKKYGDFEAvRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKpTSGRATVAGHDvVRE--PREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 427 WVGQNPQL-PAATLRDNVllarpdaseqELQAAL---DNAWVSEFLPLLPQGVDtpVGDQAARL----SVGQAQRVAVAR 498
Cdd:cd03265 77 IVFQDLSVdDELTGWENL----------YIHARLygvPGAERRERIDELLDFVG--LLEAADRLvktySGGMRRRLEIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 499 ALLNPCSLLLLDEPAASLDAHSEQRVMEALNA--ASLRQTTLMVTHQLEDlAEW--DVIWVMQDGRIIEQGRYAEL 570
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEE-AEQlcDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
350-545 |
1.54e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.95 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSyqgslringielRDLSPESwrkHLSWVG 429
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHA-VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT------------GDKSAGS---HIELLG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 430 QNPQLPAATLRD---------------NvLLARPDASEQELQAALDNA--W---VSEFLPLLPQ---GVDTPVG------ 480
Cdd:PRK09984 69 RTVQREGRLARDirksrantgyifqqfN-LVNRLSVLENVLIGALGSTpfWrtcFSWFTREQKQralQALTRVGmvhfah 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 481 DQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNaaSLRQT---TLMVT-HQLE 545
Cdd:PRK09984 148 QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLR--DINQNdgiTVVVTlHQVD 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
347-566 |
2.37e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.05 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 347 PLTIEAEDLFIT--SPEGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS----YQGSLRINGIELRDLSPE 419
Cdd:PRK09473 10 DALLDVKDLRVTfsTPDGDVTAvNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangrIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 420 SWRK----HLSWVGQ------NPQLPAATLRDNVLLARPDASEQElqaaldnAWvSEFLPLLpQGVDTPVGDQAARL--- 486
Cdd:PRK09473 90 ELNKlraeQISMIFQdpmtslNPYMRVGEQLMEVLMLHKGMSKAE-------AF-EESVRML-DAVKMPEARKRMKMyph 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 487 --SVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNaaSLRQ----TTLMVTHQLEDLAE-WDVIWVMQDG 559
Cdd:PRK09473 161 efSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLN--ELKRefntAIIMITHDLGVVAGiCDKVLVMYAG 238
|
....*..
gi 446966322 560 RIIEQGR 566
Cdd:PRK09473 239 RTMEYGN 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
344-565 |
2.50e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.33 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 344 LTDPLtIEAEDLFITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNAL------------SGFLSYQG----SLR 407
Cdd:PRK14239 1 MTEPI-LQVSDLSVYYNKKKALNS-VSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGhniySPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 408 INGIELRdlspeswrKHLSWVGQNPQLPAATLRDNVLL----------ARPD-ASEQELQAAldNAWvseflpllpQGVD 476
Cdd:PRK14239 79 TDTVDLR--------KEIGMVFQQPNPFPMSIYENVVYglrlkgikdkQVLDeAVEKSLKGA--SIW---------DEVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 477 TPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAEW-DVIWV 555
Cdd:PRK14239 140 DRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGF 219
|
250
....*....|
gi 446966322 556 MQDGRIIEQG 565
Cdd:PRK14239 220 FLDGDLIEYN 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
370-570 |
3.41e-10 |
|
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: 61.12 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESW----RKHLSWVGQNPQL-PAATLRDNV 443
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALlPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 L----LARPDASEQELQA--ALDNAWVSEFLPLLPQgvdtpvgdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:cd03294 124 AfgleVQGVPRAEREERAaeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 518 AHSEQRVMEALNA--ASLRQTTLMVTHQL-EDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
369-569 |
3.86e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.81 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPA-GQRAVLvGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRD------LSPEswRKHLSWVGQNPQL-PAATL 439
Cdd:PRK11144 17 VNLTLPAqGITAIF-GRSGAGKTSLINAISGLTRPQkGRIVLNGRVLFDaekgicLPPE--KRRIGYVFQDARLfPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 440 RDNvllarpdaseqeLQAALDNAWVSEF---LPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASL 516
Cdd:PRK11144 94 RGN------------LRYGMAKSMVAQFdkiVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 517 DAHSEQRVMEALN--AASLRQTTLMVTHQLED---LAewDVIWVMQDGRIIEQGRYAE 569
Cdd:PRK11144 160 DLPRKRELLPYLErlAREINIPILYVSHSLDEilrLA--DRVVVLEQGKVKAFGPLEE 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
371-563 |
4.44e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 371 FTLPAGQRAVLVGRSGSGKSSLLNALSGFlsYQ---GSLRINGIELRDLSP-ESWRKHLSWVGQNPQL-PAATLRDNVLL 445
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGN--YQpdaGSILIDGQEMRFASTtAALAAGVAIIYQELHLvPEMTVAENLYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 446 ARPDASEQELQAALDNAWVSEFLPLLPQGVD--TPVGdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPAASLDA-HSEQ 522
Cdd:PRK11288 103 GQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLK----YLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446966322 523 --RVMEALNAASlrQTTLMVTHQLEDLAEW-DVIWVMQDGRIIE 563
Cdd:PRK11288 179 lfRVIRELRAEG--RVILYVSHRMEEIFALcDAITVFKDGRYVA 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
350-565 |
4.82e-10 |
|
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: 59.46 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY---QGSLRINGIELRDLSP-ESWRK-- 423
Cdd:cd03217 1 LEIKDLHVSVGGKEILKG-VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevtEGEILFKGEDITDLPPeERARLgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 424 HLSWvgQNP-QLPAATLRDnvllarpdaseqelqaaldnawvseFLpllpQGVDtpVGdqaarLSVGQAQRVAVARALLN 502
Cdd:cd03217 80 FLAF--QYPpEIPGVKNAD-------------------------FL----RYVN--EG-----FSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 503 PCSLLLLDEPAASLDAHSEQRVMEALNaaSLR---QTTLMVTH--QLEDLAEWDVIWVMQDGRIIEQG 565
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVIN--KLReegKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
367-570 |
5.01e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 60.62 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 367 GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELrDLSPESWR-KHLSWVGQNP-----------Q 433
Cdd:COG4167 30 KPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIePTSGEILINGHKL-EYGDYKYRcKHIRMIFQDPntslnprlnigQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 434 LPAATLRDNVLLarpDASEQELQaaldnawVSEFLP---LLPqgvdtpvgDQAA----RLSVGQAQRVAVARALLNPCSL 506
Cdd:COG4167 109 ILEEPLRLNTDL---TAEEREER-------IFATLRlvgLLP--------EHANfyphMLSSGQKQRVALARALILQPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 507 LLLDEPAASLDahseqrvmealnaASLR-QTT-LM-------------VTHQL---EDLAewDVIWVMQDGRIIEQGRYA 568
Cdd:COG4167 171 IIADEALAALD-------------MSVRsQIInLMlelqeklgisyiyVSQHLgivKHIS--DKVLVMHQGEVVEYGKTA 235
|
..
gi 446966322 569 EL 570
Cdd:COG4167 236 EV 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
362-576 |
8.68e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.71 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 362 GKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESwrkhlSWVGQNPQL-PAATL 439
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEGPGAER-----GVVFQNEGLlPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 440 RDNV---LLARPDASEQELQAALdnawvsEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASL 516
Cdd:PRK11248 88 QDNVafgLQLAGVEKMQRLEIAH------QMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 517 DAHSEQRVMEALNA--ASLRQTTLMVTHQLED---LAEWDVIWVMQDGRIIEQGR--YAELSVAGGP 576
Cdd:PRK11248 160 DAFTREQMQTLLLKlwQETGKQVLLITHDIEEavfMATELVLLSPGPGRVVERLPlnFARRFVAGES 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
369-565 |
9.10e-10 |
|
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: 59.08 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGielrdlspeswrkHLSW-----VGQNPQLpaaTLRDN 442
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPdSGTVTVRG-------------RVSSllglgGGFNPEL---TGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 443 V-LLAR-PDASEQELQAALDnaWVSEFLPlLPQGVDTPVGdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHS 520
Cdd:cd03220 105 IyLNGRlLGLSRKEIDEKID--EIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446966322 521 EQRVMEALNaaSLRQ---TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:cd03220 178 QEKCQRRLR--ELLKqgkTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
369-543 |
1.06e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLsPESWRKHLSWVGQ----NPQLPAA-TLRDN 442
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARpDAGEVLWQGEPIRRQ-RDEYHQDLLYLGHqpgiKTELTALeNLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 443 VLLARPdASEQELQAALDNAWVSEFLpllpqgvDTPvgdqAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSeQ 522
Cdd:PRK13538 99 QRLHGP-GDDEALWEALAQVGLAGFE-------DVP----VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG-V 165
|
170 180
....*....|....*....|...
gi 446966322 523 RVMEALNAASLRQ--TTLMVTHQ 543
Cdd:PRK13538 166 ARLEALLAQHAEQggMVILTTHQ 188
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
370-571 |
1.09e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSG---FLSYQGSLRINGIELRDLS-PESWR-------------KHLSwVGQNP 432
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSGvypHGTYEGEIIFEGEELQASNiRDTERagiaiihqelalvKELS-VLENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 433 QL-----PAATLRDNVLLARPDASEQELQAALDnawvseflpllpqgVDTPVGDqaarLSVGQAQRVAVARALLNPCSLL 507
Cdd:PRK13549 104 FLgneitPGGIMDYDAMYLRAQKLLAQLKLDIN--------------PATPVGN----LGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 508 LLDEPAASLDAhSEQRVMEALnAASLRQ---TTLMVTHQLEDLAE-WDVIWVMQDGRIIEQGRYAELS 571
Cdd:PRK13549 166 ILDEPTASLTE-SETAVLLDI-IRDLKAhgiACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMT 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
369-565 |
1.30e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.94 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRING-----IELRdlspeswrkhlswVGQNPQLpaaTLRDN 442
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEpTSGRVEVNGrvsalLELG-------------AGFHPEL---TGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 443 VLLArpdA-----SEQELQAALDN----AWVSEFLpllpqgvDTPVGdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPA 513
Cdd:COG1134 109 IYLN---GrllglSRKEIDEKFDEivefAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 514 ASLDAHSEQRVMEALNaaSLRQ---TTLMVTHQLEDLAEW--DVIWvMQDGRIIEQG 565
Cdd:COG1134 175 AVGDAAFQKKCLARIR--ELREsgrTVIFVSHSMGAVRRLcdRAIW-LEKGRLVMDG 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
369-570 |
1.53e-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: 60.47 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKS----SLLNALSGFLSY-QGSLRINGIELRDLSPESWRK----HLSWVGQ------NP- 432
Cdd:COG4172 29 VSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHpSGSILFDGQDLLGLSERELRRirgnRIAMIFQepmtslNPl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 433 -----QLpAATLRDNVLLARPDASEQELQaaldnawvseflpLLPQgvdtpVG-DQAAR--------LSVGQAQRVAVAR 498
Cdd:COG4172 109 htigkQI-AEVLRLHRGLSGAAARARALE-------------LLER-----VGiPDPERrldayphqLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 499 ALLNPCSLLLLDEPAASLDAHSEQRVMEALnaASLRQTT----LMVTHQL---EDLAewDVIWVMQDGRIIEQGRYAEL 570
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLL--KDLQRELgmalLLITHDLgvvRRFA--DRVAVMRQGEIVEQGPTAEL 244
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
376-564 |
1.80e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 58.25 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 376 GQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSPESWR----KHLSWVGQNPQL-PAATLRDNV---LLA 446
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDdGSSGEVSLVGQPLHQMDEEARAklraKHVGFVFQSFMLiPTLNALENVelpALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 RPDASEQELQAALDnawvseflpLLPQ-GVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVM 525
Cdd:PRK10584 116 RGESSRQSRNGAKA---------LLEQlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446966322 526 EALNAASLRQTT--LMVTHQLEDLAEWDVIWVMQDGRIIEQ 564
Cdd:PRK10584 187 DLLFSLNREHGTtlILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
362-570 |
2.30e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.07 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 362 GKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELrdlsPESWRKHLSWVGQNPQL----PA 436
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPV----PARARLARARIGVVPQFdnldLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 437 ATLRDNVLL-ARP-DASEQELQAALDNawVSEFlPLLPQGVDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLDEPAA 514
Cdd:PRK13536 129 FTVRENLLVfGRYfGMSTREIEAVIPS--LLEF-ARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 515 SLDAHSEQRVMEALNAASLR-QTTLMVTHQLEDlAE--WDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARgKTILLTTHFMEE-AErlCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
369-565 |
3.40e-09 |
|
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: 57.38 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDlSPESWRKHLSWVGQNPQL-PAATLRDNVL-- 444
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLyDRLTARENLEyf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 -----LARpdaseQELQAALDnaWVSEFLPLLPQgVDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAH 519
Cdd:cd03266 103 aglygLKG-----DELTARLE--ELADRLGMEEL-LDRRVGG----FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446966322 520 SEQRVMEALNAASLRQTTLMV-THQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:cd03266 171 ATRALREFIRQLRALGKCILFsTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
377-548 |
3.82e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.74 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 377 QRAVLVGRSGSGKSSLLNALSGFLSYQGSLRING--------IELRDLSPESWRKHLSWVGQNPQLPAATLRDNVLLA-- 446
Cdd:PRK14258 34 KVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrveffnqnIYERRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvk 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 ----RP-----DASEQELQAAldNAWvseflpllpQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:PRK14258 114 ivgwRPkleidDIVESALKDA--DLW---------DEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLD 182
|
170 180 190
....*....|....*....|....*....|...
gi 446966322 518 AHSEQRVMEALNAASLRQ--TTLMVTHQLEDLA 548
Cdd:PRK14258 183 PIASMKVESLIQSLRLRSelTMVIVSHNLHQVS 215
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
362-570 |
4.00e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.88 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 362 GKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWVGQnpQLPAA--- 437
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPpSEGEILLDAQPLESWSSKAFARKVAYLPQ--QLPAAegm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 438 TLRDNVLLAR-PDASEQELQAALDNAWVSEFL------PLLPQGVDTpvgdqaarLSVGQAQRVAVARALLNPCSLLLLD 510
Cdd:PRK10575 101 TVRELVAIGRyPWHGALGRFGAADREKVEEAIslvglkPLAHRLVDS--------LSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446966322 511 EPAASLDAHSEQRVMEALNAASLRQ--TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAEL 235
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
16-426 |
4.18e-09 |
|
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: 59.04 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 16 QSVISQRWLNISR--LLGFVSGIliiAQAWFMARILQHMImenipreALLLPFTLLVLTFVLRAWVVWLRERVGYHA--- 90
Cdd:COG4615 5 RLLLRESRWLLLLalLLGLLSGL---ANAGLIALINQALN-------ATGAALARLLLLFAGLLVLLLLSRLASQLLltr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 91 -GQHIRFAIRRQVLDR--------LQQAGPAWIQgkpagswATLVlEQIDDMhdyyARYLPQMA-LAVSVPLLIVVAIFP 160
Cdd:COG4615 75 lGQHAVARLRLRLSRRilaaplerLERIGAARLL-------AALT-EDVRTI----SQAFVRLPeLLQSVALVLGCLAYL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 161 S--NWAAALILLgtaplipLFMALVGMGAADANRR--NFLALAR-----LSGHFLDRLRGMETLRI-FGRGEAEIES-IR 229
Cdd:COG4615 143 AwlSPPLFLLTL-------VLLGLGVAGYRLLVRRarRHLRRAReaedrLFKHFRALLEGFKELKLnRRRRRAFFDEdLQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 230 SASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVavYFGFSYLGELDFGHYdTGVTLAAGFLAlilapeffQPLRDLGT 309
Cdd:COG4615 216 PTAERYRDLRIRADTIFALANNWGNLLFFALIGLI--LFLLPALGWADPAVL-SGFVLVLLFLR--------GPLSQLVG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 310 FYHAKAQAVGAADSLKTF---METPLAHPQRGEAELALTDPLTIEAEDL---FITSPEGKTLA-GPLNFTLPAGQRAVLV 382
Cdd:COG4615 285 ALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQTLELRGVtyrYPGEDGDEGFTlGPIDLTIRRGELVFIV 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446966322 383 GRSGSGKSSLLNALSGFlsY---QGSLRINGIELRDLSPESWRKHLS 426
Cdd:COG4615 365 GGNGSGKSTLAKLLTGL--YrpeSGEILLDGQPVTADNREAYRQLFS 409
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-570 |
5.51e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.36 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 352 AEDLFITSP-----EGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIEL---RDL---SPE 419
Cdd:PRK14246 7 AEDVFNISRlylyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVLyfgKDIfqiDAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 420 SWRKHLSWVGQNPQ-LPAATLRDNV---LLARPDASEQELQAALDNAwvseflpLLPQGVDTPVGDQ----AARLSVGQA 491
Cdd:PRK14246 87 KLRKEVGMVFQQPNpFPHLSIYDNIaypLKSHGIKEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 492 QRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLAE-WDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
350-569 |
5.81e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.54 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFItSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRInGIELRdlspeswrkhLSWV 428
Cdd:COG0488 316 LELEGLSK-SYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEpDSGTVKL-GETVK----------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 429 GQNP-QL-PAATLRDNVLLARPDASEQELQAALdnawvSEFLpLLPQGVDTPVGDqaarLSVGQAQRVAVARALLNPCSL 506
Cdd:COG0488 384 DQHQeELdPDKTVLDELRDGAPGGTEQEVRGYL-----GRFL-FSGDDAFKPVGV----LSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 507 LLLDEPAASLDAHSeqrvMEALNAAsLRQ---TTLMVTHQ---LEDLAewDVIWVMQDGRIIE-QGRYAE 569
Cdd:COG0488 454 LLLDEPTNHLDIET----LEALEEA-LDDfpgTVLLVSHDryfLDRVA--TRILEFEDGGVREyPGGYDD 516
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
350-548 |
7.92e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.71 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSpeGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSLL------NALSGFLSYQGSLRINGIEL--RDLSPES 420
Cdd:PRK14243 11 LRTENLNVYY--GSFLAvKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVEGKVTFHGKNLyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 421 WRKHLSWVGQNPQLPAATLRDNVLL-ARPDASEQEL---------QAALdnaWvseflpllpQGVDTPVGDQAARLSVGQ 490
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYgARINGYKGDMdelverslrQAAL---W---------DEVKDKLKQSGLSLSGGQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 491 AQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVTHQLEDLA 548
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAA 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
363-573 |
8.42e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.92 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 363 KTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPA-ATLR 440
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 441 DnvLLARPDASEQEL--------QAALDNAW-VSEFLPLLPQGVDTpvgdqaarLSVGQAQRVAVARALLNPCSLLLLDE 511
Cdd:PRK10253 100 E--LVARGRYPHQPLftrwrkedEEAVTKAMqATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 512 PAASLDAHSEQRVMEALNAASLRQ--TTLMVTHQLEDLAEWDV-IWVMQDGRIIEQGRYAELSVA 573
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRYAShLIALREGKIVAQGAPKEIVTA 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
368-561 |
9.80e-09 |
|
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: 55.13 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 368 PLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKH-LSWVGQNPQ----LPAATLRD 441
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPpASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKreglVLDLSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 442 NVLLARpdaseqelqaaldnawvseflpllpqgvdtpvgdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSE 521
Cdd:cd03215 98 NIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446966322 522 QRVMEALNAASLRQTT-LMVTHQLEDLAEW-DVIWVMQDGRI 561
Cdd:cd03215 141 AEIYRLIRELADAGKAvLLISSELDELLGLcDRILVMYEGRI 182
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
369-565 |
1.07e-08 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 55.69 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSPEswRKHLSWVGQNPQL-PAATLRDNVLLA 446
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFDGKSYQKNIEA--LRRIGALIEAPGFyPNLTARENLRLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 RpdaseqeLQAALDNAWVSEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVME 526
Cdd:cd03268 97 A-------RLLGIRKKRIDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446966322 527 ALnaASLRQ---TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:cd03268 168 LI--LSLRDqgiTVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
369-543 |
1.08e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIEL-RDLSpeSWRKHLSWVGQNPQL-PAATLRDNVLL 445
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILFERQSIkKDLC--TYQKQLCFVGHRSGInPYLTLRENCLY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 446 arpdaseqELQAALDNAWVSEFLPLLPQG--VDTPVGdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQR 523
Cdd:PRK13540 98 --------DIHFSPGAVGITELCRLFSLEhlIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|.
gi 446966322 524 VMEALNAASLR-QTTLMVTHQ 543
Cdd:PRK13540 166 IITKIQEHRAKgGAVLLTSHQ 186
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
369-570 |
1.41e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.96 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLSPEswRKHLSWVGQNPQL-PAATLRDNVL-- 444
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDItSGDLFIGEKRMNDVPPA--ERGVGMVFQSYALyPHLSVAENMSfg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 --LARpdASEQELQAALDNawVSEFLPLlpqgvDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDA--HS 520
Cdd:PRK11000 100 lkLAG--AKKEEINQRVNQ--VAEVLQL-----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446966322 521 EQRVMEALNAASLRQTTLMVTH-QLEDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK11000 171 QMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
372-563 |
2.20e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.46 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 372 TLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESW---RKHLSWVGQNPqLPAATLRDNV--LL 445
Cdd:PRK10419 34 SLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAKLNRAQRkafRRDIQMVFQDS-ISAVNPRKTVreII 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 446 ARPDASEQELQAALDNAWVSEFLPLLpqGVDTPVGDQ-AARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRV 524
Cdd:PRK10419 113 REPLRHLLSLDKAERLARASEMLRAV--DLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446966322 525 MEALNAasLRQTT----LMVTHQLEdLAEW--DVIWVMQDGRIIE 563
Cdd:PRK10419 191 IRLLKK--LQQQFgtacLFITHDLR-LVERfcQRVMVMDNGQIVE 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
370-499 |
2.57e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.61 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRIngielrdlsPESWRkhLSWVGQNPQL-PAATLRDNV---- 443
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEpDSGEVSI---------PKGLR--IGYLPQEPPLdDDLTVLDTVldgd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 ------------LLARPDASEQ------ELQAALD--NAWVSEF--------LPLLPQGVDTPVGDqaarLSVGQAQRVA 495
Cdd:COG0488 87 aelraleaeleeLEAKLAEPDEdlerlaELQEEFEalGGWEAEAraeeilsgLGFPEEDLDRPVSE----LSGGWRRRVA 162
|
....
gi 446966322 496 VARA 499
Cdd:COG0488 163 LARA 166
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
363-570 |
2.78e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.58 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 363 KTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELrdlsPESWRKHLSWVGQNPQL----PAA 437
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLCGEPV----PSRARHARQRVGVVPQFdnldPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 438 TLRDNVLLArpdASEQELQAALDNAWVSEFLPL--LPQGVDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLDEPAAS 515
Cdd:PRK13537 96 TVRENLLVF---GRYFGLSAAAARALVPPLLEFakLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 516 LDAHSEQRVMEALNAASLR-QTTLMVTHQLEDlAE--WDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARgKTILLTTHFMEE-AErlCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
369-566 |
2.82e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQGSLRINGIELRDLSPES---WRKHLSWVGQNP-----------QL 434
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPnsslnprlnvlQI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 435 PAATLRDNVLLARPDASEQELQAALDNAwvseflpllpqGVDtPVGDQ--AARLSVGQAQRVAVARALLNPCSLLLLDEP 512
Cdd:PRK15134 385 IEEGLRVHQPTLSAAQREQQVIAVMEEV-----------GLD-PETRHryPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 513 AASLDAHSEQRVMEALNaaSLRQT----TLMVTHQLEDLAEW--DVIwVMQDGRIIEQGR 566
Cdd:PRK15134 453 TSSLDKTVQAQILALLK--SLQQKhqlaYLFISHDLHVVRALchQVI-VLRQGEVVEQGD 509
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
74-308 |
2.99e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 55.52 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 74 VLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLL 153
Cdd:cd18542 50 LLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 154 IVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASE 233
Cdd:cd18542 130 ALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENE 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 234 DFRQRTMEVLRLAFLSSGILEFFTSLSIALVAVYFGFSYL-GELDFGhydtgvTLAAgFLALILApeFFQPLRDLG 308
Cdd:cd18542 210 EYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVInGEITLG------ELVA-FISYLWM--LIWPVRQLG 276
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
344-571 |
4.17e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 344 LTDPLtIEAEDLFITSPEGKTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ---GSLRINGIELRDLSPES 420
Cdd:CHL00131 3 KNKPI-LEIKNLHASVNENEILKG-LNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKileGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 421 wRKHLswvG-----QNP-QLPAATLRDNVLLARPDASEQELQAALDNAwvsEFLPLLPQGVDTpVGDQAARL-------- 486
Cdd:CHL00131 81 -RAHL---GiflafQYPiEIPGVSNADFLRLAYNSKRKFQGLPELDPL---EFLEIINEKLKL-VGMDPSFLsrnvnegf 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 487 SVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNA-ASLRQTTLMVTH--QLEDLAEWDVIWVMQDGRIIE 563
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
....*...
gi 446966322 564 QGRyAELS 571
Cdd:CHL00131 233 TGD-AELA 239
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
368-570 |
8.35e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.64 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 368 PLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELR--DLSPESWRkhLSWVGQNP-----------Q 433
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDPstslnprqrisQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 434 LPAATLRDNVLLArPDASEQELQAALDNawvsefLPLLPqgvdtpvgDQAA----RLSVGQAQRVAVARALLNPCSLLLL 509
Cdd:PRK15112 109 ILDFPLRLNTDLE-PEQREKQIIETLRQ------VGLLP--------DHASyyphMLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446966322 510 DEPAASLDAHSEQRVMEALNAASLRQ--TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADV 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
363-565 |
8.51e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.20 E-value: 8.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 363 KTLAGpLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESW---RKHLSWVGQNPQlpaAT 438
Cdd:PRK11308 29 KALDG-VSFTLERGKTLAVVGESGCGKSTLARLLTMIETpTGGELYYQGQDLLKADPEAQkllRQKIQIVFQNPY---GS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 439 L--RDNV--LLARPDASEQELQAALDNAWVSEFLpllpqgvdTPVG---DQAAR----LSVGQAQRVAVARALLNPCSLL 507
Cdd:PRK11308 105 LnpRKKVgqILEEPLLINTSLSAAERREKALAMM--------AKVGlrpEHYDRyphmFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 508 LLDEPAASLDAHSEQRVMEALnaASLRQ----TTLMVTHQL---EDLAEwDVIwVMQDGRIIEQG 565
Cdd:PRK11308 177 VADEPVSALDVSVQAQVLNLM--MDLQQelglSYVFISHDLsvvEHIAD-EVM-VMYLGRCVEKG 237
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
369-544 |
8.57e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGF-LSYQGSLRINGIELRDLSPES---WRKHLSWVGQNPQLPA-ATLRDNV 443
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMdRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LL------ARPDASEQELQAALDNawvsefLPLLPQGVDTPVgdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:PRK10908 101 AIpliiagASGDDIRRRVSAALDK------VGLLDKAKNFPI-----QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190
....*....|....*....|....*....|
gi 446966322 518 -AHSEQ--RVMEALNAASLrqTTLMVTHQL 544
Cdd:PRK10908 170 dALSEGilRLFEEFNRVGV--TVLMATHDI 197
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
350-398 |
9.58e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 51.30 E-value: 9.58e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446966322 350 IEAEDLFITSpEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSG 398
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG 48
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
350-543 |
1.29e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 54.75 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRIngielrdlsPEswRKHLSWV 428
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPvYGGRLTK---------PA--KGKLFYV 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 429 GQNPQLPAATLRDNVL-------LARPDASEQELQAALDNAWVSEflpLLPQGVD-TPVGDQAARLSVGQAQRVAVARAL 500
Cdd:TIGR00954 521 PQRPYMTLGTLRDQIIypdssedMKRRGLSDKDLEQILDNVQLTH---ILEREGGwSAVQDWMDVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446966322 501 LNPCSLLLLDEPAASLDAHSEQRVMEalNAASLRQTTLMVTHQ 543
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMYR--LCREFGITLFSVSHR 638
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
375-570 |
1.67e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.66 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 375 AGQRAVLVGRSGSGKSSLLNALSgFLSY--QGSLRINGIELRDLSP-------------ESWRKHLSWVGQNPQLPA-AT 438
Cdd:PRK10619 30 AGDVISIIGSSGSGKSTFLRCIN-FLEKpsEGSIVVNGQTINLVRDkdgqlkvadknqlRLLRTRLTMVFQHFNLWShMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 439 LRDNVLlarpDASEQELQAALDNAWVSEFLPLLPQGVDTPV-GDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:PRK10619 109 VLENVM----EAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 518 AH---SEQRVMEALnaASLRQTTLMVTHQLE--DLAEWDVIWVMQdGRIIEQGRYAEL 570
Cdd:PRK10619 185 PElvgEVLRIMQQL--AEEGKTMVVVTHEMGfaRHVSSHVIFLHQ-GKIEEEGAPEQL 239
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
369-570 |
1.97e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.21 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQG-----SLRINGIELRDLSPESWRK----HLSWVGQNPQL---PA 436
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaeKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPMTslnPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 437 ATLRDNVLLA----RPDASEQELQAALDnawvseflpLLPQgVDTPvgDQAARLSV-------GQAQRVAVARALLNPCS 505
Cdd:PRK11022 106 YTVGFQIMEAikvhQGGNKKTRRQRAID---------LLNQ-VGIP--DPASRLDVyphqlsgGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 506 LLLLDEPAASLDAHSEQRVMEALNAASLRQTT--LMVTHQLEDLAE-WDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
354-566 |
2.71e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 354 DLFITSPEGKTLAGPLNFTLPAGQRAVLvGRSGSGKSSLLNALSGFL---SYQGSLRINGielRDLSPESWRKhLSWVGQ 430
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVL-GPSGSGKSTLLNALAGRIqgnNFTGTILANN---RKPTKQILKR-TGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 431 NPQL-PAATLRDNV----LLARPDASEQELQAALDNAWVSEFLplLPQGVDTPVGDQAAR-LSVGQAQRVAVARALLNPC 504
Cdd:PLN03211 148 DDILyPHLTVRETLvfcsLLRLPKSLTKQEKILVAESVISELG--LTKCENTIIGNSFIRgISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 505 SLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMVT-HQLED--LAEWDVIWVMQDGRIIEQGR 566
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSrvYQMFDSVLVLSEGRCLFFGK 290
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
381-570 |
2.88e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.32 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 381 LVGRSGSGKSSLLNALSGFLSYQGSLRING-----------IELRDLspeswRKHLSWVGQNP--QLPAATLRDNVLLAR 447
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipanlkkiKEVKRL-----RKEIGLVFQFPeyQLFQETIEKDIAFGP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 448 PDASEQELQAALDnawVSEFLPL--LPQgvdtpvgDQAAR----LSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSE 521
Cdd:PRK13645 117 VNLGENKQEAYKK---VPELLKLvqLPE-------DYVKRspfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446966322 522 QRVM---EALNaASLRQTTLMVTHQLED-LAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK13645 187 EDFInlfERLN-KEYKKRIIMVTHNMDQvLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
370-570 |
4.17e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.02 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSPESWRKHLSWVGQNPQLPAATL--RDNV--L 444
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVkATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLnpRMTIgeI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 LA------RPDASEQELQAALDNAWVSefLPLLPQGVDT-PvgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:PRK15079 121 IAeplrtyHPKLSRQEVKDRVKAMMLK--VGLLPNLINRyP-----HEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 518 AHSEQRVMEALNAASlRQTTLMVTHQLEDLAE----WDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK15079 194 VSIQAQVVNLLQQLQ-REMGLSLIFIAHDLAVvkhiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
74-311 |
5.47e-07 |
|
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: 51.70 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 74 VLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDyyaryLPQMALAVSVP-- 151
Cdd:cd18545 51 LVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSD-----LLSNGLINLIPdl 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 152 ---LLIVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESI 228
Cdd:cd18545 126 ltlVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 229 RSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVaVYFGFSYL--GELDFGhydtgvTLAAgFLALIlaPEFFQPLRD 306
Cdd:cd18545 206 DELNRENRKANMRAVRLNALFWPLVELISALGTALV-YWYGGKLVlgGAITVG------VLVA-FIGYV--GRFWQPIRN 275
|
....*
gi 446966322 307 LGTFY 311
Cdd:cd18545 276 LSNFY 280
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
362-565 |
6.17e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 50.34 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 362 GKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSG----FLSYQGSLRINGIELrDLSPESWRKHLSWVGQN----PQ 433
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSVEGDIHYNGIPY-KEFAEKYPGEIIYVSEEdvhfPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 434 LPAATLRDNVLLARpdaseqelqaaldnawvseflpllpqgvdtpvGDQAAR-LSVGQAQRVAVARALLNPCSLLLLDEP 512
Cdd:cd03233 98 LTVRETLDFALRCK--------------------------------GNEFVRgISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 513 AASLDAHSeqrVMEALN-----AASLRQTTLMVTHQ--LEDLAEWDVIWVMQDGRIIEQG 565
Cdd:cd03233 146 TRGLDSST---ALEILKcirtmADVLKTTTFVSLYQasDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
143-269 |
6.71e-07 |
|
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: 51.25 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 143 QMAL--AVSVPLLIVVAI---FPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRI 217
Cdd:cd18548 114 MMLLrmLVRAPIMLIGAIimaFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRA 193
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446966322 218 FGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVaVYFG 269
Cdd:cd18548 194 FNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI-LWFG 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
334-570 |
9.44e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.57 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 334 HPQRG--EAELALTDPLTIEAEDLFITSPEGktlagplNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRING 410
Cdd:PRK10070 17 HPQRAfkYIEQGLSKEQILEKTGLSLGVKDA-------SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 411 IELRDLSP----ESWRKHLSWVGQNPQL-PAATLRDNVLLARPDA---SEQELQAALDnawvseflPLLPQGVDTPVGDQ 482
Cdd:PRK10070 90 VDIAKISDaelrEVRRKKIAMVFQSFALmPHMTVLDNTAFGMELAginAEERREKALD--------ALRQVGLENYAHSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 483 AARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNA--ASLRQTTLMVTHQL-EDLAEWDVIWVMQDG 559
Cdd:PRK10070 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNG 241
|
250
....*....|.
gi 446966322 560 RIIEQGRYAEL 570
Cdd:PRK10070 242 EVVQVGTPDEI 252
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
360-561 |
1.14e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 360 PEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGflsyqgslringiELRDLSPESWR--KHLSWVGQNPQLPAA 437
Cdd:PLN03073 519 PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG-------------ELQPSSGTVFRsaKVRMAVFSQHHVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 438 TLRDNVLL----ARPDASEQELQAALDNAWVSEFLPLLPQgvdtpvgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPA 513
Cdd:PLN03073 586 DLSSNPLLymmrCFPGVPEQKLRAHLGSFGVTGNLALQPM----------YTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446966322 514 ASLDAHSEQRVMEALnaASLRQTTLMVTHQlEDL--AEWDVIWVMQDGRI 561
Cdd:PLN03073 656 NHLDLDAVEALIQGL--VLFQGGVLMVSHD-EHLisGSVDELWVVSEGKV 702
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
381-587 |
1.22e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.59 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 381 LVGRSGSGKSSLLNALSGF----LSYQGSLRINGielRDLSPESWRKHLSWVGQNPQ-LPAATLRDNVL------LARPD 449
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRspkgVKGSGSVLLNG---MPIDAKEMRAISAYVQQDDLfIPTLTVREHLMfqahlrMPRRV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 450 ASEQELQAaldnawVSEFLPL--LPQGVDTPVGD--QAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVM 525
Cdd:TIGR00955 133 TKKEKRER------VDEVLQAlgLRKCANTRIGVpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 526 EAL-NAASLRQTTLMVTHQ----LEDLaeWDVIWVMQDGRIIEQGRYAELSvaggPFATLLAHRQEE 587
Cdd:TIGR00955 207 QVLkGLAQKGKTIICTIHQpsseLFEL--FDKIILMAEGRVAYLGSPDQAV----PFFSDLGHPCPE 267
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
348-573 |
1.41e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.57 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 348 LTIEaedlFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-----YQGSLRINGIELRDLSPESWR 422
Cdd:PRK15093 9 LTIE----FKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrvTADRMRFDDIDLLRLSPRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 423 K----HLSWVGQNPQL---PAATLRDNVLLARPDASEQelqaaldNAWVSEF-------LPLLPQ-GVDTP---VGDQAA 484
Cdd:PRK15093 85 KlvghNVSMIFQEPQScldPSERVGRQLMQNIPGWTYK-------GRWWQRFgwrkrraIELLHRvGIKDHkdaMRSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 485 RLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALnaASLRQ----TTLMVTHQLEDLAEW-DVIWVMQDG 559
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLL--TRLNQnnntTILLISHDLQMLSQWaDKINVLYCG 235
|
250
....*....|....
gi 446966322 560 RIIEQGRYAELSVA 573
Cdd:PRK15093 236 QTVETAPSKELVTT 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
337-565 |
1.52e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.55 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 337 RGEAELALTDPLTIEAED----------------------------LFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSG 388
Cdd:TIGR01257 889 REERALEKTEPLTEEMEDpehpegindsfferelpglvpgvcvknlVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAG 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 389 KSSLLNALSGFLS-YQGSLRINGIELrDLSPESWRKHLSWVGQ-NPQLPAATLRDNVLLARP------DASEQELQAALD 460
Cdd:TIGR01257 969 KTTTLSILTGLLPpTSGTVLVGGKDI-ETNLDAVRQSLGMCPQhNILFHHLTVAEHILFYAQlkgrswEEAQLEMEAMLE 1047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 461 NAwvseflpllpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMV 540
Cdd:TIGR01257 1048 DT-----------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMS 1116
|
250 260
....*....|....*....|....*..
gi 446966322 541 THQLE--DLAEwDVIWVMQDGRIIEQG 565
Cdd:TIGR01257 1117 THHMDeaDLLG-DRIAIISQGRLYCSG 1142
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
361-564 |
1.55e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.61 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 361 EGKTLA-GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS------YQGSLRINGIELRDlspeswrKHLSWVGQNPQ 433
Cdd:PRK11650 14 DGKTQViKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERitsgeiWIGGRVVNELEPAD-------RDIAMVFQNYA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 434 L-PAATLRDNV---LLARPDASEQELQAALDNAWVSEFLPLLpqgvdtpvgDQAAR-LSVGQAQRVAVARALLNPCSLLL 508
Cdd:PRK11650 87 LyPHMSVRENMaygLKIRGMPKAEIEERVAEAARILELEPLL---------DRKPReLSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 509 LDEPAASLDAhseqrvmeALNAA----------SLRQTTLMVTH-QLE--DLAewDVIWVMQDGRiIEQ 564
Cdd:PRK11650 158 FDEPLSNLDA--------KLRVQmrleiqrlhrRLKTTSLYVTHdQVEamTLA--DRVVVMNGGV-AEQ 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
350-571 |
2.50e-06 |
|
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: 50.19 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 350 IEAEDLfITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-------------------------- 403
Cdd:TIGR03269 1 IEVKNL-TKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsgriiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 404 -------GSLRINGIELRDLSPESWRKHLSWVGQNPQLPAA-----TLRDNVLLARPDAsEQELQAALDNAwvsefLPLL 471
Cdd:TIGR03269 80 epcpvcgGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFAlygddTVLDNVLEALEEI-GYEGKEAVGRA-----VDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 472 PQ-GVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMV-----THQLE 545
Cdd:TIGR03269 154 EMvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVltshwPEVIE 233
|
250 260
....*....|....*....|....*.
gi 446966322 546 DLAEWdVIWvMQDGRIIEQGRYAELS 571
Cdd:TIGR03269 234 DLSDK-AIW-LENGEIKEEGTPDEVV 257
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
369-562 |
2.78e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.21 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL---SYQGSLRINGIEL-----RD--------------LSPESWRKHLS 426
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgTWDGEIYWSGSPLkasniRDteragiviihqeltLVPELSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 427 WVGQNPQLPAATLRDNVLLARPDASEQELQAALDNawvseflpllpqgVDTPVGDqaarLSVGQAQRVAVARALLNPCSL 506
Cdd:TIGR02633 100 FLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADN-------------VTRPVGD----YGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 507 LLLDEPAASLDAHSEQRVMEALNAASLRQTT-LMVTHQLEDL-AEWDVIWVMQDGRII 562
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDLKAHGVAcVYISHKLNEVkAVCDTICVIRDGQHV 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
349-428 |
3.09e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.97 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 349 TIEAEDLFITSPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSG-FLSYQGSLRINGIELRDLSPESWRKHLSW 427
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
.
gi 446966322 428 V 428
Cdd:PRK10522 402 V 402
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
147-269 |
4.33e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 48.56 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 147 AVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIE 226
Cdd:cd18541 124 ALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIE 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446966322 227 SIRSASEDFRQRTMEVLRL-AFLSSgILEFFTSLSIALVaVYFG 269
Cdd:cd18541 204 RFDKLNEEYVEKNLRLARVdALFFP-LIGLLIGLSFLIV-LWYG 245
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
72-317 |
4.65e-06 |
|
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: 48.72 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 72 TFVLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVP 151
Cdd:cd18565 63 AFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 152 LLIVVAIFPSNWAAALILLGTAPLIpLFMALVGMGAA----DANRRnflALARLSGHFLDRLRGMETLRIFGRGEAEIES 227
Cdd:cd18565 143 LGIGAILFYLNWQLALVALLPVPLI-IAGTYWFQRRIepryRAVRE---AVGDLNARLENNLSGIAVIKAFTAEDFERER 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 228 IRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVAVYFGFSYLgeldFGHYDTGVTLAAGFLA--LILAPEFFQPLR 305
Cdd:cd18565 219 VADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVL----DGPPLFTGTLTVGTLVtfLFYTQRLLWPLT 294
|
250
....*....|....*.
gi 446966322 306 DLG----TFYHAKAQA 317
Cdd:cd18565 295 RLGdlidQYQRAMASA 310
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
370-573 |
7.03e-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: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFlsYQ---GSLRINGIELRDLSPESWRKH-LSWVGQNPQL-PAATLRDNVL 444
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGL--YQpdsGEILIDGKPVRIRSPRDAIALgIGMVHQHFMLvPNLTVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 LARPD---------ASEQELQAALDnawvsEF-LPLLPqgvDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLDEPAA 514
Cdd:COG3845 103 LGLEPtkggrldrkAARARIRELSE-----RYgLDVDP---DAKVED----LSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 515 SL-DAHSEQ--RVMEALNAASLrqTTLMVTHQLE---DLAewDVIWVMQDGRIIEQGRYAELSVA 573
Cdd:COG3845 171 VLtPQEADElfEILRRLAAEGK--SIIFITHKLRevmAIA--DRVTVLRRGKVVGTVDTAETSEE 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
369-570 |
7.55e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKS----SLLNAL-SGFLSY-QGSLRINGIELRDLSPESWRK----HLSWVGQNPQL---P 435
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYpSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMVslnP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 436 AATLRDN---VLL----ARPDASEQELQAALDNAWVSEFLPLLpqgvdtpvGDQAARLSVGQAQRVAVARALLNPCSLLL 508
Cdd:PRK15134 108 LHTLEKQlyeVLSlhrgMRREAARGEILNCLDRVGIRQAAKRL--------TDYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446966322 509 LDEPAASLDAHSEQRVMEALNaaSLRQ----TTLMVTHQL---EDLAewDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLR--ELQQelnmGLLFITHNLsivRKLA--DRVAVMQNGRCVEQNRAATL 244
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
141-307 |
8.07e-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: 47.78 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 141 LPQMALAVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGR 220
Cdd:cd18547 123 LTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 221 GEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVAVYFGFSYL-GELDFGhydtgvTLAAgFlaLILAPE 299
Cdd:cd18547 203 EEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVInGALTVG------VIQA-F--LQYSRQ 273
|
....*...
gi 446966322 300 FFQPLRDL 307
Cdd:cd18547 274 FSQPINQI 281
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
381-550 |
8.52e-06 |
|
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: 48.78 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 381 LVGRSGSGKSSLLnalsgflsyqgslRI-NGIElRDLSPESWRKHLSWVG---QNPQL-PAATLRDNV------------ 443
Cdd:TIGR03719 36 VLGLNGAGKSTLL-------------RImAGVD-KDFNGEARPQPGIKVGylpQEPQLdPTKTVRENVeegvaeikdald 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 -------LLARPDA------SEQ-ELQAALD--NAWvsEFLPLLPQGVDT---PVGDQ-AARLSVGQAQRVAVARALLNP 503
Cdd:TIGR03719 102 rfneisaKYAEPDAdfdklaAEQaELQEIIDaaDAW--DLDSQLEIAMDAlrcPPWDAdVTKLSGGERRRVALCRLLLSK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446966322 504 CSLLLLDEPAASLDAHS----EQRVMEalnaasLRQTTLMVTHQ---LEDLAEW 550
Cdd:TIGR03719 180 PDMLLLDEPTNHLDAESvawlERHLQE------YPGTVVAVTHDryfLDNVAGW 227
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
369-565 |
9.18e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.51 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL---------SYQGSLRINGIELRDLSPESWRKHLSWVGQNPQLP-AAT 438
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAfAFS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 439 LRDNVLLAR-PDASEQELQAALDNAWVSEFLPLlpQGVDTPVGDQAARLSVGQAQRVAVARA---------LLNPCSLLL 508
Cdd:PRK13547 100 AREIVLLGRyPHARRAGALTHRDGEIAWQALAL--AGATALVGRDVTTLSGGELARVQFARVlaqlwpphdAAQPPRYLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 509 LDEPAASLDAHSEQRVMEALNAAS--LRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:PRK13547 178 LDEPTAALDLAHQHRLLDTVRRLArdWNLGVLAIVHDPNLAARHaDRIAMLADGAIVAHG 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
369-565 |
1.16e-05 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 46.50 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSG-FLSYQGSLRINGielRDLSPESWRKhlswVGQNPQ----LPAATLRDNV 443
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPDSGEVLFDG---KPLDIAARNR----IGYLPEerglYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 L-LAR-PDASEQELQAALDNaWVSEFlpllpqgvdtPVGDQAAR----LSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:cd03269 92 VyLAQlKGLKKEEARRRIDE-WLERL----------ELSEYANKrveeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446966322 518 AHSEQRVMEALNAASLRQTT-LMVTHQLEDLAEW-DVIWVMQDGRIIEQG 565
Cdd:cd03269 161 PVNVELLKDVIRELARAGKTvILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
486-565 |
1.30e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 486 LSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLR-QTTLMVTHQLEDLAEWD--VIwVMQDGRII 562
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTkrTI-FFKDGKII 244
|
...
gi 446966322 563 EQG 565
Cdd:PRK13651 245 KDG 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
351-498 |
2.58e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.94 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 351 EAEDLFITSPEGKTLAGPLNFTLPAGQraVL--VGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSPESWRKH-LS 426
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGE--ILgiAGVAGNGQSELAEALAGLRPPAsGSIRLDGEDITGLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 427 WVGQNPQ----LPAATLRDNVLLARPDASEQ------ELQAALDNA--WVSEFlpllpqGVDTPVGDQAAR-LSVGQAQR 493
Cdd:COG3845 337 YIPEDRLgrglVPDMSVAENLILGRYRRPPFsrggflDRKAIRAFAeeLIEEF------DVRTPGPDTPARsLSGGNQQK 410
|
....*
gi 446966322 494 VAVAR 498
Cdd:COG3845 411 VILAR 415
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
381-570 |
2.86e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.15 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 381 LVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELrDLSPE---SWRKHLSWVGQNP--QLPAATLRDNVLLARPD--ASE 452
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRpQKGAVLWQGKPL-DYSKRgllALRQQVATVFQDPeqQIFYTDIDSDIAFSLRNlgVPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 453 QELQAALDNAWvseflpllpqgvdTPVGDQAAR------LSVGQAQRVAVARALLNPCSLLLLDEPAASLD-AHSEQRVM 525
Cdd:PRK13638 111 AEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpAGRTQMIA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446966322 526 EALNAASLRQTTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK13638 178 IIRRIVAQGNHVIISSHDIDLIYEIsDAVYVLRQGQILTHGAPGEV 223
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
380-469 |
3.12e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 46.11 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 380 VLVGRSGSGKSSLLNALSGFLS----YQGSLRINgieLRDLSPESWRKHlSWVGQNPQLPAATLRDNVLLARPDASEQEL 455
Cdd:COG4938 24 LLIGPNGSGKSTLIQALLLLLQsnfiYLPAERSG---PARLYPSLVREL-SDLGSRGEYTADFLAELENLEILDDKSKEL 99
|
90
....*....|....
gi 446966322 456 QAALdNAWVSEFLP 469
Cdd:COG4938 100 LEQV-EEWLEKIFP 112
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
370-570 |
5.74e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.98 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSGFlsYQ---GSLRINGIELRDL-SPESWRKHLSWVGQNPQL-PAATLRDNVL 444
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGF--YKptgGTILLRGQHIEGLpGHQIARMGVVRTFQHVRLfREMTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 LAR---------------PDASEQElQAALDNA--WVsEFLPLLPQgvdtpVGDQAARLSVGQAQRVAVARALLNPCSLL 507
Cdd:PRK11300 103 VAQhqqlktglfsgllktPAFRRAE-SEALDRAatWL-ERVGLLEH-----ANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 508 LLDEPAASLDAHsEQRVMEALnAASLRQ----TTLMVTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK11300 176 MLDEPAAGLNPK-ETKELDEL-IAELRNehnvTVLLIEHDMKLVMGIsDRIYVVNQGTPLANGTPEEI 241
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
369-550 |
5.94e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.56 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQGSLRINGIELRDLSPE-SWRKHLSWVGQNPQ----LPAATLRDNV 443
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREaSLIDAIGRKGDFKDavelLNAVGLSDAV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LLARPdaseqelqaaldnawVSEflpllpqgvdtpvgdqaarLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQR 523
Cdd:COG2401 129 LWLRR---------------FKE-------------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180 190
....*....|....*....|....*....|.
gi 446966322 524 VmeALNAASL---RQTTLMV-THQlEDLAEW 550
Cdd:COG2401 175 V--ARNLQKLarrAGITLVVaTHH-YDVIDD 202
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
130-264 |
6.01e-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: 45.16 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 130 IDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILLG----TAPLIPLFMALVGMGAADANRRnflALARLSGHF 205
Cdd:cd18585 102 IDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAglllAGVVIPLLFYRLGKKIGQQLVQ---LRAELRTEL 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446966322 206 LDRLRGMETLRIFGRGEAEIESIRSASEDF--RQRTMEvlRLAFLSSGILEFFTSLSIALV 264
Cdd:cd18585 179 VDGLQGMAELLIFGALERQRQQLEQLSDALikEQRRLA--RLSGLSQALMILLSGLTVWLV 237
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
368-565 |
7.58e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 368 PLNFTLPAGQRAVLVGRSGSGKSSLLNALS----GFL-SYQGSLRINGIELRDLSPEsWRKHLSWVGQNP-QLPAATLRD 441
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHiGVEGVITYDGITPEEIKKH-YRGDVVYNAETDvHFPHLTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 442 NVLLA--------RPDA-SEQELQAALDNAWVSEFLplLPQGVDTPVGDQAAR-LSVGQAQRVAVARALLNPCSLLLLDE 511
Cdd:TIGR00956 158 TLDFAarcktpqnRPDGvSREEYAKHIADVYMATYG--LSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 512 PAASLDAHSEQRVMEALN--AASLRQTTLMVTHQL-EDLAE-WDVIWVMQDGRIIEQG 565
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKtsANILDTTPLVAIYQCsQDAYElFDKVIVLYEGYQIYFG 293
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
359-568 |
9.33e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 359 SPEGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ---GSLRINGIELRDLSPESWRKHLSWVG-QNP-Q 433
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGTVEFKGKDLLELSPEDRAGEGIFMAfQYPvE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 434 LPAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPvGDQAAR-----LSVGQAQRVAVARALLNPCSLLL 508
Cdd:PRK09580 90 IPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMP-EDLLTRsvnvgFSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 509 LDEPAASLDAHSEQRVMEALNaaSLR---QTTLMVTH--QLEDLAEWDVIWVMQDGRIIEQGRYA 568
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVN--SLRdgkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFT 231
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
369-565 |
1.37e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.08 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALsgfLSYQGSLRINgielrDLSPESWRKHLSWVGQnpqlpaatlrdnvllarp 448
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLI-----SFLPKFSRNKLIFIDQ------------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 449 daseqeLQAALDNAWvsEFLPLlpqgvdtpvGDQAARLSVGQAQRVAVAR--ALLNPCSLLLLDEPAASLDAHSEQRVME 526
Cdd:cd03238 68 ------LQFLIDVGL--GYLTL---------GQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446966322 527 ALNaaSLRQ---TTLMVTHQLEDLAEWDVIWVM------QDGRIIEQG 565
Cdd:cd03238 131 VIK--GLIDlgnTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
369-570 |
1.69e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.60 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESW---RKHLSWVGQNPQL-PAATLRDNV 443
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIApDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALfTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 llARPDASEQELQAALDNAWVseFLPLLPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQ- 522
Cdd:PRK11831 106 --AYPLREHTQLPAPLLHSTV--MMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGv 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446966322 523 --RVMEALNAAsLRQTTLMVTHQL-EDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK11831 182 lvKLISELNSA-LGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
376-559 |
2.22e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 376 GQRAVLVGRSGSGKSSLLNALSGFLSY----QGSLRINGIELRdlspESWRKHLSWVGQNP-QLPAATLRDNV----LLA 446
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTgvitGGDRLVNGRPLD----SSFQRSIGYVQQQDlHLPTSTVRESLrfsaYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 RPdaseQELQAALDNAWVSEFLPLL--PQGVDTPVGDQAARLSVGQAQRVAVA-RALLNPCSLLLLDEPAASLDAHSEQR 523
Cdd:TIGR00956 865 QP----KSVSKSEKMEYVEEVIKLLemESYADAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDEPTSGLDSQTAWS 940
|
170 180 190
....*....|....*....|....*....|....*....
gi 446966322 524 VMEAL-NAASLRQTTLMVTHQ--LEDLAEWDVIWVMQDG 559
Cdd:TIGR00956 941 ICKLMrKLADHGQAILCTIHQpsAILFEEFDRLLLLQKG 979
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
378-398 |
2.92e-04 |
|
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: 40.68 E-value: 2.92e-04
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
375-398 |
3.85e-04 |
|
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: 42.00 E-value: 3.85e-04
10 20
....*....|....*....|....
gi 446966322 375 AGQRAVLVGRSGSGKSSLLNALSG 398
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
375-398 |
4.50e-04 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 42.41 E-value: 4.50e-04
10 20
....*....|....*....|....
gi 446966322 375 AGQRAVLVGRSGSGKSSLLNALSG 398
Cdd:COG1162 165 KGKTSVLVGQSGVGKSTLINALLP 188
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
367-517 |
5.40e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 41.76 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 367 GPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGielRDLSPESWRKHLSWVGQNPQLpaatlrdnvll 445
Cdd:PRK13543 28 GPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESGQIQIDG---KTATRGDRSRFMAYLGHLPGL----------- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 446 aRPDASEQELQAALdNAWVSEFLPLLPQGVDTPVG-----DQAAR-LSVGQAQRVAVARALLNPCSLLLLDEPAASLD 517
Cdd:PRK13543 94 -KADLSTLENLHFL-CGLHGRRAKQMPGSALAIVGlagyeDTLVRqLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
370-563 |
6.89e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 370 NFTLPAGQRAVLVGRSGSGKSSLLNALSG---FLSYQGSLRING--IELRDLSpESWRKHLSWVGQN----PQLPAAtlr 440
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSGvypHGSYEGEILFDGevCRFKDIR-DSEALGIVIIHQElaliPYLSIA--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 441 DNVLLARPDAS-------EQELQAA--LDNAWVSEflplLPqgvDTPVGDqaarLSVGQAQRVAVARALLNPCSLLLLDE 511
Cdd:NF040905 97 ENIFLGNERAKrgvidwnETNRRARelLAKVGLDE----SP---DTLVTD----IGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 512 PAASLDAHSEQRVMEALnaASLRQ---TTLMVTHQLEDLAE-WDVIWVMQDGRIIE 563
Cdd:NF040905 166 PTAALNEEDSAALLDLL--LELKAqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
381-550 |
6.99e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 381 LVGRSGSGKSSLLnalsgflsyqgslRI-NGIElRDLSPESWRKHLSWVG---QNPQL-PAATLRDNV---------LLA 446
Cdd:PRK11819 38 VLGLNGAGKSTLL-------------RImAGVD-KEFEGEARPAPGIKVGylpQEPQLdPEKTVRENVeegvaevkaALD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 447 R----------PDA------SEQ-ELQAALD--NAWVSEflPLLPQGVD---TPVGDQA-ARLSVGQAQRVAVARALLNP 503
Cdd:PRK11819 104 RfneiyaayaePDAdfdalaAEQgELQEIIDaaDAWDLD--SQLEIAMDalrCPPWDAKvTKLSGGERRRVALCRLLLEK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 504 CSLLLLDEPAASLDAHS----EQRvmealnaasLRQ---TTLMVTHQ---LEDLAEW 550
Cdd:PRK11819 182 PDMLLLDEPTNHLDAESvawlEQF---------LHDypgTVVAVTHDryfLDNVAGW 229
|
|
| TIGR00157 |
TIGR00157 |
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and ... |
354-403 |
7.89e-04 |
|
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and are now designated RsgA (ribosome small subunit-dependent GTPase A). The strongest motif in the alignment of these proteins is GXSGVGKS[ST], a classic P-loop for nucleotide binding. This protein has been shown to cleave GTP and remain bound to GDP. A role as a regulator of translation has been suggested. The Aquifex aeolicus ortholog is split into consecutive open reading frames. Consequently, this model was build in fragment mode (-f option). [Protein synthesis, Translation factors]
Pssm-ID: 272934 [Multi-domain] Cd Length: 245 Bit Score: 41.63 E-value: 7.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446966322 354 DLFITSPEGKTLAGPLnFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ 403
Cdd:TIGR00157 99 QVLMTSSKNQDGLKEL-IEALQNRISVFAGQSGVGKSSLINALDPSVKQQ 147
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
376-543 |
8.50e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 40.69 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 376 GQRAVLVGRSGSGKSSLLNALSGFL---SYQGSLRINGIELrdlsPESWRKHLSWVGQNP-QLPAATLRDNVllarpdas 451
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKtagVITGEILINGRPL----DKNFQRSTGYVEQQDvHSPNLTVREAL-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 452 eqELQAALdnawvseflpllpqgvdtpvgdqaaR-LSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEAL-N 529
Cdd:cd03232 101 --RFSALL-------------------------RgLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLkK 153
|
170
....*....|....
gi 446966322 530 AASLRQTTLMVTHQ 543
Cdd:cd03232 154 LADSGQAILCTIHQ 167
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
381-570 |
9.66e-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: 42.10 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 381 LVGRSGSGKSSLLNALSGFL---SYQGSLRING--IELRDLSPESWRKHLSWVG---QNPQL-PAATLRDNVL------- 444
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLeptSGEVNVRVGDewVDMTKPGPDGRGRAKRYIGilhQEYDLyPHRTVLDNLTeaiglel 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 445 ---LARPDASEQELQAALDNAWVSEFLPLLPQgvdtpvgdqaaRLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSE 521
Cdd:TIGR03269 395 pdeLARMKAVITLKMVGFDEEKAEEILDKYPD-----------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITK 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446966322 522 QRVMEALNAA--SLRQTTLMVTHQLEDLAE-WDVIWVMQDGRIIEQGRYAEL 570
Cdd:TIGR03269 464 VDVTHSILKAreEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEI 515
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
379-479 |
1.02e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 379 AVLVGRSGSGKSSLLNALSGFLSYQGSLRINGIELRDLSPESWrkhlSWVGQNPQLPAATLRDNVLLARPDASEQELQAA 458
Cdd:pfam13304 2 NVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGG----IPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLD 77
|
90 100
....*....|....*....|.
gi 446966322 459 LDNAWVSEFLPLLPQGVDTPV 479
Cdd:pfam13304 78 LEREDVEEKLSSKPTLLEKRL 98
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
162-310 |
1.02e-03 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 41.28 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 162 NWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTME 241
Cdd:cd18549 141 NVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKK 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446966322 242 VLR-LAFLSSGIlEFFTSLsIALVAVYFG--FSYLGELDFGhydtgvTLAAgFLALILApeFFQPLRDLGTF 310
Cdd:cd18549 221 AYKaMAYFFSGM-NFFTNL-LNLVVLVAGgyFIIKGEITLG------DLVA-FLLYVNV--FIKPIRRLVNF 281
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
371-517 |
1.43e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.47 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 371 FTLPAGQRAVLVGRSGSGKSSLLNALS-------GFLSYQGSLRINGIEL---RDLSPESWrkhlSWVGQNPQLPAATLR 440
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNgevllddGRIIYEQDLIVARLQQdppRNVEGTVY----DFVAEGIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 441 D----NVLLARpDASE------QELQAALD--NAW-----VSEFLPLLPQGVDTPVGDqaarLSVGQAQRVAVARALLNP 503
Cdd:PRK11147 100 RyhdiSHLVET-DPSEknlnelAKLQEQLDhhNLWqlenrINEVLAQLGLDPDAALSS----LSGGWLRKAALGRALVSN 174
|
170
....*....|....
gi 446966322 504 CSLLLLDEPAASLD 517
Cdd:PRK11147 175 PDVLLLDEPTNHLD 188
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
363-570 |
1.45e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 363 KTLAGPlNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLS-YQGSLRINGIELRDLSPESWRKHLSWVGQnpqlpaatlRD 441
Cdd:PRK10938 17 KTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPlLSGERQSQFSHITRLSFEQLQKLVSDEWQ---------RN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 442 NVLLARPD-------ASEQELQAALDNAWVSEFLPLLpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAA 514
Cdd:PRK10938 87 NTDMLSPGeddtgrtTAEIIQDEVKDPARCEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 515 SLDAHSEQRVMEALNAASLRQTTLM-VTHQLEDLAEW-DVIWVMQDGRIIEQGRYAEL 570
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDFvQFAGVLADCTLAETGEREEI 222
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
375-411 |
1.52e-03 |
|
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: 39.83 E-value: 1.52e-03
10 20 30
....*....|....*....|....*....|....*..
gi 446966322 375 AGQRAVLVGRSGSGKSSLLNALSGflsyQGSLRINGI 411
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLP----ELDLRTGEI 137
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
369-517 |
1.54e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.38 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQ-GSLRINGIELRDLSP---ESWRKHLSWVGQNPQL---PAATLRD 441
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYAsldPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 442 NVLLA-RPDASEQELQAALDNAWVSEFLPLLPQgvdtpvgdQAAR----LSVGQAQRVAVARALLNPCSLLLLDEPAASL 516
Cdd:PRK10261 423 SIMEPlRVHGLLPGKAAAARVAWLLERVGLLPE--------HAWRypheFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
.
gi 446966322 517 D 517
Cdd:PRK10261 495 D 495
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
89-297 |
1.55e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 40.92 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 89 HAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPL-LIVVAiFPSNWAAAL 167
Cdd:cd18577 73 ITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIaGFIIA-FIYSWKLTL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 168 ILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESirsasedFRQRTMEVLRLAF 247
Cdd:cd18577 152 VLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKR-------YSKALEKARKAGI 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446966322 248 -------LSSGILEFFTSLSIALvAVYFGfSYLgeLDFGHYDTGVTLAAGFLALILA 297
Cdd:cd18577 225 kkglvsgLGLGLLFFIIFAMYAL-AFWYG-SRL--VRDGEISPGDVLTVFFAVLIGA 277
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
141-322 |
1.93e-03 |
|
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: 40.49 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 141 LPQMALAVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGR 220
Cdd:cd18551 114 LPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 221 GEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVAVYFGfsYL---GELDFGhydtgvTLAAgFLALIla 297
Cdd:cd18551 194 EERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGG--ARvasGALTVG------TLVA-FLLYL-- 262
|
170 180
....*....|....*....|....*...
gi 446966322 298 pefFQ---PLRDLGTFYHAKAQAVGAAD 322
Cdd:cd18551 263 ---FQlitPLSQLSSFFTQLQKALGALE 287
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
376-441 |
2.03e-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: 38.89 E-value: 2.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446966322 376 GQRAVLVGRSGSGKSSLLNALSGFLSYQGS--LRINGIELRDLSPESWRKHLSWVGQNPQLPAATLRD 441
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGgvIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRL 69
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
376-398 |
2.05e-03 |
|
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: 39.01 E-value: 2.05e-03
10 20
....*....|....*....|...
gi 446966322 376 GQRAVLVGRSGSGKSSLLNALSG 398
Cdd:cd04164 3 GIKVVIAGKPNVGKSSLLNALAG 25
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
380-398 |
2.44e-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: 38.98 E-value: 2.44e-03
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
369-561 |
2.68e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.58 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL--SYQGSLRING--IELRD----------LSPESWRKH----LSWVGQ 430
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYpgKFEGNVFINGkpVDIRNpaqairagiaMVPEDRKRHgivpILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 431 NPQLpaATLRDNVLLARPDAS--EQELQAALDNAWVSEFLPLLPQGvdtpvgdqaaRLSVGQAQRVAVARALLNPCSLLL 508
Cdd:TIGR02633 359 NITL--SVLKSFCFKMRIDAAaeLQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446966322 509 LDEPAASLDAHSEQRVMEALNAASLRQTTL-MVTHQL-EDLAEWDVIWVMQDGRI 561
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQEGVAIiVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
376-578 |
2.69e-03 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 39.70 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 376 GQRAVLVGRSGSGKSSLLNALSGflsyqgslrinGIELRDLSPESWRKHLSWvgqNPQLPAA----TLRDnvLLARPDAS 451
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAG-----------VLKPDEGDIEIELDTVSY---KPQYIKAdyegTVRD--LLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 452 eqelqAALDNAWVSEFLPllPQGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDahSEQRVME----- 526
Cdd:cd03237 89 -----FYTHPYFKTEIAK--PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMAskvir 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 527 --ALNAaslRQTTLMVTHqledlaewDVIWV--MQDGRIIEQGRYAELSVAGGPFA 578
Cdd:cd03237 160 rfAENN---EKTAFVVEH--------DIIMIdyLADRLIVFEGEPSVNGVANPPQS 204
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
369-570 |
2.77e-03 |
|
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: 39.83 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSY-QGSLRINGIELRDLsPESWRKHLSwVGQNPQLPAA----TLRDNV 443
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGKILLDGQDITKL-PMHKRARLG-IGYLPQEASIfrklTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 444 LLA---RPDASEQELQAAldNAWVSEFlpllpqGVDTPVGDQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHS 520
Cdd:cd03218 97 LAVleiRGLSKKEREEKL--EELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446966322 521 EQRVMEALNAASLRQTTLMVT-HQL-EDLAEWDVIWVMQDGRIIEQGRYAEL 570
Cdd:cd03218 169 VQDIQKIIKILKDRGIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
369-544 |
3.42e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 39.71 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 369 LNFTLPAGQRAVLVGRSGSGKSSLLNAL-------SGFLSYQGSLRINGIelrdlsPEswRKHLswvgqNPQLPAATLRd 441
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVlglvapdEGVIKRNGKLRIGYV------PQ--KLYL-----DTTLPLTVNR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 442 nVLLARPDASEQELQAALDNAWVSEFLpllpqgvDTPVgdqaARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSE 521
Cdd:PRK09544 89 -FLRLRPGTKKEDILPALKRVQAGHLI-------DAPM----QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....*..
gi 446966322 522 QRVMEALNaaSLRQT----TLMVTHQL 544
Cdd:PRK09544 157 VALYDLID--QLRREldcaVLMVSHDL 181
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
375-398 |
4.04e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 39.42 E-value: 4.04e-03
10 20
....*....|....*....|....
gi 446966322 375 AGQRAVLVGRSGSGKSSLLNALSG 398
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTLLNALAP 186
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
380-398 |
4.15e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 38.38 E-value: 4.15e-03
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
380-396 |
5.95e-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: 37.88 E-value: 5.95e-03
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
363-553 |
5.98e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.72 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 363 KTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSgflsyqgslringielrdlspeswrkhlswvgqnpqlpAATLRDN 442
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG--------------------------------------LALGGAQ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 443 VLLARPDASEQELQAALDNAwvsEFLPLLPQgvdtpvgdqaarLSVGQAQRVAVA----RALLNPCSLLLLDEPAASLDA 518
Cdd:cd03227 50 SATRRRSGVKAGCIVAAVSA---ELIFTRLQ------------LSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 446966322 519 HSEQRVMEALNAASLRQTTLMV-THQLEDLAEWDVI 553
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIViTHLPELAELADKL 150
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
147-307 |
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 446966322 147 AVSVPLLIVVAIFPSNWAAALILLGTAPliplFMALVGMgaadANRRNFLALAR--------LSGHFLDRLRGMETLRIF 218
Cdd:cd18540 126 GITYMIGILIVMLILNWKLALIVLAVVP----VLAVVSI----YFQKKILKAYRkvrkinsrITGAFNEGITGAKTTKTL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 219 GRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVAVYFGFSYL-GELDFGhydtgvTLAAgFLALILa 297
Cdd:cd18540 198 VREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLaGAITIG------TLVA-FISYAT- 269
|
170
....*....|
gi 446966322 298 pEFFQPLRDL 307
Cdd:cd18540 270 -QFFEPIQQL 278
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
74-317 |
7.49e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 38.65 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 74 VLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLL 153
Cdd:cd18564 65 LLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 154 IVVAIFPSNWAAALILLGTAPLipLFMALVGMG-----AADANRRNFLALARLSGhfldrlRGMETLRI---FGRGEAEI 225
Cdd:cd18564 145 MLGVMFWLDWQLALIALAVAPL--LLLAARRFSrrikeASREQRRREGALASVAQ------ESLSAIRVvqaFGREEHEE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 226 ESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVaVYFGfSYL---GELDFGhydtGVTLAAGFLALilapeFFQ 302
Cdd:cd18564 217 RRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALV-LWFG-AWLvlaGRLTPG----DLLVFLAYLKN-----LYK 285
|
250
....*....|....*....
gi 446966322 303 PLRDL----GTFYHAKAQA 317
Cdd:cd18564 286 PVRDLakltGRIAKASASA 304
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
363-561 |
7.80e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.22 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 363 KTLAGP----LNFTLPAGQRAVLVGRSGSGKSSLLNALSGFL-SYQGSLRINGIELRDLSPESW-----------RKH-- 424
Cdd:PRK10762 261 DNLSGPgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALpRTSGYVTLDGHEVVTRSPQDGlangivyisedRKRdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 425 ----LSwVGQNPQLPAATLRDNVLLARPDASEQELqaaldnawVSEFLPLLpqGVDTPVGDQA-ARLSVGQAQRVAVARA 499
Cdd:PRK10762 341 lvlgMS-VKENMSLTALRYFSRAGGSLKHADEQQA--------VSDFIRLF--NIKTPSMEQAiGLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446966322 500 LLNPCSLLLLDEPAASLDAHSEQRVMEALN---AASLrqTTLMVTHQL-EDLAEWDVIWVMQDGRI 561
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINqfkAEGL--SIILVSSEMpEVLGMSDRILVMHEGRI 473
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
91-270 |
8.12e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 38.62 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 91 GQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILL 170
Cdd:cd18550 67 GQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 171 GTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLR--GMETLRIFGRGEAEIESIRSASEDFRQ---RTMEVLRL 245
Cdd:cd18550 147 VLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDlgvRQALAGRW 226
|
170 180
....*....|....*....|....*
gi 446966322 246 AFLssgILEFFTSLSIALVAVYFGF 270
Cdd:cd18550 227 FFA---ALGLFTAIGPALVYWVGGL 248
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
380-461 |
8.82e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 37.73 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446966322 380 VLVGRSGSGKSSLLNALSGFLSYQGS-LRINGIELRDLSPESwrkhlswvgqnPQLPAATLRDNVLLARPDAS---EQEL 455
Cdd:pfam06414 15 LLGGQPGAGKTELARALLDELGRQGNvVRIDPDDFRELHPHY-----------RELQAADPKTASEYTQPDASrwvEKLL 83
|
....*.
gi 446966322 456 QAALDN 461
Cdd:pfam06414 84 QHAIEN 89
|
|
| |
