|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-558 |
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: 595.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 5 KRLQALALAEKRHIVGLVIAAVMIGLSILAQAYLIVDIVDQVFLKNASFESIVPTLGWLILALVTRAGFGYMSGRIGASL 84
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 85 SEKAKRTLRLQLLDRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMM 164
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 165 VTAPFIPIFFIIIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSG 244
Cdd:COG4988 166 VTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLSS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 245 LMLEFISMLSTGVVALEVALQMvVWENLTFFSGFLILVLAPEYYLAIKDLGGAFHTGRGSMGAADRIFEALDAPDERLTW 324
Cdd:COG4988 246 AVLEFFASLSIALVAVYIGFRL-LGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAPA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 325 GDRMLT-SRTPDLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETY 403
Cdd:COG4988 325 GTAPLPaAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 404 TDSSWYDTIGYISQNPYLFAGTVADNIALGE-TADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLAL 482
Cdd:COG4988 405 DPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLAL 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 483 ARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-542 |
2.79e-150 |
|
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: 442.50 E-value: 2.79e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 15 KRHIVGLVIAAVMIGLSILAQAYLIVDIVDQVFLKNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRL 94
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 95 QLLDRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFF 174
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 175 IIIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFISMLS 254
Cdd:TIGR02857 162 ILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 255 TGVVALEVALQMVVwENLTFFSGFLILVLAPEYYLAIKDLGGAFHTGRGSMGAADRIFEALDAPdERLTWGDRMLTS-RT 333
Cdd:TIGR02857 242 VALVAVYIGFRLLA-GDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAA-PRPLAGKAPVTAaPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 334 PDLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIG 413
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 414 YISQNPYLFAGTVADNIALGET-ADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGI 492
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARPdASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2048238220 493 ILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFM 542
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-571 |
3.38e-126 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 382.59 E-value: 3.38e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 1 MNAVKRLQALALAEKRHIVGLVIAAVMIGLSILAQAYLIVDIVDQVFLKNaSFESIVPTLGWLILALVTRAGFGYMSGRI 80
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 81 GASLSEKAKRTLRLQLLDRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISG 160
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 161 VIMMVTAPFIPIFFIIIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTA 240
Cdd:COG1132 165 LIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 241 FLSGLMLEFISMLSTGVVALeVALQMVVWENLTF-----FSGFLILVLAPeyylaIKDLGGAFHTGRGSMGAADRIFEAL 315
Cdd:COG1132 245 ALFFPLMELLGNLGLALVLL-VGGLLVLSGSLTVgdlvaFILYLLRLFGP-----LRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 316 DAPDERL-TWGDRMLTSRTPDLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVL 394
Cdd:COG1132 319 DEPPEIPdPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 395 VDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIHT---------- 463
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGrPDATDEEVEEAAKAAQAHEFIEALPDGYDTvvgergvnls 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 464 --ElgeggyglsggeRQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWF 541
Cdd:COG1132 479 ggQ------------RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILV 546
|
570 580 590
....*....|....*....|....*....|.
gi 2048238220 542 MDDGKLLAQGTHDELL-SVPQYADLFTLQKG 571
Cdd:COG1132 547 LDDGRIVEQGTHEELLaRGGLYARLYRLQFG 577
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-556 |
1.91e-115 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 354.92 E-value: 1.91e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 22 VIAAVMIGLSILAQAYLIVDIVDQVFLKNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQLLDRYT 101
Cdd:PRK11174 28 ILLGFLSGLLLIAQAWLLATILQALIIENIPREALLPPFILLILLFVLRALLAWLRERVGFKAGQHIRQQIRQQVLDKLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 102 S-NPIEtsLSGQS-GKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFIIIGI 179
Cdd:PRK11174 108 QlGPAW--IQGKPaGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFPINWAAGLILLGTAPLIPLFMALVGM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 180 ATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFISMLSTGVVA 259
Cdd:PRK11174 186 GAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASISIALVA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 260 leVALQMVVWENLTF---------FSGFLILVLAPEYYLAIKDLGGAFHTGRGSMGAADRIFEALDAPDERLTWGDRMLT 330
Cdd:PRK11174 266 --VYFGFSYLGELNFghygtgvtlFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 331 SRTPdLELDA---VSFAYEGGRFTlDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVkPDSGRVLVDGEPLETYTDSS 407
Cdd:PRK11174 344 SNDP-VTIEAedlEILSPDGKTLA-GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPES 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 408 WYDTIGYISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAF 486
Cdd:PRK11174 421 WRKHLSWVGQNPQLPHGTLRDNVLLGnPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARAL 500
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 487 LKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDEL 556
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
21-311 |
3.21e-105 |
|
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: 318.20 E-value: 3.21e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 21 LVIAAVMIGLSILAQAYLIVDIVDQVFLKNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQLLDRY 100
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 101 TSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFIIIGIA 180
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 181 TQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFISMLSTGVVAL 260
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2048238220 261 EVALQMvVWENLTFFSGFLILVLAPEYYLAIKDLGGAFHTGRGSMGAADRI 311
Cdd:cd18584 241 YIGFRL-LGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-569 |
1.26e-93 |
|
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: 301.75 E-value: 1.26e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 5 KRLQALALAEKRHIVGLVIAAVMIGLSILAQAYLIVDIVDQVfLKNASFESIVPTLGWLILALVTRAGFGYMSGRIGASL 84
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRV-LPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 85 SEKAKRTLRLQLLDRYTSNPIETSLSGQSGKKVSVFMDaVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMM 164
Cdd:COG2274 224 GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 165 VTAPFIPIFFIIIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSG 244
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 245 LMLEFISMLSTGVVaLEVALQMVVWENLTF-----FSGFLILVLAPeyylaIKDLGGAFHTGRGSMGAADRIFEALDAPD 319
Cdd:COG2274 383 TLSGLLQQLATVAL-LWLGAYLVIDGQLTLgqliaFNILSGRFLAP-----VAQLIGLLQRFQDAKIALERLDDILDLPP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 320 ERLTWGDRMLTSR-TPDLELDAVSFAYEG-GRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDG 397
Cdd:COG2274 457 EREEGRSKLSLPRlKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 398 EPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGE 476
Cdd:COG2274 537 IDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQ 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 477 RQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDEL 556
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
570
....*....|....
gi 2048238220 557 LSVP-QYADLFTLQ 569
Cdd:COG2274 697 LARKgLYAELVQQQ 710
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
180-568 |
8.59e-82 |
|
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: 266.63 E-value: 8.59e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 180 ATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATmvvLKTAFLSGLMlEFISMLSTG--- 256
Cdd:COG4987 179 LGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQ---RRLARLSALA-QALLQLAAGlav 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 257 VVALEVALQMVVWENL--TFFSGFLILVLA-PEyylAIKDLGGAFHTGRGSMGAADRIFEALDAPDERLTWGDRMLTSRT 333
Cdd:COG4987 255 VAVLWLAAPLVAAGALsgPLLALLVLAALAlFE---ALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 334 PDLELDAVSFAYEGGRFT-LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTI 412
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIHT------------ElgeggyglsggeRQR 479
Cdd:COG4987 412 AVVPQRPHLFDTTLRENLRLArPDATDEELWAALERVGLGDWLAALPDGLDTwlgeggrrlsggE------------RRR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 480 LALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSV 559
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
410
....*....|
gi 2048238220 560 -PQYADLFTL 568
Cdd:COG4987 560 nGRYRQLYQR 569
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-569 |
3.07e-76 |
|
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: 252.33 E-value: 3.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 20 GLVIAAVMIGLSILAQAYLIV---DIVDQVF-LKNASFESIVPTLgwLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQ 95
Cdd:TIGR02203 15 GLVLAGVAMILVAATESTLAAllkPLLDDGFgGRDRSVLWWVPLV--VIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 96 LLDRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFI 175
Cdd:TIGR02203 93 MFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 176 IIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFISMLST 255
Cdd:TIGR02203 173 RVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLAL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 256 GVVaLEVALQMVVWENLTF--FSGF---LILVLAPEYYLAikDLGGAFHTGrgsMGAADRIFEALDAPDERLTwGDRMLT 330
Cdd:TIGR02203 253 AVV-LFIALFQAQAGSLTAgdFTAFitaMIALIRPLKSLT--NVNAPMQRG---LAAAESLFTLLDSPPEKDT-GTRAIE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 331 SRTPDLELDAVSFAYEG-GRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWY 409
Cdd:TIGR02203 326 RARGDVEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 410 DTIGYISQNPYLFAGTVADNIALGET--ADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFL 487
Cdd:TIGR02203 406 RQVALVSQDVVLFNDTIANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 488 KRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVP-QYADLF 566
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNgLYAQLH 565
|
...
gi 2048238220 567 TLQ 569
Cdd:TIGR02203 566 NMQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
335-557 |
3.96e-66 |
|
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: 214.78 E-value: 3.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 335 DLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGY 414
Cdd:cd03254 2 EIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGII 493
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGrPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 494 LFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELL 557
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
336-566 |
1.13e-65 |
|
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: 214.02 E-value: 1.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEG-GRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGY 414
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGII 493
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 494 LFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVP-QYADLF 566
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGgVYAKLH 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
336-569 |
8.34e-63 |
|
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: 206.31 E-value: 8.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYI 415
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIIL 494
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 495 FDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVP-QYADLFTLQ 569
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGgLYAEMWKAQ 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
336-546 |
3.38e-61 |
|
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: 199.92 E-value: 3.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGG-RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGY 414
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAGTVADNIaL--GEtadeikileaanaaglndviaqlpngihtelgeggyglsggeRQRLALARAFLKRPGI 492
Cdd:cd03228 81 VPQDPFLFSGTIRENI-LsgGQ------------------------------------------RQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 493 ILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGK 546
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
337-569 |
2.03e-60 |
|
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: 200.07 E-value: 2.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 337 ELDAVSFAYEG--GRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGY 414
Cdd:cd03249 2 EFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAGTVADNIALG---ETADEIKilEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPG 491
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGkpdATDEEVE--EAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048238220 492 IILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVP-QYADLFTLQ 569
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKgVYAKLVKAQ 238
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
336-569 |
9.36e-52 |
|
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: 177.29 E-value: 9.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEG-GRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETyTDSSWYD-TIG 413
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL-ADPAWLRrQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 414 YISQNPYLFAGTVADNIALGETADEI-KILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGI 492
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMeRVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 493 ILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSV-PQYADLFTLQ 569
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEnGLYAYLYQLQ 237
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-571 |
1.29e-51 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 186.38 E-value: 1.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 20 GLVIAAVMIGLSILAQAYLIV---DIVDQVFLK-NASFESIVPTLgwLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQ 95
Cdd:PRK11176 26 GLIVAGVALILNAASDTFMLSllkPLLDDGFGKaDRSVLKWMPLV--VIGLMILRGITSFISSYCISWVSGKVVMTMRRR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 96 LLDRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQ--TSIIPLLILVVVFSqhWISGVIMMVTAPFIPIF 173
Cdd:PRK11176 104 LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVRegASIIGLFIMMFYYS--WQLSLILIVIAPIVSIA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 174 FIIIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFISML 253
Cdd:PRK11176 182 IRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 254 STGVVaLEVALQMVVWENLT------FFSGFLILvLAPeyylaIKDL---GGAFHTGrgsMGAADRIFEALDAPDERLTw 324
Cdd:PRK11176 262 ALAFV-LYAASFPSVMDTLTagtitvVFSSMIAL-MRP-----LKSLtnvNAQFQRG---MAACQTLFAILDLEQEKDE- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 325 GDRMLTSRTPDLELDAVSFAYEGG-RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETY 403
Cdd:PRK11176 331 GKRVIERAKGDIEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 404 TDSSWYDTIGYISQNPYLFAGTVADNIAL--GETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLA 481
Cdd:PRK11176 411 TLASLRNQVALVSQNVHLFNDTIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 482 LARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVP- 560
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNg 570
|
570
....*....|.
gi 2048238220 561 QYADLFTLQKG 571
Cdd:PRK11176 571 VYAQLHKMQFG 581
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-569 |
1.48e-51 |
|
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: 186.56 E-value: 1.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 16 RHIVGLVIAAVMIGLSILAQAYLIVDIVDQVFLKNASFESIVPTLGWLILALVtragFGYMSGRIGASL----------- 84
Cdd:COG5265 29 PPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLL----LAYGLLRLLSVLfgelrdalfar 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 85 -SEKAKRTLRLQL------------LDRYT---SNPIETSLSGqsgkkVSVFMdavdevdaYFSQYwpqviqtSIIP--- 145
Cdd:COG5265 105 vTQRAVRRLALEVfrhlhalslrfhLERQTgglSRDIERGTKG-----IEFLL--------RFLLF-------NILPtll 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 146 --LLILVVVFSQ-HWISGVIMMVTapfipifFIIIGIATQKKSEQQME---KMNQF----SGKFLDVLQGLTTLKLYGRT 215
Cdd:COG5265 165 eiALVAGILLVKyDWWFALITLVT-------VVLYIAFTVVVTEWRTKfrrEMNEAdseaNTRAVDSLLNYETVKYFGNE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 216 EREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFIsmLSTGVVALEV-ALQMVVWENLTFfsGFLILVLApeY----YLA 290
Cdd:COG5265 238 AREARRYDEALARYERAAVKSQTSLALLNFGQALI--IALGLTAMMLmAAQGVVAGTMTV--GDFVLVNA--YliqlYIP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 291 IKDLGGAFHTGRGSMGAADRIFEAL-------DAPDERltwgdrMLTSRTPDLELDAVSFAYEGGRFTLDPLSGMIPTGA 363
Cdd:COG5265 312 LNFLGFVYREIRQALADMERMFDLLdqppevaDAPDAP------PLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 364 HVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALG-ETADEIKIL 442
Cdd:COG5265 386 TVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGrPDASEEEVE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 443 EAANAAGLNDVIAQLPNGIHT------------ElgeggyglsggeRQRLALARAFLKRPGIILFDEPTTGLDLVTEQIV 510
Cdd:COG5265 466 AAARAAQIHDFIESLPDGYDTrvgerglklsggE------------KQRVAIARTLLKNPPILIFDEATSALDSRTERAI 533
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 511 RRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSvpQ---YADLFTLQ 569
Cdd:COG5265 534 QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLA--QgglYAQMWARQ 593
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
335-551 |
9.95e-49 |
|
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: 168.54 E-value: 9.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 335 DLELDAVSFAYEGG-RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGepletyTDSSWYD--- 410
Cdd:cd03245 2 RIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG------TDIRQLDpad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 ---TIGYISQNPYLFAGTVADNIALGET-ADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAF 486
Cdd:cd03245 76 lrrNIGYVPQDVTLFYGTLRDNITLGAPlADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048238220 487 LKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQG 551
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
307-569 |
7.87e-48 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 176.06 E-value: 7.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 307 AADRIFEALDAPDERLTWGDRMLTSRTpdLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLV 386
Cdd:PRK10790 314 AGERVFELMDGPRQQYGNDDRPLQSGR--IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 387 KPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALGETADEIKILEAANAAGLNDVIAQLPNGIHTELG 466
Cdd:PRK10790 392 PLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 467 EGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGK 546
Cdd:PRK10790 472 EQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
250 260
....*....|....*....|....
gi 2048238220 547 LLAQGTHDELLSVP-QYADLFTLQ 569
Cdd:PRK10790 552 AVEQGTHQQLLAAQgRYWQMYQLQ 575
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-557 |
2.54e-47 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 174.38 E-value: 2.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 7 LQALAlAEKRHIVGLVIAAVMIGLSILAQAYLIVDIVDQVflknASFESIVPTLG-WlilalvtrAGFGYMSGRIGASLS 85
Cdd:PRK13657 11 LQYLG-AEKRLGILLAVANVLLAAATFAEPILFGRIIDAI----SGKGDIFPLLAaW--------AGFGLFNIIAGVLVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 86 EKAKRTL---RLQLLDRYTSNPIETSLSGQSGKKVSVFMDA-VDEVDAYFSqYWPQVIQ---TSIIPLLILV-VVFSQHW 157
Cdd:PRK13657 78 RHADRLAhrrRLAVLTEYFERIIQLPLAWHSQRGSGRALHTlLRGTDALFG-LWLEFMRehlATLVALVVLLpLALFMNW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 158 ISGVIMMVTAPFIPIFFIIIGIATQkksEQQMEKMNQFSGKF---LDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATM 234
Cdd:PRK13657 157 RLSLVLVVLGIVYTLITTLVMRKTK---DGQAAVEEHYHDLFahvSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 235 VVLKT-AFLSGL--MLEFISMLSTGVV--ALEVALQMVVWENLTF--FSGFLILVLapeyylaikDLGGAFHTGrgSMGA 307
Cdd:PRK13657 234 PVLSWwALASVLnrAASTITMLAILVLgaALVQKGQLRVGEVVAFvgFATLLIGRL---------DQVVAFINQ--VFMA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 308 ADRI---FEALDA-PDERLTWGDRMLTSRTPDLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLS 383
Cdd:PRK13657 303 APKLeefFEVEDAvPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 384 GLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIH 462
Cdd:PRK13657 383 RVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGrPDATDEEMRAAAERAQAHDFIERKPDGYD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 463 TELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFM 542
Cdd:PRK13657 463 TVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVF 542
|
570
....*....|....*
gi 2048238220 543 DDGKLLAQGTHDELL 557
Cdd:PRK13657 543 DNGRVVESGSFDELV 557
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
306-569 |
2.61e-47 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 174.12 E-value: 2.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 306 GAADRIFEALDA-PDERLTWGDRMLTSRTP-DLELDAVSFAYEG--GRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNV 381
Cdd:TIGR02204 306 GAAERLIELLQAePDIKAPAHPKTLPVPLRgEIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 382 LSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALGET-ADEIKILEAANAAGLNDVIAQLPNG 460
Cdd:TIGR02204 386 LLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPdATDEEVEAAARAAHAHEFISALPEG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 461 IHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIW 540
Cdd:TIGR02204 466 YDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIV 545
|
250 260 270
....*....|....*....|....*....|
gi 2048238220 541 FMDDGKLLAQGTHDELL-SVPQYADLFTLQ 569
Cdd:TIGR02204 546 VMDQGRIVAQGTHAELIaKGGLYARLARLQ 575
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
336-558 |
6.09e-46 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 161.35 E-value: 6.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYI 415
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNP--YLFAGTVADNIA-----LGETADEIK--ILEAANAAGLND----VIAQLPNGihtelgeggyglsggERQRLAL 482
Cdd:COG1122 81 FQNPddQLFAPTVEEDVAfgpenLGLPREEIRerVEEALELVGLEHladrPPHELSGG---------------QKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 483 ARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE-ATLVTVAHRLHTI-KQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
138-560 |
8.68e-46 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 171.68 E-value: 8.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 138 VIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFIIIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTER 217
Cdd:TIGR03797 256 TLLSGIFALLNLGLMFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 218 EAQAI-----EKSSLDFRDATMVVLKTAFLSGLMLEFISMLSTGVVALEVALQMVVWENLTFFSGFLILVLApeyylaIK 292
Cdd:TIGR03797 336 AFARWaklfsRQRKLELSAQRIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGA------VT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 293 DLGGAFHTGRGSMGAADRIFEALDAPDErlTWGDRMLTSR-TPDLELDAVSFAY-EGGRFTLDPLSGMIPTGAHVALVGA 370
Cdd:TIGR03797 410 QLSNTLISILAVIPLWERAKPILEALPE--VDEAKTDPGKlSGAIEVDRVTFRYrPDGPLILDDVSLQIEPGEFVAIVGP 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 371 SGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALGE--TADEIkiLEAANAA 448
Cdd:TIGR03797 488 SGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAplTLDEA--WEAARMA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 449 GLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSreATLVTVAH 528
Cdd:TIGR03797 566 GLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK--VTRIVIAH 643
|
410 420 430
....*....|....*....|....*....|..
gi 2048238220 529 RLHTIKQADAIWFMDDGKLLAQGTHDELLSVP 560
Cdd:TIGR03797 644 RLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
307-571 |
1.20e-45 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 171.46 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 307 AADRIFEALDAPDERLTWGDRMLTSRTPDLELDAVSFAY-EGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGL 385
Cdd:TIGR01846 427 ALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRYaPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRL 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 386 VKPDSGRVLVDGEPLeTYTDSSWYD-TIGYISQNPYLFAGTVADNIALGE-TADEIKILEAANAAGLNDVIAQLPNGIHT 463
Cdd:TIGR01846 507 YTPQHGQVLVDGVDL-AIADPAWLRrQMGVVLQENVLFSRSIRDNIALCNpGAPFEHVIHAAKLAGAHDFISELPQGYNT 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 464 ELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMD 543
Cdd:TIGR01846 586 EVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLE 665
|
250 260
....*....|....*....|....*....
gi 2048238220 544 DGKLLAQGTHDELLSVP-QYADLFTLQKG 571
Cdd:TIGR01846 666 KGQIAESGRHEELLALQgLYARLWQQQSG 694
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
112-530 |
1.61e-45 |
|
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: 168.31 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 112 QSGKKVSVFMDAVDEVDAYfsqyWPQVIQTSIIPLL--ILVVVFSQ--HWISGVIMMVTAPFIPIFFIIIGIATQKKSEQ 187
Cdd:TIGR02868 108 RRGDLLGRLGADVDALQDL----YVRVIVPAGVALVvgAAAVAAIAvlSVPAALILAAGLLLAGFVAPLVSLRAARAAEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 188 QMEKM-NQFSGKFLDVLQGLTTLKLYGR----------TEREAQAIEKssldfRDATMVVLKTAFLSGLM-LEFISMLST 255
Cdd:TIGR02868 184 ALARLrGELAAQLTDALDGAAELVASGAlpaalaqveeADRELTRAER-----RAAAATALGAALTLLAAgLAVLGALWA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 256 GVVALEVALQMVVWenltfFSGFLILVLApeYYLAIKDLGGAFHTGRGSMGAADRIFEALDAPDERLTW---GDRMLTSR 332
Cdd:TIGR02868 259 GGPAVADGRLAPVT-----LAVLVLLPLA--AFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGsapAAGAVGLG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTI 412
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPG 491
Cdd:TIGR02868 412 SVCAQDAHLFDTTVRENLRLArPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAP 491
|
410 420 430
....*....|....*....|....*....|....*....
gi 2048238220 492 IILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRL 530
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-557 |
4.90e-45 |
|
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: 169.54 E-value: 4.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 2 NAVKRLQALALAEKRHIVGLVIAAVMIGLSILAQAYLIVDIVDqVFLKNASFESI-VPTLGwLILALVTRAGFGYMSGRI 80
Cdd:TIGR01193 142 NSLLKFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIID-TYIPHKMMGTLgIISIG-LIIAYIIQQILSYIQIFL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 81 GASLSEKAKRTLRLQLLDRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFsQHWISG 160
Cdd:TIGR01193 220 LNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVR-QNMLLF 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 161 VIMMVTAPFIPIFFIIIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTA 240
Cdd:TIGR01193 299 LLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKAD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 241 FLSGLmLEFISMLSTGVVALEVALQMVVWENLTF-----FSGFLILVLAPeyYLAIKDLGGAFHTGRGsmgAADRIFEAL 315
Cdd:TIGR01193 379 QGQQA-IKAVTKLILNVVILWTGAYLVMRGKLTLgqlitFNALLSYFLTP--LENIINLQPKLQAARV---ANNRLNEVY 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 316 DAPDERLTWGDRM-LTSRTPDLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVL 394
Cdd:TIGR01193 453 LVDSEFINKKKRTeLNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIL 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 395 VDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALG--ETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGL 472
Cdd:TIGR01193 533 LNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSI 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 473 SGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELsREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGT 552
Cdd:TIGR01193 613 SGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGS 691
|
....*
gi 2048238220 553 HDELL 557
Cdd:TIGR01193 692 HDELL 696
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
304-556 |
6.29e-45 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 169.52 E-value: 6.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 304 SMGAADRIFEALDAPDERLTWGDRMLTSRTPDLELDAVSFAY---------EGGRFTLDPlsgmiptGAHVALVGASGSG 374
Cdd:TIGR00958 447 AVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYpnrpdvpvlKGLTFTLHP-------GEVVALVGPSGSG 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 375 KTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALGET-ADEIKILEAANAAGLNDV 453
Cdd:TIGR00958 520 KSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTdTPDEEIMAAAKAANAHDF 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 454 IAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSReaTLVTVAHRLHTI 533
Cdd:TIGR00958 600 IMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASR--TVLLIAHRLSTV 677
|
250 260
....*....|....*....|...
gi 2048238220 534 KQADAIWFMDDGKLLAQGTHDEL 556
Cdd:TIGR00958 678 ERADQILVLKKGSVVEMGTHKQL 700
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-558 |
9.63e-45 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 166.37 E-value: 9.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 15 KRHIVGLVIAAVMIGLSILAQAYLIVDIVDQVfLKNASfesiVPTLGWL-ILALVTRAGFGYMS---GRIGASLSEKakr 90
Cdd:TIGR01842 5 KRTFIIVGLFSFVINILMLAPPLYMLQVYDRV-LTSGS----VPTLLMLtVLALGLYLFLGLLDalrSFVLVRIGEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 91 tLRLQLLDRYTSNPIETSLSGQSGKKVSVFMDaVDEVDAYFSQywPQVIQTSIIPLLI--LVVVFSQH-WIsGVIMMVTA 167
Cdd:TIGR01842 77 -LDGALNQPIFAASFSATLRRGSGDGLQALRD-LDQLRQFLTG--PGLFAFFDAPWMPiyLLVCFLLHpWI-GILALGGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 168 PFIPIFFIIIGIATQKKSEQQME---KMNQFSGKFL---DVLQGLTTLK-LYGRTEREAQAiekssldFRDATMVVLKTA 240
Cdd:TIGR01842 152 VVLVGLALLNNRATKKPLKEATEasiRANNLADSALrnaEVIEAMGMMGnLTKRWGRFHSK-------YLSAQSAASDRA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 241 -FLSGLMLEFISMLSTGVVALEVALqmVVWENLTffSGFLIL-------VLAPeyylaIKDLGGAFHTGRGSMGAADRI- 311
Cdd:TIGR01842 225 gMLSNLSKYFRIVLQSLVLGLGAYL--AIDGEIT--PGMMIAgsilvgrALAP-----IDGAIGGWKQFSGARQAYKRLn 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 312 --FEALDAPDERLTwgdrmLTSRTPDLELDAVSFAYEGG-RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKP 388
Cdd:TIGR01842 296 elLANYPSRDPAMP-----LPEPEGHLSVENVTIVPPGGkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 389 DSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIA-LGETADEIKILEAANAAGLNDVIAQLPNGIHTELGE 467
Cdd:TIGR01842 371 TSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGP 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 468 GGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEEL-SREATLVTVAHRLHTIKQADAIWFMDDGK 546
Cdd:TIGR01842 451 GGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGR 530
|
570
....*....|..
gi 2048238220 547 LLAQGTHDELLS 558
Cdd:TIGR01842 531 IARFGERDEVLA 542
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
303-558 |
9.31e-44 |
|
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: 164.15 E-value: 9.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 303 GSMGAADRIFEALDAPDERltwGDRM-LTSRTPDLELDAVSFAYEGG-RFTLDPLSGMIPTGAHVALVGASGSGKTTVLN 380
Cdd:COG4618 300 SARQAYRRLNELLAAVPAE---PERMpLPRPKGRLSVENLTVVPPGSkRPILRGVSFSLEPGEVLGVIGPSGSGKSTLAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 381 VLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALGETADEIKILEAANAAGLNDVIAQLPNG 460
Cdd:COG4618 377 LLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDG 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 461 IHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEEL-SREATLVTVAHRLHTIKQADAI 539
Cdd:COG4618 457 YDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKL 536
|
250
....*....|....*....
gi 2048238220 540 WFMDDGKLLAQGTHDELLS 558
Cdd:COG4618 537 LVLRDGRVQAFGPRDEVLA 555
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
334-552 |
1.15e-43 |
|
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: 154.96 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 334 PDLELDAVSFAY-EGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTI 412
Cdd:cd03244 1 GDIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYLFAGTVADNIA-LGETADEiKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPG 491
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGEYSDE-ELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2048238220 492 IILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGT 552
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
341-547 |
1.51e-43 |
|
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: 154.94 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 341 VSFAY---------EGGRFTLDPlsgmiptGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT 411
Cdd:cd03248 17 VTFAYptrpdtlvlQDVSFTLHP-------GEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 IGYISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRP 490
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 491 GIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKL 547
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
336-565 |
1.75e-43 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 165.12 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAY--------EGgrFTLDplsgmIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSS 407
Cdd:TIGR03796 478 VELRNITFGYspleppliEN--FSLT-----LQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREV 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 408 WYDTIGYISQNPYLFAGTVADNIALGE-TADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAF 486
Cdd:TIGR03796 551 LANSVAMVDQDIFLFEGTVRDNLTLWDpTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARAL 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 487 LKRPGIILFDEPTTGLDLVTEQIVRRSIEElsREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVP-QYADL 565
Cdd:TIGR03796 631 VRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGgAYARL 708
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
182-558 |
3.54e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 162.69 E-value: 3.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 182 QKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDA--TMVVLkTAFLSGLMlefisMLSTGVva 259
Cdd:PRK11160 186 KKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAqrRQANL-TGLSQALM-----ILANGL-- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 260 levALQMVVW------ENLTFFSGFLILV----------LAPeyylaikdLGGAF-HTGrGSMGAADRIFEALDAPDERL 322
Cdd:PRK11160 258 ---TVVLMLWlaaggvGGNAQPGALIALFvfaalaafeaLMP--------VAGAFqHLG-QVIASARRINEITEQKPEVT 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 323 TWGDRMLTSRTPDLELDAVSFAY-EGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLE 401
Cdd:PRK11160 326 FPTTSTAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 402 TYTDSSWYDTIGYISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIA--------------QLPNGihtelg 466
Cdd:PRK11160 406 DYSEAALRQAISVVSQRVHLFSATLRDNLLLAaPNASDEALIEVLQQVGLEKLLEddkglnawlgeggrQLSGG------ 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 467 eggyglsggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGK 546
Cdd:PRK11160 480 ---------EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQ 550
|
410
....*....|..
gi 2048238220 547 LLAQGTHDELLS 558
Cdd:PRK11160 551 IIEQGTHQELLA 562
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
336-547 |
4.39e-42 |
|
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: 148.90 E-value: 4.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGG-RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGY 414
Cdd:cd03246 1 LEVENVSFRYPGAePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAGTVADNIalgetadeikileaanaaglndviaqLPNGihtelgeggyglsggERQRLALARAFLKRPGIIL 494
Cdd:cd03246 81 LPQDDELFSGSIAENI--------------------------LSGG---------------QRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 495 FDEPTTGLDLVTEQIVRRSIEELS-REATLVTVAHRLHTIKQADAIWFMDDGKL 547
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
4-556 |
2.01e-41 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 157.74 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 4 VKRLQALALaEKRHIVGLVIAAVMIGLSILAQAYLIVDIVDQVflknASFESIVPTLgwlilalVTRAGFGYMSGRIGAS 83
Cdd:TIGR01192 8 VRALSYLNV-HKNRVLLIVIANITLAAITIAEPILFGRIIDAI----SSKSDVLPTL-------ALWAGFGVFNTIAYVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 84 LSEKAKRTL---RLQLLDRYTSNPIETSLSGQSGKKVS----VFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQH 156
Cdd:TIGR01192 76 VAREADRLAhgrRATLLTEAFGRIISMPLSWHQQRGTSnalhTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 157 WISGVIMMVTAPFIPIFFIIIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVV 236
Cdd:TIGR01192 156 WRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 237 LKT-AFLSGL--MLEFISMLSTGVVA--LEVALQMVVWENLTF--FSGFLILVLapeyylaikDLGGAFHTGRGSMGAA- 308
Cdd:TIGR01192 236 LDWwALASGLnrMASTISMMCILVIGtvLVIKGELSVGEVIAFigFANLLIGRL---------DQMSGFITQIFEARAKl 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 309 DRIFEALDAPDERLTWGD-RMLTSRTPDLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVK 387
Cdd:TIGR01192 307 EDFFDLEDSVFQREEPADaPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 388 PDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIHTELG 466
Cdd:TIGR01192 387 PTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGrEGATDEEVYEAAKAAAAHDFILKRSNGYDTLVG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 467 EGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGK 546
Cdd:TIGR01192 467 ERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGR 546
|
570
....*....|
gi 2048238220 547 LLAQGTHDEL 556
Cdd:TIGR01192 547 LIEKGSFQEL 556
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
21-311 |
2.69e-41 |
|
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: 150.89 E-value: 2.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 21 LVIAAVMIGLSILAQAYLIVDIVDQVFLkNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQLLDRY 100
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFA-GGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 101 TSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFIIIGIA 180
Cdd:cd18561 80 LKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 181 TQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFISMLSTgVVAL 260
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGT-ALAL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2048238220 261 EVALQMVVWENLTFFSGFLILVLAPEYYLAIKDLGGAFHTGRGSMGAADRI 311
Cdd:cd18561 239 GVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
336-550 |
2.81e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 148.65 E-value: 2.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGM---IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSW---- 408
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVslsIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 409 YDTIGYISQNPYLFAG-TVADNIAL-----GETADEIK--ILEAANAAGLNDVIAQLPN----GihtelgeggyglsggE 476
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALplllaGVSRKERRerARELLERVGLGDRLDHRPSqlsgG---------------Q 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 477 RQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQADAIWFMDDGKLLAQ 550
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
337-546 |
1.28e-39 |
|
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: 143.76 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 337 ELDAVSFAYEGG-RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYI 415
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNP--YLFAGTVADNIA-----LGETADEI--KILEAANAAGLND----VIAQLPNGihtelgeggyglsggERQRLAL 482
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAfglenLGLPEEEIeeRVEEALELVGLEGlrdrSPFTLSGG---------------QKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 483 ARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE-ATLVTVAHRLHTIKQ-ADAIWFMDDGK 546
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
336-547 |
1.58e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.72 E-value: 1.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFtLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYI 415
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAGTVADNIAL-----GETADEIKILEAANAAGLNDVIAQLPngIHT----ElgeggyglsggeRQRLALARAF 486
Cdd:COG4619 80 PQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDILDKP--VERlsggE------------RQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 487 LKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKL 547
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
336-558 |
1.56e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.66 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYtDSSWYDTIGYI 415
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD-PAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAG-TVADNIAL-----GETADEIK--ILEAANAAGLNDV----IAQLPNGihtelgeggyglsggERQRLALA 483
Cdd:COG1131 79 PQEPALYPDlTVRENLRFfarlyGLPRKEARerIDELLELFGLTDAadrkVGTLSGG---------------MKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 484 RAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE-ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLS 558
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
336-551 |
1.44e-36 |
|
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: 134.36 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFT-LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwYDTIGY 414
Cdd:cd03247 1 LSINNVSFSYPEQEQQvLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL-SSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAGTVADNIAlgetadeikileaanaaglndviAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIIL 494
Cdd:cd03247 80 LNQRPYLFDTTLRNNLG-----------------------RRFSGG---------------ERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 495 FDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQG 551
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
331-557 |
2.07e-36 |
|
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: 135.88 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 331 SRTPDLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYD 410
Cdd:COG1127 1 MSEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 T---IGYISQNPYLFAG-TVADNIAL------GETADEIK--ILEAANAAGLNDVIAQLPN----GIhtelgeggyglsg 474
Cdd:COG1127 80 LrrrIGMLFQGGALFDSlTVFENVAFplrehtDLSEAEIRelVLEKLELVGLPGAADKMPSelsgGM------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 475 geRQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQG 551
Cdd:COG1127 147 --RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElgLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*.
gi 2048238220 552 THDELL 557
Cdd:COG1127 225 TPEELL 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
336-566 |
2.84e-36 |
|
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: 135.94 E-value: 2.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYI 415
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYL-FAGTVADNIALGET-----------ADEIKILEAANAAGLNDV----IAQLPNGihtElgeggyglsggeRQR 479
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRYphlglfgrpsaEDREAVEEALERTGLEHLadrpVDELSGG---E------------RQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 480 LALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRL-HTIKQADAIWFMDDGKLLAQGTHDEL 556
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEV 225
|
250
....*....|
gi 2048238220 557 LSVPQYADLF 566
Cdd:COG1120 226 LTPELLEEVY 235
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
336-547 |
1.07e-35 |
|
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: 133.00 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGM---IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSW---- 408
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVslsIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 409 YDTIGYISQN----PYLfagTVADNIAL-----GETADEIK--ILEAANAAGLNDVIAQLPN----Gihtelgeggygls 473
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELplllaGVPKKERRerAEELLERVGLGDRLNHYPSelsgG------------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 474 ggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHTIKQADAIWFMDDGKL 547
Cdd:cd03255 145 --QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
336-556 |
1.45e-35 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 133.40 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT---I 412
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYLFAG-TVADNIA--------LGETADEIKILEAANAAGLNDVI----AQLPNGIhtelgeggyglsggeRQR 479
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAfplrehtrLSEEEIREIVLEKLEAVGLRGAEdlypAELSGGM---------------KKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 480 LALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDEL 556
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
336-561 |
2.73e-35 |
|
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: 133.00 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAY---EGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTI 412
Cdd:COG1124 2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYLFA---GTVADNIA-----LGETADEIKILEAANAAGLNDVIA-----QLPNGihtelgeggyglsggERQR 479
Cdd:COG1124 82 QMVFQDPYASLhprHTVDRILAeplriHGLPDREERIAELLEQVGLPPSFLdryphQLSGG---------------QRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 480 LALARAFLKRPGIILFDEPTTGLDLVTE-QIVRRsIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDE 555
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQaEILNL-LKDLREErgLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
....*.
gi 2048238220 556 LLSVPQ 561
Cdd:COG1124 226 LLAGPK 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
336-558 |
3.28e-35 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 132.67 E-value: 3.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYtDSSWYDTIGYI 415
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAG-TVADNIAL-----GETADEIK--ILEAANAAGLNDV----IAQLPNGihtelgeggyglsggERQRLALA 483
Cdd:COG4555 80 PDERGLYDRlTVRENIRYfaelyGLFDEELKkrIEELIELLGLEEFldrrVGELSTG---------------MKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 484 RAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVA-HRLHTI-KQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVeALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
306-561 |
3.82e-33 |
|
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: 133.10 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 306 GAADRIF------EALDAPDERLTWGDRMLTSRTPDLELDAVSFAYEGGRFT----LDPLSGMIPTGAHVALVGASGSGK 375
Cdd:COG1123 225 GPPEEILaapqalAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 376 TTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYD---TIGYISQNPY--LFAG-TVADNIALG------ETADEI--KI 441
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRVQMVFQDPYssLNPRmTVGDIIAEPlrlhglLSRAERreRV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 442 LEAANAAGLNDVIA-----QLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLDL-VTEQIVRRsIE 515
Cdd:COG1123 385 AELLERVGLPPDLAdryphELSGG---------------QRQRVAIARALALEPKLLILDEPTSALDVsVQAQILNL-LR 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2048238220 516 ELSREA--TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:COG1123 449 DLQRELglTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
337-546 |
1.32e-32 |
|
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: 122.74 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 337 ELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYIS 416
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 QnpylfagtvadnIALGEtadeikileaanaaglndviaqlpngihtelgeggyglsggeRQRLALARAFLKRPGIILFD 496
Cdd:cd00267 80 Q------------LSGGQ------------------------------------------RQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 497 EPTTGLDLVTEQIVRRSIEELSRE-ATLVTVAHRLHTIKQA-DAIWFMDDGK 546
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-561 |
2.39e-32 |
|
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: 130.41 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYEGGR-FTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPD---SGRVLVDGEPLETYTDSSW 408
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 409 YDTIGYISQNPY--LFAGTVADNIA-----LGETADEIK--ILEAANAAGLNDVIAQLPNgihtelgeggyGLSGGERQR 479
Cdd:COG1123 82 GRRIGMVFQDPMtqLNPVTVGDQIAealenLGLSRAEARarVLELLEAVGLERRLDRYPH-----------QLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 480 LALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDEL 556
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEI 230
|
....*
gi 2048238220 557 LSVPQ 561
Cdd:COG1123 231 LAAPQ 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
336-531 |
3.21e-32 |
|
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: 123.74 E-value: 3.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFT---LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSswydtI 412
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYLFA-GTVADNIALG-----ETADEIK--ILEAANAAGLNDV----IAQLPNGIhtelgeggyglsggeRQRL 480
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgVPKAEARerAEELLELVGLSGFenayPHQLSGGM---------------RQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 481 ALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLH 531
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtgKTVLLVTHDID 193
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
336-547 |
3.41e-32 |
|
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: 121.74 E-value: 3.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDsSWYDTIGYI 415
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAG-TVADNIAL--GEtadeikileaanaaglndviaqlpngihtelgeggyglsggeRQRLALARAFLKRPGI 492
Cdd:cd03230 79 PEEPSLYENlTVRENLKLsgGM------------------------------------------KQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 493 ILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVA-HRLHTIKQ-ADAIWFMDDGKL 547
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
333-566 |
6.29e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.66 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYtdsswYDTI 412
Cdd:COG1121 4 MPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYL---FAGTVADNIALG-----------ETADEIKILEAANAAGLNDV----IAQLPNGihtelgeggyglsg 474
Cdd:COG1121 78 GYVPQRAEVdwdFPITVRDVVLMGrygrrglfrrpSRADREAVDEALERVGLEDLadrpIGELSGG-------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 475 gERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE-ATLVTVAHRLHTIKQ-ADAIWFMDDGkLLAQGT 552
Cdd:COG1121 144 -QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVLLLNRG-LVAHGP 221
|
250
....*....|....
gi 2048238220 553 HDELLSVPQYADLF 566
Cdd:COG1121 222 PEEVLTPENLSRAY 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
336-556 |
1.26e-31 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 122.29 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVK-----PDSGRVLVDGEPL--ETYTDSSW 408
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 409 YDTIGYISQNPYLFAGTVADNIALG---------ETADEIkILEAANAAGLNDVIAQLPNGIHtelgeggygLSGGERQR 479
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiklkEELDER-VEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 480 LALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDEL 556
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
337-551 |
1.52e-31 |
|
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: 120.23 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 337 ELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYIS 416
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 QnpylfagtvadnialgetadeikILEAANAAGLND-VIAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILF 495
Cdd:cd03214 80 Q-----------------------ALELLGLAHLADrPFNELSGG---------------ERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2048238220 496 DEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRL-HTIKQADAIWFMDDGKLLAQG 551
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
336-546 |
3.65e-31 |
|
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: 119.21 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSS--WYDTIG 413
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 414 YISQNPYLFAG-TVADNIALGetadeikileaanaaglndviaqLPNGihtelgeggyglsggERQRLALARAFLKRPGI 492
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG-----------------------LSGG---------------QQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 493 ILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLH-TIKQADAIWFMDDGK 546
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
336-551 |
8.00e-31 |
|
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: 119.55 E-value: 8.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDT-IGY 414
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV---TGVPPERRnIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAG-TVADNIALG-------ETADEIKILEAANAAGLNDVIAQLPNGIHTelgeggyglsgGERQRLALARAF 486
Cdd:cd03259 77 VFQDYALFPHlTVAENIAFGlklrgvpKAEIRARVRELLELVGLEGLLNRYPHELSG-----------GQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 487 LKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRL-HTIKQADAIWFMDDGKLLAQG 551
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
198-558 |
4.19e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 126.24 E-value: 4.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 198 KFLDVLQGLTTLKLYGRTEREAQaIEKSSLD----FRDATM-----VVLKTAFLSGLMLEFISMLSTgvvalevaLQMVV 268
Cdd:PLN03232 1091 QFGEALNGLSSIRAYKAYDRMAK-INGKSMDnnirFTLANTssnrwLTIRLETLGGVMIWLTATFAV--------LRNGN 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 269 WENLTFFSGFLILVLApeYYLAIKDL-GGAFHTG---RGSMGAADRIFEALDAPDER--LTWGDRMLTS--RTPDLELDA 340
Cdd:PLN03232 1162 AENQAGFASTMGLLLS--YTLNITTLlSGVLRQAskaENSLNSVERVGNYIDLPSEAtaIIENNRPVSGwpSRGSIKFED 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 341 VSFAYEGGrftLDP----LSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYIS 416
Cdd:PLN03232 1240 VHLRYRPG---LPPvlhgLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIP 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 QNPYLFAGTVADNIALGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFD 496
Cdd:PLN03232 1317 QSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 497 EPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
352-500 |
7.36e-30 |
|
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: 114.67 E-value: 7.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAG-TVADNI 430
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 431 ALG-------ETADEIKILEAANAAGLNDVIAQ-LPNGIHT----ElgeggyglsggeRQRLALARAFLKRPGIILFDEP 498
Cdd:pfam00005 81 RLGlllkglsKREKDARAEEALEKLGLGDLADRpVGERPGTlsggQ------------RQRVAIARALLTKPKLLLLDEP 148
|
..
gi 2048238220 499 TT 500
Cdd:pfam00005 149 TA 150
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
336-560 |
1.10e-29 |
|
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: 117.02 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYI 415
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAG-TVADNIAL-----GETADEIK--ILEAANAAGLNDVI------AQLPNGihtelgeggyglsggERQRLA 481
Cdd:cd03295 81 IQQIGLFPHmTVEENIALvpkllKWPKEKIRerADELLALVGLDPAEfadrypHELSGG---------------QQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 482 LARAFLKRPGIILFDEPTTGLDLVT----EQIVRRSIEELSReaTLVTVAHRL-HTIKQADAIWFMDDGKLLAQGTHDEL 556
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITrdqlQEEFKRLQQELGK--TIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
....
gi 2048238220 557 LSVP 560
Cdd:cd03295 224 LRSP 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
332-566 |
5.53e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 117.89 E-value: 5.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 332 RTPDLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetytdsswydT 411
Cdd:COG3842 2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----------T 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 --------IGYISQN----PYLfagTVADNIA-----LGETADEI--KILEAANAAGLNDV----IAQLPNGihtelgeg 468
Cdd:COG3842 71 glppekrnVGMVFQDyalfPHL---TVAENVAfglrmRGVPKAEIraRVAELLELVGLEGLadryPHQLSGG-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 469 gyglsggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRlhtikQADAIWF----- 541
Cdd:COG3842 140 -------QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElgITFIYVTHD-----QEEALALadria 207
|
250 260
....*....|....*....|....*.
gi 2048238220 542 -MDDGKLLAQGTHDELLSVPqyADLF 566
Cdd:COG3842 208 vMNDGRIEQVGTPEEIYERP--ATRF 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
341-546 |
8.51e-29 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 113.33 E-value: 8.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 341 VSFAYEGGR----FTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGepletytdsswydTIGYIS 416
Cdd:cd03250 6 ASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 QNPYLFAGTVADNIALGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFD 496
Cdd:cd03250 73 QEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 497 EPTTGLD-LVTEQIVRRSI-EELSREATLVTVAHRLHTIKQADAIWFMDDGK 546
Cdd:cd03250 153 DPLSAVDaHVGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
336-558 |
1.05e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.08 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDpLSgmIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYD---TI 412
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD-LT--IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL---TALPPAErpvSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 gyISQNPYLFAG-TVADNIALG-------ETADEIKILEAANAAGLNDVIAQLPN----GihtelgeggyglsggERQRL 480
Cdd:COG3840 76 --LFQENNLFPHlTVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLPGqlsgG---------------QRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 481 ALARAFL-KRPgIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDEL 556
Cdd:COG3840 139 ALARCLVrKRP-ILLLDEPFSALDPALRQEMLDLVDELCRErgLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
..
gi 2048238220 557 LS 558
Cdd:COG3840 218 LD 219
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
30-311 |
1.25e-28 |
|
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: 115.33 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 30 LSILAQ---AYLIVDIVDQVFLKNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQLLDRYTSnpie 106
Cdd:cd18781 7 ISLLANiafVFSIANLLQKLLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 107 tsLSGQSGKKVS------VFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFIiigiA 180
Cdd:cd18781 83 --LGPSYQEKVStaevvqLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISII----A 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 181 TQKKSEQQMEKM-NQFSG---KFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFISMlstG 256
Cdd:cd18781 157 VQKIAKKLLSKYwGSYTDlgdSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVAY---G 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2048238220 257 VVALEVALqmVVWE----NLTFFSGFLILVLAPEYYLAIKDLGGAFHTGRGSMGAADRI 311
Cdd:cd18781 234 GAALGIIL--ALLQfangSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAASDKI 290
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
330-528 |
1.53e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 114.42 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 330 TSRTPDLELDAVSFAY--EGGRFT-LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDS 406
Cdd:COG1116 2 SAAAPALELRGVSKRFptGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 407 swydtIGYISQNPYLFA-GTVADNIALG-----ETADEIK--ILEAANAAGLNDVIAQLPN----Gihtelgeggyglsg 474
Cdd:COG1116 82 -----RGVVFQEPALLPwLTVLDNVALGlelrgVPKAERRerARELLELVGLAGFEDAYPHqlsgG-------------- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 475 gERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAH 528
Cdd:COG1116 143 -MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTH 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
337-533 |
2.41e-28 |
|
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: 112.63 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 337 ELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETytDSSWydtIGYIS 416
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK--ERKR---IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 QNPYL---FAGTVADNIALG-----------ETADEIKILEAANAAGLNDV----IAQLPNGihtelgeggyglsggERQ 478
Cdd:cd03235 75 QRRSIdrdFPISVRDVVLMGlyghkglfrrlSKADKAKVDEALERVGLSELadrqIGELSGG---------------QQQ 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 479 RLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE-ATLVTVAHRLHTI 533
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLV 195
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
334-547 |
5.65e-28 |
|
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: 111.35 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 334 PDLE--LDAVSFAYEGGrftldplsgmiptgAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGE-----PLETYTDS 406
Cdd:cd03369 18 PDLPpvLKNVSFKVKAG--------------EKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 407 swydtIGYISQNPYLFAGTVADNIALGETADEIKILEAANAA--GLNdviaqLPNGihtelgeggyglsggERQRLALAR 484
Cdd:cd03369 84 -----LTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVSegGLN-----LSQG---------------QRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 485 AFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKL 547
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
352-558 |
8.35e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 119.07 E-value: 8.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIA 431
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 432 LGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVR 511
Cdd:PLN03130 1335 PFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ 1414
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2048238220 512 RSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:PLN03130 1415 KTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
336-551 |
9.99e-28 |
|
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: 111.06 E-value: 9.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFT---LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYD-- 410
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 -TIGYISQNPY-----LFagTVADNIA---------LGETADEIKILEAANAAGLNDVIA-----QLPNGihtelgeggy 470
Cdd:cd03257 82 kEIQMVFQDPMsslnpRM--TIGEQIAeplrihgklSKKEARKEAVLLLLVGVGLPEEVLnryphELSGG---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 471 glsggERQRLALARAFLKRPGIILFDEPTTGLDLVTE-QIVRRsIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGK 546
Cdd:cd03257 150 -----QRQRVAIARALALNPKLLIADEPTSALDVSVQaQILDL-LKKLQEElgLTLLFITHDLGVVAKiADRVAVMYAGK 223
|
....*
gi 2048238220 547 LLAQG 551
Cdd:cd03257 224 IVEEG 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
348-558 |
1.08e-27 |
|
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: 114.43 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 348 GRFTLD-----PLSGMiptgahVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPletytdssWYDT----------- 411
Cdd:COG4148 12 GGFTLDvdftlPGRGV------TALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV--------LQDSargiflpphrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 -IGYISQNPYLFAG-TVADNIALGETadeiKILEAANAAGLNDVIAQLpnGIHT------------ElgeggyglsggeR 477
Cdd:COG4148 78 rIGYVFQEARLFPHlSVRGNLLYGRK----RAPRAERRISFDEVVELL--GIGHlldrrpatlsggE------------R 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 478 QRLALARAFLKRPGIILFDEPTTGLDLvteqiVRRS-----IEELSREATL--VTVAH------RLhtikqADAIWFMDD 544
Cdd:COG4148 140 QRVAIGRALLSSPRLLLMDEPLAALDL-----ARKAeilpyLERLRDELDIpiLYVSHsldevaRL-----ADHVVLLEQ 209
|
250
....*....|....
gi 2048238220 545 GKLLAQGTHDELLS 558
Cdd:COG4148 210 GRVVASGPLAEVLS 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
329-557 |
1.27e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.31 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 329 LTSRTPDLELDAVSFAYEGG-RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSS 407
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 408 WYDTIGYISQNP-YLFAG-TVADNIALG-----ETADEIK--ILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQ 478
Cdd:PRK13632 81 IRKKIGIIFQNPdNQFIGaTVEDDIAFGlenkkVPPKKMKdiIDDLAKKVGMEDYLDKEPQNL-----------SGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 479 RLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDEL 556
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
.
gi 2048238220 557 L 557
Cdd:PRK13632 230 L 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
335-566 |
1.51e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 110.93 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 335 DLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYD-TIG 413
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKDrNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 414 YISQNPYLF-AGTVADNIALG-----ETADEI--KILEAANAAGLNDVI----AQLPNGihtelgeggyglsggERQRLA 481
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlklrkVPKAEIdrRVREAAELLGLEDLLdrkpKQLSGG---------------QRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 482 LARAFLKRPGIILFDEPTTGLD--LVTEqiVRRSIEELSRE--ATLVTVAHRlhtikQADA------IWFMDDGKLLAQG 551
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDakLRVE--MRAEIKRLHRRlgTTTIYVTHD-----QVEAmtladrIAVMNDGRIQQVG 216
|
250
....*....|....*
gi 2048238220 552 THDELLSVPqyADLF 566
Cdd:COG3839 217 TPEELYDRP--ANLF 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
337-547 |
1.69e-26 |
|
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: 106.96 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 337 ELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwydTIGYIS 416
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRK---SIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 QNP--YLFAGTVADNIALG--ETADEI----KILEAANAAGLNDVIAQ-LPNGihtelgeggyglsggERQRLALARAFL 487
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGlkELDAGNeqaeTVLKDLDLYALKERHPLsLSGG---------------QKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 488 KRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVA-HRLHTI-KQADAIWFMDDGKL 547
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVItHDYEFLaKVCDRVLLLANGAI 204
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
336-569 |
2.93e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.85 E-value: 2.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYegGRFT-LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwyD-TIG 413
Cdd:COG1118 3 IEVRNISKRF--GSFTlLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPR--ErRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 414 YISQNPYLFAG-TVADNIALG-----ETADEIK-----ILEAANAAGLNDV-IAQLPNGihtelgeggyglsggERQRLA 481
Cdd:COG1118 79 FVFQHYALFPHmTVAENIAFGlrvrpPSKAEIRarveeLLELVQLEGLADRyPSQLSGG---------------QRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 482 LARAFLKRPGIILFDEPTTGLD-LVTEQI---VRRSIEELSReaTLVTVAH------RLhtikqADAIWFMDDGKLLAQG 551
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDaKVRKELrrwLRRLHDELGG--TTVFVTHdqeealEL-----ADRVVVMNQGRIEQVG 216
|
250
....*....|....*...
gi 2048238220 552 THDELLSVPqyADLFTLQ 569
Cdd:COG1118 217 TPDEVYDRP--ATPFVAR 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
302-570 |
3.07e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 112.88 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 302 RGSmGAADRIFEALDAPDErLTWGDRMLTSRTPDLELDAVSFAYEGG--------RFTLDPlsgmiptGAHVALVGASGS 373
Cdd:PRK10789 282 RGS-AAYSRIRAMLAEAPV-VKDGSEPVPEGRGELDVNIRQFTYPQTdhpalenvNFTLKP-------GQMLGICGPTGS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 374 GKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALGE-TADEIKILEAANAAGLND 452
Cdd:PRK10789 353 GKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHD 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 453 VIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHT 532
Cdd:PRK10789 433 DILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSA 512
|
250 260 270
....*....|....*....|....*....|....*....
gi 2048238220 533 IKQADAIWFMDDGKLLAQGTHDELLSVPQ-YADLFTLQK 570
Cdd:PRK10789 513 LTEASEILVMQHGHIAQRGNHDQLAQQSGwYRDMYRYQQ 551
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
336-561 |
3.90e-26 |
|
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: 106.90 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGM---IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYD-- 410
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVslsVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 -TIGYISQNPYLFAG-TVADNIAL-----GETADEI--KILEAANAAGLND----VIAQLPNGihtelgeggyglsggER 477
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIeeRVLELLELVGLEDkadaYPAQLSGG---------------QK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 478 QRLALARAFLKRPGIILFDEPTTGLD-LVTEQIVRRsIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTH 553
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDpETTQSILAL-LRDINRElgLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*...
gi 2048238220 554 DELLSVPQ 561
Cdd:cd03258 226 EEVFANPQ 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
328-549 |
4.04e-26 |
|
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: 106.75 E-value: 4.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 328 MLTSRTPDLELDAVSFAYEGGRFTLDPLSGM---IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYT 404
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAGELTILKGIsleVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 405 DsswyDT--------IGYISQNPYLFAG-TVADNIAL-----GETADEIKILEAANAAGLNDVI----AQLPNGihtElg 466
Cdd:COG4181 81 E----DArarlrarhVGFVFQSFQLLPTlTALENVMLplelaGRRDARARARALLERVGLGHRLdhypAQLSGG---E-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 467 eggyglsggeRQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQADAIWFMDD 544
Cdd:COG4181 152 ----------QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErgTTLVLVTHDPALAARCDRVLRLRA 221
|
....*
gi 2048238220 545 GKLLA 549
Cdd:COG4181 222 GRLVE 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
347-561 |
4.69e-26 |
|
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: 106.65 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 347 GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwyDTIGYISQNPYLFAG-T 425
Cdd:cd03299 10 WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHmT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 426 VADNIALG-------ETADEIKILEAANAAG----LNDVIAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIIL 494
Cdd:cd03299 88 VYKNIAYGlkkrkvdKKEIERKVLEIAEMLGidhlLNRKPETLSGG---------------EQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2048238220 495 FDEPTTGLDLVTEQIVRRSIEELSREATlVTVAHRLHTIKQA----DAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFG-VTVLHVTHDFEEAwalaDKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
345-547 |
4.91e-26 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 106.28 E-value: 4.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 345 YEGGRFTLDPLSGM---IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYD----TIGYISQ 417
Cdd:TIGR02211 11 YQEGKLDTRVLKGVslsIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkKLGFIYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 418 NPYLFAG-TVADNIALGETADEIKILEAANAA-------GLNDVIAQLPNGIhtelgeggyglSGGERQRLALARAFLKR 489
Cdd:TIGR02211 91 FHHLLPDfTALENVAMPLLIGKKSVKEAKERAyemlekvGLEHRINHRPSEL-----------SGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 490 PGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQADAIWFMDDGKL 547
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRElnTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
336-556 |
9.35e-26 |
|
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: 106.11 E-value: 9.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDS---SWYDTI 412
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYLFAG-TVADNI---ALGET------------ADEIKILEAANAAGLNDVI----AQLPNGihtelgeggygl 472
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVlsgRLGRRstwrslfglfpkEEKQRALAALERVGLLDKAyqraDQLSGG------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 473 sggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLA 549
Cdd:cd03256 149 ---QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAREyADRIVGLKDGRIVF 225
|
....*..
gi 2048238220 550 QGTHDEL 556
Cdd:cd03256 226 DGPPAEL 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
359-561 |
1.28e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 105.46 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLeTYTDSSWYD---TIGYISQNPYLFAG-TVADNIALG- 433
Cdd:COG1126 24 VEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKlrrKVGMVFQQFNLFPHlTVLENVTLAp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 434 --------ETADEI--KILEAAnaaGLNDVI----AQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPT 499
Cdd:COG1126 103 ikvkkmskAEAEERamELLERV---GLADKAdaypAQLSGG---------------QQQRVAIARALAMEPKVMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 500 TGLD--LVTEqiVRRSIEELSREA-TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:COG1126 165 SALDpeLVGE--VLDVMRDLAKEGmTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
334-503 |
1.30e-25 |
|
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: 104.48 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 334 PDLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETyTDSSWYDTIG 413
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 414 YISQNPYLFAG-TVADNIAL-----GETADEIKILEAANAAGLNDV----IAQLPNGIhtelgeggyglsggeRQRLALA 483
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLAGLadlpVRQLSAGQ---------------KRRVALA 143
|
170 180
....*....|....*....|
gi 2048238220 484 RAFLKRPGIILFDEPTTGLD 503
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALD 163
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
348-561 |
6.88e-25 |
|
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: 103.57 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 348 GRFT-LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEpletytDSSWYDT----IGYISQNPYLF 422
Cdd:cd03296 13 GDFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE------DATDVPVqernVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 423 AG-TVADNIALG---------ETADEIK-----ILEAANAAGLNDVI-AQLPNGihtelgeggyglsggERQRLALARAF 486
Cdd:cd03296 87 RHmTVFDNVAFGlrvkprserPPEAEIRakvheLLKLVQLDWLADRYpAQLSGG---------------QRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 487 LKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAH-RLHTIKQADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElhVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
336-551 |
1.13e-24 |
|
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: 101.89 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRfTLDPLSGMIPTGAHvALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSsWYDTIGYI 415
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAGTVA----DNIAL--GETADEIK--ILEAANAAGLNDV----IAQLPNGIhtelgeggyglsggeRQRLALA 483
Cdd:cd03264 78 PQEFGVYPNFTVreflDYIAWlkGIPSKEVKarVDEVLELVNLGDRakkkIGSLSGGM---------------RRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 484 RAFLKRPGIILFDEPTTGLDlVTEQI-VRRSIEELSREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQG 551
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLD-PEERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
336-547 |
1.27e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.05 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSswyD----- 410
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRR---Eipylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 -TIGYISQNPYLFAG-TVADNIAL-----GETADEIK--ILEAANAAGLNDVIAQLPN----GIhtelgeggyglsggeR 477
Cdd:COG2884 79 rRIGVVFQDFRLLPDrTVYENVALplrvtGKSRKEIRrrVREVLDLVGLSDKAKALPHelsgGE---------------Q 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 478 QRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVA-HRLHTIKQADA-IWFMDDGKL 547
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRL 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
336-561 |
1.39e-24 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 102.32 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYD-TIGY 414
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKrPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAG-TVADNIALGET-----ADEIK--ILEAANAAGL----NDVIAQLPNGihtelgeggyglsggERQRLAL 482
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGLRlkklpKAEIKerVAEALDLVQLegyaNRKPSQLSGG---------------QQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 483 ARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAH-RLHTIKQADAIWFMDDGKLLAQGTHDELLSV 559
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElgITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
..
gi 2048238220 560 PQ 561
Cdd:cd03300 222 PA 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
365-561 |
6.97e-24 |
|
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: 100.59 E-value: 6.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 365 VALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDT----IGYISQNPYLFAG-TVADNIALG------ 433
Cdd:cd03219 29 HGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI---TGLPPHEIarlgIGRTFQIPRLFPElTVLENVMVAaqartg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 434 ----------------ETADEikILEAANAAGLNDVIA-QLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFD 496
Cdd:cd03219 106 sglllararreerearERAEE--LLERVGLADLADRPAgELSYG---------------QQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 497 EPTTGLDLV-TEQIVRRsIEELSRE-ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:cd03219 169 EPAAGLNPEeTEELAEL-IRELRERgITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
389-559 |
8.78e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 106.65 E-value: 8.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 389 DSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALG-ETADEIKILEAANAAGLNDVIAQLPNGIHTELGE 467
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGP 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 468 GGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHTIKQADAIWFMDD- 544
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNNp 1434
|
170
....*....|....*....
gi 2048238220 545 ---GKLL-AQGTHDELLSV 559
Cdd:PTZ00265 1435 drtGSFVqAHGTHEELLSV 1453
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
365-547 |
1.08e-23 |
|
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: 99.14 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 365 VALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLeTYTDSSWYD---TIGYISQNPYLFAG-TVADNIALG------- 433
Cdd:cd03262 29 VVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINElrqKVGMVFQQFNLFPHlTVLENITLApikvkgm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 434 --ETADEI--KILEAAnaaGLNDVI----AQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLD-- 503
Cdd:cd03262 108 skAEAEERalELLEKV---GLADKAdaypAQLSGG---------------QQQRVAIARALAMNPKVMLFDEPTSALDpe 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2048238220 504 LVTEqiVRRSIEELSREA-TLVTVAHRLHTIKQ-ADAIWFMDDGKL 547
Cdd:cd03262 170 LVGE--VLDVMKDLAEEGmTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
345-527 |
1.82e-23 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 97.88 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 345 YEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLEtYTDSS---WYDTIGYISQNP-- 419
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGlleRRQRVGLVFQDPdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 420 YLFAGTVADNIA-----LGETADEI--KILEAANAAGLNDVIAQLPNGI-HTElgeggyglsggeRQRLALARAFLKRPG 491
Cdd:TIGR01166 80 QLFAADVDQDVAfgplnLGLSEAEVerRVREALTAVGASGLRERPTHCLsGGE------------KKRVAIAGAVAMRPD 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 2048238220 492 IILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVA 527
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVIS 183
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
336-551 |
1.86e-23 |
|
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: 98.59 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFT---LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDG-----EPLETYTDss 407
Cdd:cd03266 2 ITADALTKRFRDVKKTvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEARRR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 408 wydtIGYISQNPYLFAG-TVADNIAL-----GETADEIKileaanaAGLNDVIAQLpnGIHTELGEGGYGLSGGERQRLA 481
Cdd:cd03266 80 ----LGFVSDSTGLYDRlTARENLEYfaglyGLKGDELT-------ARLEELADRL--GMEELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 482 LARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVA-HRLHTIKQ-ADAIWFMDDGKLLAQG 551
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
346-558 |
3.20e-23 |
|
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: 99.54 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 346 EGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDsGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGT 425
Cdd:cd03289 14 EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 426 VADNI-ALGETADEiKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDL 504
Cdd:cd03289 93 FRKNLdPYGKWSDE-EIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 505 VTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:cd03289 172 ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
265-529 |
9.97e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.19 E-value: 9.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 265 QMVVWE-NLTFFSG--------FLILVLAPeYYLAIK-DLGG------AFHTGRGSMG--------------AADRI--- 311
Cdd:COG4178 260 RLIRRQrNLTFFTTgygqlaviFPILVAAP-RYFAGEiTLGGlmqaasAFGQVQGALSwfvdnyqslaewraTVDRLagf 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 312 FEALDAPDERLTWGDRMLTSRTPDLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSG 391
Cdd:COG4178 339 EEALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 392 RVLV--DGEPLetytdsswydtigYISQNPYLFAGTVADNIALGETADEI---KILEAANAAGLNDVIAQLpngihTELG 466
Cdd:COG4178 419 RIARpaGARVL-------------FLPQRPYLPLGTLREALLYPATAEAFsdaELREALEAVGLGHLAERL-----DEEA 480
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 467 EGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHR 529
Cdd:COG4178 481 DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
336-558 |
1.20e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.84 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLEtYTDSSWYD---TI 412
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEvrkTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNP--YLFAGTVADNIA-----LGETADEI--KILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLALA 483
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAfgplnLGLSKEEVekRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 484 RAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRLHTI-KQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGiTIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
341-572 |
1.22e-22 |
|
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: 99.42 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 341 VSFAYEGGRFTLDpLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEpletytdsSWYDT--------- 411
Cdd:TIGR02142 3 ARFSKRLGDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR--------TLFDSrkgiflppe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 ---IGYISQNPYLFAG-TVADNIALG---ETADEIKILEAANAA--GLNDVIAQLPNGIhtelgeggyglSGGERQRLAL 482
Cdd:TIGR02142 74 krrIGYVFQEARLFPHlSVRGNLRYGmkrARPSERRISFERVIEllGIGHLLGRLPGRL-----------SGGEKQRVAI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 483 ARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATL--VTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSV 559
Cdd:TIGR02142 143 GRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIpiLYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222
|
250
....*....|...
gi 2048238220 560 PQYADLFTLQKGV 572
Cdd:TIGR02142 223 PDLPWLAREDQGS 235
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
352-558 |
1.25e-22 |
|
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: 97.29 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIA 431
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 432 LGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVR 511
Cdd:cd03288 117 PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2048238220 512 RSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:cd03288 197 KVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
341-551 |
1.34e-22 |
|
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: 96.21 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 341 VSFAYEGGRFTLDpLSGMIPTGAhVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPletytdssWYDT--------- 411
Cdd:cd03297 4 VDIEKRLPDFTLK-IDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV--------LFDSrkkinlppq 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 ---IGYISQNPYLFAG-TVADNIALG---ETADEIKILEAANAAGL------NDVIAQLPNGihtelgeggyglsggERQ 478
Cdd:cd03297 74 qrkIGLVFQQYALFPHlNVRENLAFGlkrKRNREDRISVDELLDLLgldhllNRYPAQLSGG---------------EKQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 479 RLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVT--VAHRLHTI-KQADAIWFMDDGKLLAQG 551
Cdd:cd03297 139 RVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVifVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
303-570 |
1.71e-22 |
|
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: 102.68 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 303 GSMGAADRIFEALDAPDER---------------LTWGDRMLTSRTPD---LELDAVSFAY-EGGRFTLDPLSGMIPTGA 363
Cdd:TIGR01271 1167 GLMRSVSRVFKFIDLPQEEprpsggggkyqlstvLVIENPHAQKCWPSggqMDVQGLTAKYtEAGRAVLQDLSFSVEGGQ 1246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 364 HVALVGASGSGKTTVLNVLSGLVKPDsGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALGETADEIKILE 443
Cdd:TIGR01271 1247 RVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWK 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 444 AANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATL 523
Cdd:TIGR01271 1326 VAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTV 1405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 524 VTVAHRLH--------------TIKQADAIwfmddGKLLAQGTH-DELLSVPQYADLFTLQK 570
Cdd:TIGR01271 1406 ILSEHRVEallecqqflviegsSVKQYDSI-----QKLLNETSLfKQAMSAADRLKLFPLHR 1462
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
345-556 |
3.55e-22 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 95.26 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 345 YEGGRFT-LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwYDTIGYISQNPYLFA 423
Cdd:cd03263 10 YKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA-RQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 424 G-TVADNIAL-----GETADEIK--ILEAANAAGLNDV----IAQLPNGIhtelgeggyglsggeRQRLALARAFLKRPG 491
Cdd:cd03263 89 ElTVREHLRFyarlkGLPKSEIKeeVELLLRVLGLTDKankrARTLSGGM---------------KRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 492 IILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDEL 556
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
18-311 |
4.50e-22 |
|
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: 96.47 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 18 IVGLVIAAVMIGLSILAQAYLIVDIVDQVfLKNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQLL 97
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV-IPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 98 DRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFIII 177
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 178 GIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFISMLSTGV 257
Cdd:cd07346 160 RRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 258 VALEVALQMVVWE----NLTFFSGFLILVLAPeyylaIKDLGGAFHTGRGSMGAADRI 311
Cdd:cd07346 240 VLLYGGYLVLQGSltigELVAFLAYLGMLFGP-----IQRLANLYNQLQQALASLERI 292
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
347-539 |
4.89e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.84 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 347 GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEpletytdsswyDTIGYISQN---PYLFA 423
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRsevPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 424 GTVADNIALGE----------TADEIKILEAANAA-GLNDV----IAQLPNGihtelgeggyglsggERQRLALARAFLK 488
Cdd:NF040873 72 LTVRDLVAMGRwarrglwrrlTRDDRAAVDDALERvGLADLagrqLGELSGG---------------QRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 489 RPGIILFDEPTTGLDLVTEQIVRRSIEELSRE-ATLVTVAHRLHTIKQADAI 539
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPC 188
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
336-566 |
5.06e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.48 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYD-TIGY 414
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQrDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAG-TVADNIA-----LGETADEIK-----ILEAANAAGLND-VIAQLPNGihtelgeggyglsggERQRLAL 482
Cdd:PRK11432 83 VFQSYALFPHmSLGENVGyglkmLGVPKEERKqrvkeALELVDLAGFEDrYVDQISGG---------------QQQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 483 ARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAH-RLHTIKQADAIWFMDDGKLLAQGTHDELLSV 559
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfnITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
....*..
gi 2048238220 560 PqyADLF 566
Cdd:PRK11432 228 P--ASRF 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
347-551 |
5.09e-22 |
|
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: 94.21 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 347 GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEplETYTDSSWYDTIGYISQNPYLFAG-T 425
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALIEAPGFYPNlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 426 VADNIalgETADEIKILEAANAAGLNDVIaqlpnGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLV 505
Cdd:cd03268 89 ARENL---RLLARLLGIRKKRIDEVLDVV-----GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2048238220 506 TEQIVRRSIEELSREATLVTVA-HRLHTIKQ-ADAIWFMDDGKLLAQG 551
Cdd:cd03268 161 GIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
336-550 |
7.84e-22 |
|
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: 92.49 E-value: 7.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRfTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSswydtigyi 415
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 sqnpylfagtvadnialgetadeikileAANAAGLNdVIAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILF 495
Cdd:cd03216 71 ----------------------------DARRAGIA-MVYQLSVG---------------ERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 496 DEPTTGLDLVTEQIVRRSIEEL-SREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQ 550
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLrAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
336-558 |
8.83e-22 |
|
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: 94.04 E-value: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSfAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDT---- 411
Cdd:cd03224 1 LEVENLN-AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI---TGLPPHERarag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 IGYISQNPYLFAG-TVADNIALGETADEikilEAANAAGLNDVIAQLPN--------------GihtelgeggyglsggE 476
Cdd:cd03224 77 IGYVPEGRRIFPElTVEENLLLGAYARR----RAKRKARLERVYELFPRlkerrkqlagtlsgG---------------E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 477 RQRLALARAFLKRPGIILFDEPTTGLD-LVTEQIVRRsIEELSRE-ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTH 553
Cdd:cd03224 138 QQMLAIARALMSRPKLLLLDEPSEGLApKIVEEIFEA-IRELRDEgVTILLVEQNARFALEiADRAYVLERGRVVLEGTA 216
|
....*
gi 2048238220 554 DELLS 558
Cdd:cd03224 217 AELLA 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
336-547 |
1.14e-21 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 93.47 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYD-TIGY 414
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLPPKDrDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAG-TVADNIALG-----ETADEI--KILEAANAAGLNDVI----AQLPNGihtelgeggyglsggERQRLAL 482
Cdd:cd03301 77 VFQNYALYPHmTVYDNIAFGlklrkVPKDEIdeRVREVAELLQIEHLLdrkpKQLSGG---------------QRQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 483 ARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAH-RLHTIKQADAIWFMDDGKL 547
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
336-551 |
1.23e-21 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 93.33 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPlsgMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwyDTIGYI 415
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDL---TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAG-TVADNIALGET-------ADEIKILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLALARAFL 487
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGLSpglkltaEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 488 KRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQG 551
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
333-555 |
1.47e-21 |
|
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: 94.34 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDT- 411
Cdd:COG0411 2 DPLLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI---TGLPPHRIa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 ---IGYISQNPYLFAG-TVADNIALG----------------------ETADEIKILEAANAAGLNDVI----AQLPNGi 461
Cdd:COG0411 78 rlgIARTFQNPRLFPElTVLENVLVAaharlgrgllaallrlprarreEREARERAEELLERVGLADRAdepaGNLSYG- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 462 htelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLDLV-TEQIVRRsIEELSREA--TLVTVAHRLHTIKQ-AD 537
Cdd:COG0411 157 --------------QQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELAEL-IRRLRDERgiTILLIEHDMDLVMGlAD 221
|
250
....*....|....*...
gi 2048238220 538 AIWFMDDGKLLAQGTHDE 555
Cdd:COG0411 222 RIVVLDFGRVIAEGTPAE 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-558 |
1.49e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.70 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 334 PDLELDAVSFAYEGG-RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDT- 411
Cdd:PRK13635 4 EIIRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETVWDVr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 --IGYISQNP-YLFAG-TVADNIALG-ETA----DEI--KILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRL 480
Cdd:PRK13635 81 rqVGMVFQNPdNQFVGaTVQDDVAFGlENIgvprEEMveRVDQALRQVGMEDFLNREPHRL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 481 ALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
329-547 |
1.80e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.97 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 329 LTSRTPdLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDssw 408
Cdd:PRK11247 7 LNQGTP-LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 409 yDTIGYISQNPYLFAGTVADNIALGETAD-EIKILEAANAAGL----NDVIAQLPNGihtelgeggyglsggERQRLALA 483
Cdd:PRK11247 82 -DTRLMFQDARLLPWKKVIDNVGLGLKGQwRDAALQALAAVGLadraNEWPAALSGG---------------QKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 484 RAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRL-HTIKQADAIWFMDDGKL 547
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
343-545 |
2.61e-21 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 92.78 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 343 FAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVL----VDGEPLETYTDSSWYDTIGYISQN 418
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 419 PYLFAGTVADNIALGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEP 498
Cdd:cd03290 88 PWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2048238220 499 TTGLDL-VTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQADAIWFMDDG 545
Cdd:cd03290 168 FSALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
346-569 |
4.44e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 92.69 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 346 EGGRftLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVkPDSGRVLVDGEPLETYTDSSWYDTIGYISQN-PYLFAG 424
Cdd:PRK03695 8 VSTR--LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 425 TV--------ADNIALGETADEIKILeaANAAGLNDV----IAQLPNGihtelgeggyglsggERQRLALARAFLK-RPG 491
Cdd:PRK03695 85 PVfqyltlhqPDKTRTEAVASALNEV--AEALGLDDKlgrsVNQLSGG---------------EWQRVRLAAVVLQvWPD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 492 I------ILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVA-HRL-HTIKQADAIWFMDDGKLLAQGTHDELLSVPQYA 563
Cdd:PRK03695 148 InpagqlLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSsHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTPENLA 227
|
....*.
gi 2048238220 564 DLFTLQ 569
Cdd:PRK03695 228 QVFGVN 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
326-558 |
5.07e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 97.89 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 326 DRMLTSRTP-DLELDAVS-----FAYE--GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDS-GRVLVD 396
Cdd:PLN03130 599 ERVLLPNPPlEPGLPAISikngyFSWDskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIR 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 397 GepletytdsswydTIGYISQNPYLFAGTVADNIALGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGE 476
Cdd:PLN03130 679 G-------------TVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQ 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 477 RQRLALARAFLKRPGIILFDEPTTGLDL-VTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDE 555
Cdd:PLN03130 746 KQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEE 825
|
...
gi 2048238220 556 LLS 558
Cdd:PLN03130 826 LSN 828
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
336-560 |
1.10e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.17 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYI 415
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNP--YLFAGTVADNIALG-------ETADEIKILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLALARAF 486
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 487 LKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVP 560
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
367-560 |
1.19e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 93.33 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 367 LVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYdtIGYISQNPYLFAG-TVADNIALG-----ETADEIK 440
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH--INMVFQSYALFPHmTVEENVAFGlkmrkVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 441 --ILEAANAAGLNDV----IAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSI 514
Cdd:TIGR01187 79 prVLEALRLVQLEEFadrkPHQLSGG---------------QQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2048238220 515 EELSRE--ATLVTVAH-RLHTIKQADAIWFMDDGKLLAQGTHDELLSVP 560
Cdd:TIGR01187 144 KTIQEQlgITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
336-558 |
1.21e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.17 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAY-EGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDS---GRVLVDGEPLETYTDSSWYDT 411
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 IGYISQNP-YLFAG-TVADNIALG------ETADEIKIL-EAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLAL 482
Cdd:PRK13640 86 VGIVFQNPdNQFVGaTVGDDVAFGlenravPRPEMIKIVrDVLADVGMLDYIDSEPANL-----------SGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 483 ARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
367-561 |
1.29e-20 |
|
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: 91.94 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 367 LVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYD----TIGYISQNPYLFAG-TVADNIALG-------E 434
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTVLENVAFGlevqgvpR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 435 TADEIKILEAANAAGLNDVIAQLPN----GIhtelgeggyglsggeRQRLALARAFLKRPGIILFDEPTTGLDlvteQIV 510
Cdd:cd03294 135 AEREERAAEALELVGLEGWEHKYPDelsgGM---------------QQRVGLARALAVDPDILLMDEAFSALD----PLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 511 RRSIEE----LSREA--TLVTVAHRL-HTIKQADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:cd03294 196 RREMQDellrLQAELqkTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNPA 253
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
335-551 |
1.51e-20 |
|
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: 89.53 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 335 DLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKP--DSGRVLVDGEPLEtytDSSWYDTI 412
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLD---KRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYLFAG-TVADNIalgetadeikileaanaaglnDVIAQLpNGIHTElgeggyglsggERQRLALARAFLKRPG 491
Cdd:cd03213 85 GYVPQDDILHPTlTVRETL---------------------MFAAKL-RGLSGG-----------ERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 492 IILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRLHT--IKQADAIWFMDDGKLLAQG 551
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADTGrTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
335-569 |
1.71e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.23 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 335 DLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGY 414
Cdd:PRK11231 2 TLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAG-TVADNIALGE-----------TADEIKILEAANAAGLNDV----IAQLPNGihtelgeggyglsggERQ 478
Cdd:PRK11231 81 LPQHHLTPEGiTVRELVAYGRspwlslwgrlsAEDNARVNQAMEQTRINHLadrrLTDLSGG---------------QRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 479 RLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVahrLHTIKQA----DAIWFMDDGKLLAQGTH 553
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGkTVVTV---LHDLNQAsrycDHLVVLANGHVMAQGTP 222
|
250
....*....|....*.
gi 2048238220 554 DELLSVPQYADLFTLQ 569
Cdd:PRK11231 223 EEVMTPGLLRTVFDVE 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
336-557 |
2.21e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 90.53 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVL-VDGEPLETYtdsSWYD---T 411
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGE---DVWElrkR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 IGYIS---QNPYLFAGTVADNIALG-----------ETADEIKILEAANAAGLNDV----IAQLPNGihtelgeggygls 473
Cdd:COG1119 80 IGLVSpalQLRFPRDETVLDVVLSGffdsiglyrepTDEQRERARELLELLGLAHLadrpFGTLSQG------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 474 ggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHTIKQA-DAIWFMDDGKLLAQ 550
Cdd:COG1119 147 --EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
....*..
gi 2048238220 551 GTHDELL 557
Cdd:COG1119 225 GPKEEVL 231
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
347-561 |
3.58e-20 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 89.64 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 347 GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDT----IGYISQNPYLF 422
Cdd:TIGR04406 12 KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI---THLPMHERarlgIGYLPQEASIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 423 AG-TVADNI-ALGETADEIKilEAANAAGLNDVIAQLpnGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTT 500
Cdd:TIGR04406 89 RKlTVEENImAVLEIRKDLD--RAEREERLEALLEEF--QISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 501 GLDLVTEQIVRRSIEELsRE---ATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHL-KErgiGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
329-539 |
4.50e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.00 E-value: 4.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 329 LTSRTPDLELDAVSFAyEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSW 408
Cdd:PRK10247 1 MQENSPLLQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 409 YDTIGYISQNPYLFAGTVADNIAL-----GETADEIKILEAANAAGLNDV-----IAQLPNGihtelgeggyglsggERQ 478
Cdd:PRK10247 80 RQQVSYCAQTPTLFGDTVYDNLIFpwqirNQQPDPAIFLDDLERFALPDTiltknIAELSGG---------------EKQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 479 RLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVT--VAHRLHTIKQADAI 539
Cdd:PRK10247 145 RISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADKV 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
359-561 |
6.74e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.42 E-value: 6.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT--------IGYISQNPYLFAG-TVADN 429
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGlirqlrqhVGFVFQNFNLFPHrTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 430 IALGETADEIKILEAANAAGlNDVIAQLpnGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLD--LVTE 507
Cdd:PRK11264 106 IIEGPVIVKGEPKEEATARA-RELLAKV--GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpeLVGE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 508 qiVRRSIEELSREA-TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:PRK11264 183 --VLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
338-547 |
6.85e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.21 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 338 LDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEpletytdsswyDTIGYISQ 417
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 418 NPYLFAG-TVADNI--ALGETADEIKILEAANAAG----------------------------LNDVIAQLpnGIHTElg 466
Cdd:COG0488 69 EPPLDDDlTVLDTVldGDAELRALEAELEELEAKLaepdedlerlaelqeefealggweaearAEEILSGL--GFPEE-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 467 eggyglsGGERQ----------RLALARAFLKRPGIILFDEPTTGLDLvteqivrRSIEEL-----SREATLVTVAH-R- 529
Cdd:COG0488 145 -------DLDRPvselsggwrrRVALARALLSEPDLLLLDEPTNHLDL-------ESIEWLeeflkNYPGTVLVVSHdRy 210
|
250
....*....|....*....
gi 2048238220 530 -LHTIkqADAIWFMDDGKL 547
Cdd:COG0488 211 fLDRV--ATRILELDRGKL 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
336-561 |
8.35e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.91 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVS--FAYEGGRFT-LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT- 411
Cdd:COG1135 2 IELENLSktFPTKGGPVTaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 --IGYISQNPYLFAG-TVADNIAL-----GETADEI--KILEAANAAGLNDVI----AQLPNGihtelgeggyglsggER 477
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALpleiaGVPKAEIrkRVAELLELVGLSDKAdaypSQLSGG---------------QK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 478 QRLALARAFLKRPGIILFDEPTTGLDLVTEQivrrSIEELSREA------TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQ 550
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTR----SILDLLKDInrelglTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
250
....*....|.
gi 2048238220 551 GTHDELLSVPQ 561
Cdd:COG1135 223 GPVLDVFANPQ 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
352-561 |
9.06e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.72 E-value: 9.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDT-----IGYISQNP--YLFAG 424
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI---TDKKVKLSdirkkVGLVFQYPeyQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 425 TVADNIA-----LGETADEIK--ILEAANAAGLN-DVIA-----QLPNGihtelgeggyglsggERQRLALARAFLKRPG 491
Cdd:PRK13637 100 TIEKDIAfgpinLGLSEEEIEnrVKRAMNIVGLDyEDYKdkspfELSGG---------------QKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 492 IILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTI-KQADAIWFMDDGKLLAQGTHDEL-----------L 557
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEynMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVfkevetlesigL 244
|
....
gi 2048238220 558 SVPQ 561
Cdd:PRK13637 245 AVPQ 248
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
336-561 |
9.59e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 93.69 E-value: 9.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAY-EGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGY 414
Cdd:PTZ00243 1309 LVFEGVQMRYrEGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSM 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAGTVADNIALGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKR-PGII 493
Cdd:PTZ00243 1389 IPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFI 1468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 494 LFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:PTZ00243 1469 LMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
320-556 |
1.23e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 93.50 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 320 ERLTWGDRMLTSRTPDLELDAVSFAYEGGRF---------TLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKP-D 389
Cdd:PLN03232 592 EELLLSEERILAQNPPLQPGAPAISIKNGYFswdsktskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaE 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 390 SGRVLVDGepletytdsswydTIGYISQNPYLFAGTVADNIALGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGG 469
Cdd:PLN03232 672 TSSVVIRG-------------SVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERG 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 470 YGLSGGERQRLALARAFLKRPGIILFDEPTTGLDL-VTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLL 548
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
....*...
gi 2048238220 549 AQGTHDEL 556
Cdd:PLN03232 819 EEGTFAEL 826
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
337-561 |
1.55e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 90.25 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 337 ELDAVSFAYEGGRFT---LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT-- 411
Cdd:PRK11153 3 ELKNISKVFPQGGRTihaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 -IGYISQNPYLFAG-TVADNIAL-----GETADEIK--ILEAANAAGLNDVI----AQLPNGihtelgeggyglsggERQ 478
Cdd:PRK11153 83 qIGMIFQHFNLLSSrTVFDNVALplelaGTPKAEIKarVTELLELVGLSDKAdrypAQLSGG---------------QKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 479 RLALARAFLKRPGIILFDEPTTGLDLVTEqivrRSIEELSREA------TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQG 551
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATT----RSILELLKDInrelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
250
....*....|
gi 2048238220 552 THDELLSVPQ 561
Cdd:PRK11153 224 TVSEVFSHPK 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
352-556 |
1.75e-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: 93.05 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEpletytdsswydtIGYISQNPYLFAGTVADNIA 431
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 432 LGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTE-QIV 510
Cdd:TIGR01271 509 FGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkEIF 588
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2048238220 511 RRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDEL 556
Cdd:TIGR01271 589 ESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
22-284 |
1.93e-19 |
|
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: 88.47 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 22 VIAAVMIGLSILAQAYLIVDIVDQVF-LKNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQLLDRY 100
Cdd:pfam00664 5 ILLAILSGAISPAFPLVLGRILDVLLpDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 101 TSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFIIIGIA 180
Cdd:pfam00664 85 LRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 181 TQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFISMLSTgVVAL 260
Cdd:pfam00664 165 LRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY-ALAL 243
|
250 260
....*....|....*....|....
gi 2048238220 261 EVALQMVVWENLTFFSGFLILVLA 284
Cdd:pfam00664 244 WFGAYLVISGELSVGDLVAFLSLF 267
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
343-561 |
2.13e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.18 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 343 FAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTI------GYIS 416
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIklrkevGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 QNPYLFAG-TVADNIA-------LGETADEIKILEAAnaagLNDViaQLPNGIHTELGEGGYGLSGGERQRLALARAFLK 488
Cdd:PRK14246 97 QQPNPFPHlSIYDNIAyplkshgIKEKREIKKIVEEC----LRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 489 RPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPK 244
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
355-551 |
2.18e-19 |
|
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: 87.33 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 355 LSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPD---SGRVLVDGEPLETYTdssWYDTIGYISQNPYLFAG-TVAD-- 428
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQ---FQKCVAYVRQDDILLPGlTVREtl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 429 ----NIALGE-TADEIKILEAA----NAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLALARAFLKRPGIILFDEPT 499
Cdd:cd03234 103 tytaILRLPRkSSDAIRKKRVEdvllRDLALTRIGGNLVKGI-----------SGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 500 TGLDLVTEQIVRRSIEELSREATLVTVahrlhTIKQA--------DAIWFMDDGKLLAQG 551
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVIL-----TIHQPrsdlfrlfDRILLLSSGEIVYSG 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
336-551 |
3.10e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 86.45 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDpLSgmIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEpleTYTDSSWYD-TIGY 414
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFD-LN--VADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ---SHTGLAPYQrPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAG-TVADNIALG-------ETADEIKILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLALARAF 486
Cdd:TIGR01277 75 LFQENNLFAHlTVRQNIGLGlhpglklNAEQQEKVVDAAQQVGIADYLDRLPEQL-----------SGGQRQRVALARCL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 487 LKRPGIILFDEPTTGLDLVTEQ----IVRRSIEElsREATLVTVAHRLH-TIKQADAIWFMDDGKLLAQG 551
Cdd:TIGR01277 144 VRPNPILLLDEPFSALDPLLREemlaLVKQLCSE--RQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVS 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
341-570 |
3.51e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.84 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 341 VSFAYEGG-----RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGepLETYTDSSWYD---TI 412
Cdd:PRK13633 10 VSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDirnKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNP--YLFAGTVADNIA-----LGETADEIK--ILEAANAAGLNDVIAQLPNgihtelgeggyGLSGGERQRLALA 483
Cdd:PRK13633 88 GMVFQNPdnQIVATIVEEDVAfgpenLGIPPEEIRerVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 484 RAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDEL----- 556
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIfkeve 236
|
250 260
....*....|....*....|.
gi 2048238220 557 ------LSVPQYADL-FTLQK 570
Cdd:PRK13633 237 mmkkigLDVPQVTELaYELKK 257
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
336-551 |
3.61e-19 |
|
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: 86.18 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYegGRFT-LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetytDSSWYDTIGY 414
Cdd:cd03269 1 LEVENVTKRF--GRVTaLDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAG-TVADN-IALGETADeIKILEAANAA-------GL----NDVIAQLPNGihtelgeggyglsggERQRLA 481
Cdd:cd03269 75 LPEERGLYPKmKVIDQlVYLAQLKG-LKKEEARRRIdewlerlELseyaNKRVEELSKG---------------NQQKVQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 482 LARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQG 551
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGkTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
73-558 |
4.37e-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: 91.93 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 73 FGY-MSGRIGASLsekAKRTLRLQLLDRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFsqywPQVIqtsiipLLILVV 151
Cdd:TIGR00957 1023 FGYsMAVSIGGIQ---ASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMI----PPVI------KMFMGS 1089
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 152 VFSQHWISGVIMMVT--APFIPIFFIIIGIATQK---KSEQQMEKMNQFS-----GKFLDVLQGLTTLKLYGRTER-EAQ 220
Cdd:TIGR00957 1090 LFNVIGALIVILLATpiAAVIIPPLGLLYFFVQRfyvASSRQLKRLESVSrspvySHFNETLLGVSVIRAFEEQERfIHQ 1169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 221 AIEKSSLDFRDATMVVLKTAFLSgLMLEFI----------------SMLSTGVVALEVALQMVVwenlTFFSGFLILVLA 284
Cdd:TIGR00957 1170 SDLKVDENQKAYYPSIVANRWLA-VRLECVgncivlfaalfavisrHSLSAGLVGLSVSYSLQV----TFYLNWLVRMSS 1244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 285 peyylaikDLggafhtgRGSMGAADRIFEALDAPDERlTWgdRMLTSRTPD-------LELDAVSFAY-EGGRFTLDPLS 356
Cdd:TIGR00957 1245 --------EM-------ETNIVAVERLKEYSETEKEA-PW--QIQETAPPSgwpprgrVEFRNYCLRYrEDLDLVLRHIN 1306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 357 GMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNI-ALGET 435
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQY 1386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 436 ADEiKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIE 515
Cdd:TIGR00957 1387 SDE-EVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR 1465
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2048238220 516 ELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:TIGR00957 1466 TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
365-557 |
5.10e-19 |
|
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: 86.44 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 365 VALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYT-DSSWYDTIGYISQNPYLFAG-TVADNIALgeTADEIKIL 442
Cdd:cd03218 29 VGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASIFRKlTVEENILA--VLEIRGLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 443 EAANAAGLNDVIAQLpnGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE-- 520
Cdd:cd03218 107 KKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRgi 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 2048238220 521 ATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELL 557
Cdd:cd03218 185 GVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
336-556 |
5.20e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.13 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAyEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYI 415
Cdd:PRK11831 8 VDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 S---QNPYLFAG-TVADNIA--------LGETADEIKILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLALA 483
Cdd:PRK11831 87 SmlfQSGALFTDmNVFDNVAyplrehtqLPAPLLHSTVMMKLEAVGLRGAAKLMPSEL-----------SGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 484 RAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRL-HTIKQADAIWFMDDGKLLAQGTHDEL 556
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlgVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
336-569 |
5.30e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.60 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSfAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGepletyTDSSWYDT---- 411
Cdd:PRK10851 3 IEIANIK-KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG------TDVSRLHArdrk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 IGYISQNPYLFAG-TVADNIALGET---------ADEIK-----ILEAANAAGL-NDVIAQLPNGihtelgeggyglsgg 475
Cdd:PRK10851 76 VGFVFQHYALFRHmTVFDNIAFGLTvlprrerpnAAAIKakvtqLLEMVQLAHLaDRYPAQLSGG--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 476 ERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAH-RLHTIKQADAIWFMDDGKLLAQGT 552
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
250
....*....|....*..
gi 2048238220 553 HDELLSVPqyADLFTLQ 569
Cdd:PRK10851 221 PDQVWREP--ATRFVLE 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
334-517 |
5.36e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.84 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 334 PDLELDAVSFAYEGGRFT---LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwyd 410
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 tiGYISQN----PYLfagTVADNIALG------ETADEIKILEAANAA-GLNDV----IAQLPNGIhtelgeggyglsgg 475
Cdd:COG4525 79 --GVVFQKdallPWL---NVLDNVAFGlrlrgvPKAERRARAEELLALvGLADFarrrIWQLSGGM-------------- 139
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2048238220 476 eRQRLALARAFLKRPGIILFDEPTTGLDLVTeqivRRSIEEL 517
Cdd:COG4525 140 -RQRVGIARALAADPRFLLMDEPFGALDALT----REQMQEL 176
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
336-546 |
5.97e-19 |
|
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: 83.65 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGepletytdsswYDTIGYI 415
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQnpylFAGtvadnialGETAdeikileaanaaglndviaqlpngihtelgeggyglsggerqRLALARAFLKRPGIILF 495
Cdd:cd03221 69 EQ----LSG--------GEKM------------------------------------------RLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 496 DEPTTGLDLVTEQIVRRSIEELSReaTLVTVAHRLHTIKQ-ADAIWFMDDGK 546
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYPG--TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
338-572 |
6.97e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.77 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 338 LDAVSFAYEGgRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQ 417
Cdd:PRK10575 14 LRNVSFRVPG-RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 418 N-PYLFAGTVADNIALGE-----------TADEIKILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLALARA 485
Cdd:PRK10575 93 QlPAAEGMTVRELVAIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSL-----------SGGERQRAWIAML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 486 FLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLvTVAHRLHTIKQA----DAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGL-TVIAVLHDINMAarycDYLVALRGGEMIAQGTPAELMRGET 240
|
250
....*....|.
gi 2048238220 562 YADLFTLQKGV 572
Cdd:PRK10575 241 LEQIYGIPMGI 251
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
347-556 |
8.22e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 85.50 E-value: 8.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 347 GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDG-----EPLETYTdsswydTIGYISQNPYL 421
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvrEPREVRR------RIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 422 FAG-TVADNIAL--------GETADEiKILEAANAAGLNDVIAQLpngihtelgegGYGLSGGERQRLALARAFLKRPGI 492
Cdd:cd03265 85 DDElTGWENLYIharlygvpGAERRE-RIDELLDFVGLLEAADRL-----------VKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 493 ILFDEPTTGLDLVTEQIVRRSIEELSREATlVTVAHRLHTIKQADA----IWFMDDGKLLAQGTHDEL 556
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFG-MTILLTTHYMEEAEQlcdrVAIIDHGRIIAEGTPEEL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
331-552 |
8.43e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.64 E-value: 8.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 331 SRTPDLELDAVSFAYEGGRFTLDPL---SGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSS 407
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLhnvSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 408 WYD----TIGYISQNPYLFAG-TVADNIAL-----GETADEI--KILEAANAAGL----NDVIAQLPNGihtelgeggyg 471
Cdd:PRK11629 81 KAElrnqKLGFIYQFHHLLPDfTALENVAMplligKKKPAEInsRALEMLAAVGLehraNHRPSELSGG----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 472 lsggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE---ATLVtVAHRLHTIKQADAIWFMDDGKLL 548
Cdd:PRK11629 150 ----ERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLqgtAFLV-VTHDLQLAKRMSRQLEMRDGRLT 224
|
....
gi 2048238220 549 AQGT 552
Cdd:PRK11629 225 AELS 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
329-573 |
1.13e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.19 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 329 LTSRTPDLELDAVSFAYegGRFTL-DPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSS 407
Cdd:PRK10253 1 MTESVARLRGEQLTLGY--GKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 408 WYDTIGYISQNPYLFAG-TVADNIALG-----------ETADEIKILEAANAAGLNDVIAQlpngihtelgeGGYGLSGG 475
Cdd:PRK10253 79 VARRIGLLAQNATTPGDiTVQELVARGryphqplftrwRKEDEEAVTKAMQATGITHLADQ-----------SVDTLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 476 ERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLH-TIKQADAIWFMDDGKLLAQGT 552
Cdd:PRK10253 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGA 227
|
250 260
....*....|....*....|.
gi 2048238220 553 HDELLSvpqyADLFTLQKGVR 573
Cdd:PRK10253 228 PKEIVT----AELIERIYGLR 244
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
336-558 |
1.42e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.55 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYI 415
Cdd:COG4559 2 LEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYL-FAGTVADNIALG-------ETADEIKILEAANAAGLNDVIA----QLPNGihtElgeggyglsggeRQRLALA 483
Cdd:COG4559 81 PQHSSLaFPFTVEEVVALGraphgssAAQDRQIVREALALVGLAHLAGrsyqTLSGG---E------------QQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 484 RAFL-------KRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE-ATLVTVAHRLH-TIKQADAIWFMDDGKLLAQGTHD 554
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRgGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPE 225
|
....
gi 2048238220 555 ELLS 558
Cdd:COG4559 226 EVLT 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
336-565 |
1.52e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGepLETYTDSSWYDT---I 412
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIrklV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYL-FAG-TVADNIALGE---TADEIKILEAANAAglndvIAQLpnGIHTELGEGGYGLSGGERQRLALARAFL 487
Cdd:PRK13644 80 GIVFQNPETqFVGrTVEEDLAFGPenlCLPPIEIRKRVDRA-----LAEI--GLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048238220 488 KRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVPQYADL 565
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-574 |
2.93e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 347 GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKP-----DSGRVLVDGEPLETYTDS-SWYDTIGYISQNPY 420
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVlEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 421 LFAGTVADNIALGETADEI---KILEAANAAGLNDViaQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDE 497
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKLvprKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 498 PTTGLDLVTEQIVRRSIEELSREATLVTVAHRL-HTIKQADAIWFMDDGKLLAQGTHDELLSVPQYADLFTLQKGVRG 574
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
336-558 |
3.31e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.28 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLEtYTDSSWYD---TI 412
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKlreSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNP--YLFAGTVADNIALGetADEIKILEAANAAGLNDVIAQlpNGIHTELGEGGYGLSGGERQRLALARAFLKRP 490
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSFG--AVNLKLPEDEVRKRVDNALKR--TGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2048238220 491 GIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHTIK-QADAIWFMDDGKLLAQGTHDELLS 558
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
336-527 |
4.34e-18 |
|
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: 83.23 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSS---WYDTI 412
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQ-NPYLFAGTVADNIAL-----GETADEI--KILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLALAR 484
Cdd:cd03292 81 GVVFQdFRLLPDRNVYENVAFalevtGVPPREIrkRVPAALELVGLSHKHRALPAEL-----------SGGEQQRVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2048238220 485 AFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVA 527
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
336-558 |
5.19e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.48 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEG--GRFTLDplsgmIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEpleTYTDSSwydtig 413
Cdd:PRK10771 2 LKLTDITWLYHHlpMRFDLT-----VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ---DHTTTP------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 414 yISQNPY--------LFAG-TVADNIALGE------TADEIKILEA-ANAAGLNDVIAQLPNGIhtelgeggyglSGGER 477
Cdd:PRK10771 68 -PSRRPVsmlfqennLFSHlTVAQNIGLGLnpglklNAAQREKLHAiARQMGIEDLLARLPGQL-----------SGGQR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 478 QRLALARAFLKRPGIILFDEPTTGLD--LVTE--QIVRRSIEElsREATLVTVAHRLH-TIKQADAIWFMDDGKLLAQGT 552
Cdd:PRK10771 136 QRVALARCLVREQPILLLDEPFSALDpaLRQEmlTLVSQVCQE--RQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGP 213
|
....*.
gi 2048238220 553 HDELLS 558
Cdd:PRK10771 214 TDELLS 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
336-561 |
7.16e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.02 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYI 415
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNP--YLFAGTVADNIA-----LGETADEIK--ILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLALARAF 486
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAfgpvnMGLDKDEVErrVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 487 LKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVA-HRLHTIKQ-ADAIWFMDDGKLLAQGThDELLSVPQ 561
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDED 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
352-551 |
8.50e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 82.77 E-value: 8.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGE-PletytdssWYDTIGYISQNPYLFA--GTVAD 428
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvP--------WKRRKKFLRRIGVVFGqkTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 429 NIALGET---ADEIKILEAANAAGLNDVIAQLPNgIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLV 505
Cdd:cd03267 109 DLPVIDSfylLAAIYDLPPARFKKRLDELSELLD-LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2048238220 506 TEQIVRRSIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQG 551
Cdd:cd03267 188 AQENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
338-503 |
8.54e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 82.02 E-value: 8.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 338 LDAVSFAYE-GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDsSWYDTIGYIS 416
Cdd:TIGR01189 1 LAARNLACSrGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 QNPYLFAG-TVADNI----ALGETADEiKILEAANAAGLNDV----IAQLPNGihtelgeggyglsggERQRLALARAFL 487
Cdd:TIGR01189 80 HLPGLKPElSALENLhfwaAIHGGAQR-TIEDALAAVGLTGFedlpAAQLSAG---------------QQRRLALARLWL 143
|
170
....*....|....*.
gi 2048238220 488 KRPGIILFDEPTTGLD 503
Cdd:TIGR01189 144 SRRPLWILDEPTTALD 159
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
336-558 |
8.71e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAY--EGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLEtyTDSSW--YDT 411
Cdd:PRK13650 5 IEVKNLTFKYkeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT--EENVWdiRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 IGYISQNP-YLFAG-TVADNIALG-ETA----DEIK--ILEAANAAGLNDVI----AQLPNGihtelgeggyglsggERQ 478
Cdd:PRK13650 83 IGMVFQNPdNQFVGaTVEDDVAFGlENKgiphEEMKerVNEALELVGMQDFKerepARLSGG---------------QKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 479 RLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDEL 556
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
..
gi 2048238220 557 LS 558
Cdd:PRK13650 228 FS 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
335-561 |
8.81e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.92 E-value: 8.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 335 DLELDAVSFAYEGG----RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYD 410
Cdd:PRK13634 2 DITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 TI----GYISQNP--YLFAGTVADNIALG-------ETADEIKILEAANAAGLN-DVIAQLP---NGihtelgeggygls 473
Cdd:PRK13634 82 PLrkkvGIVFQFPehQLFEETVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPeELLARSPfelSG------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 474 gGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQ 550
Cdd:PRK13634 149 -GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQ 227
|
250
....*....|.
gi 2048238220 551 GTHDELLSVPQ 561
Cdd:PRK13634 228 GTPREIFADPD 238
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-401 |
8.84e-18 |
|
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: 86.78 E-value: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 21 LVIAAVMIGLSILAQAYLIVdIVDQVFlkNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQLLDRY 100
Cdd:COG4615 15 LLLALLLGLLSGLANAGLIA-LINQAL--NATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 101 TSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYwPQVIQTSIIPLLILVVVFsqhWISGVIMMVTAPFIPIFFIIIGIA 180
Cdd:COG4615 92 LAAPLERLERIGAARLLAALTEDVRTISQAFVRL-PELLQSVALVLGCLAYLA---WLSPPLFLLTLVLLGLGVAGYRLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 181 TQK---KSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTERE--AQAIEKSSLDFRDATMVVLkTAFLSGLMLEFISMLst 255
Cdd:COG4615 168 VRRarrHLRRAREAEDRLFKHFRALLEGFKELKLNRRRRRAffDEDLQPTAERYRDLRIRAD-TIFALANNWGNLLFF-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 256 GVVALEV-ALQMVVWENLTFFSGFLILVLapeyYLA--IKDLGGAFHT---GRGSMGAADRIFEALDAPDERLTWGDRML 329
Cdd:COG4615 245 ALIGLILfLLPALGWADPAVLSGFVLVLL----FLRgpLSQLVGALPTlsrANVALRKIEELELALAAAEPAAADAAAPP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 330 TSRTPD-LELDAVSFAY----EGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLE 401
Cdd:COG4615 321 APADFQtLELRGVTYRYpgedGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT 397
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
336-558 |
9.43e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.28 E-value: 9.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYI 415
Cdd:PRK13548 3 LEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYL-FAGTVADNIALG-------ETADEIKILEAANAAGLNDV----IAQLPNGihtElgeggyglsggeRQRLALA 483
Cdd:PRK13548 82 PQHSSLsFPFTVEEVVAMGraphglsRAEDDALVAAALAQVDLAHLagrdYPQLSGG---E------------QQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 484 RAFL------KRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLH-TIKQADAIWFMDDGKLLAQGTHD 554
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPA 226
|
....
gi 2048238220 555 ELLS 558
Cdd:PRK13548 227 EVLT 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
359-558 |
1.28e-17 |
|
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: 83.37 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEpletytdsswydtIGYISQNPYLFAGTVADNIALGETADE 438
Cdd:cd03291 60 IEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENIIFGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 439 IKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTE-QIVRRSIEEL 517
Cdd:cd03291 127 YRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEkEIFESCVCKL 206
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2048238220 518 SREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:cd03291 207 MANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
355-560 |
1.68e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.62 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 355 LSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLV-DGEPLETYTDSSWYDTIGYISQNPYLFAGTVADNIALG 433
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 434 ----------------------------------------------------------ETADEIKILEAANAAGLNDVIA 455
Cdd:PTZ00265 484 lyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyQTIKDSEVVDVSKKVLIHDFVS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 456 QLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVT--VAHRLHTI 533
Cdd:PTZ00265 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITiiIAHRLSTI 643
|
250 260
....*....|....*....|....*..
gi 2048238220 534 KQADAIWFMDDGKLLAQGTHDELLSVP 560
Cdd:PTZ00265 644 RYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
337-566 |
2.36e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.05 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 337 ELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYIS 416
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 QNPYLFAG-TVADNIALG---------ETADEIKILEAANAAGLNDV----IAQLPNGihtelgeggyglsggERQRLAL 482
Cdd:COG4604 82 QENHINSRlTVRELVAFGrfpyskgrlTAEDREIIDEAIAYLDLEDLadryLDELSGG---------------QRQRAFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 483 ARAFLKRPGIILFDEPTTGLDL----VTEQIVRRSIEELSReaTLVTVahrLHTIKQA----DAIWFMDDGKLLAQGTHD 554
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGK--TVVIV---LHDINFAscyaDHIVAMKDGRVVAQGTPE 221
|
250
....*....|..
gi 2048238220 555 ELLSVPQYADLF 566
Cdd:COG4604 222 EIITPEVLSDIY 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
336-547 |
2.76e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.73 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVdGEPLEtytdsswydtIGYI 415
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAG--TVADNIAlgETADEIKILEAANAAG--------LNDVIAQLPNGihtElgeggyglsggeRQRLALARA 485
Cdd:COG0488 384 DQHQEELDPdkTVLDELR--DGAPGGTEQEVRGYLGrflfsgddAFKPVGVLSGG---E------------KARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 486 FLKRPGIILFDEPTTGLDLVTeqivRRSIEE-LSR-EATLVTVAH-R--LHTIkqADAIWFMDDGKL 547
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIET----LEALEEaLDDfPGTVLLVSHdRyfLDRV--ATRILEFEDGGV 507
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
333-560 |
2.89e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.73 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYEGgRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYtdSSWYDTI 412
Cdd:PRK11607 17 TPLLEIRNLTKSFDG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYLFAG-TVADNIALGETADEIKILEaanaagLNDVIAQLPNGIHTELGEGGY--GLSGGERQRLALARAFLKR 489
Cdd:PRK11607 94 NMMFQSYALFPHmTVEQNIAFGLKQDKLPKAE------IASRVNEMLGLVHMQEFAKRKphQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 490 PGIILFDEPTTGLD-LVTEQIVRRSIEELSR-EATLVTVAH-RLHTIKQADAIWFMDDGKLLAQGTHDELLSVP 560
Cdd:PRK11607 168 PKLLLLDEPMGALDkKLRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
336-558 |
4.66e-17 |
|
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: 80.80 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDT---- 411
Cdd:COG0410 4 LEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI---TGLPPHRIarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 IGYISQNPYLFAG-TVADNIALGETADEIKileAANAAGLNDVIAQLPN--------------GihtElgeggyglsgge 476
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENLLLGAYARRDR---AEVRADLERVYELFPRlkerrrqragtlsgG---E------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 477 RQRLALARAFLKRPGIILFDEPTTGLD-LVTEQIVRRsIEELSRE-ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTH 553
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGLApLIVEEIFEI-IRRLNREgVTILLVEQNARFALEiADRAYVLERGRIVLEGTA 220
|
....*
gi 2048238220 554 DELLS 558
Cdd:COG0410 221 AELLA 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
336-535 |
5.38e-17 |
|
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: 78.73 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVlvdgepletytDSSWYDTIGYI 415
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAGTVADNIA--------LGEtadeikileaanaaglndviaqlpngihtelgeggyglsggeRQRLALARAFL 487
Cdd:cd03223 70 PQRPYLPLGTLREQLIypwddvlsGGE------------------------------------------QQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2048238220 488 KRPGIILFDEPTTGLDLVTEQIVRRSIEELSreATLVTVAHRlHTIKQ 535
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR-PSLWK 152
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
352-560 |
9.72e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 79.75 E-value: 9.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGepLETYTDSSWYDTI----GYISQNPYLFAGTVA 427
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLIrqeaGMVFQQFYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 428 -DNIALG---------ETADEIKiLEAANAAGL----NDVIAQLPNGihtelgeggyglsggERQRLALARAFLKRPGII 493
Cdd:PRK09493 95 lENVMFGplrvrgaskEEAEKQA-RELLAKVGLaeraHHYPSELSGG---------------QQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048238220 494 LFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVP 560
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
351-557 |
1.65e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 83.46 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 351 TLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGepletytdsswydTIGYISQNPYLFAGTVADNI 430
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 431 ALGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDL-VTEQI 509
Cdd:TIGR00957 720 LFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHI 799
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2048238220 510 VRRSI--EELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELL 557
Cdd:TIGR00957 800 FEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
362-557 |
3.48e-16 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 77.97 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 362 GAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPletytDSSWYDTIGYISQN-------PYLFAGTV-------- 426
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQRhefawdfPISVAHTVmsgrtghi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 427 --------ADNIALGETADEIKILEAANAAglndvIAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEP 498
Cdd:TIGR03771 81 gwlrrpcvADFAAVRDALRRVGLTELADRP-----VGELSGG---------------QRQRVLVARALATRPSVLLLDEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2048238220 499 TTGLDLVTEQIVRRSIEELSREA-TLVTVAHRL-HTIKQADAIWFMdDGKLLAQGTHDELL 557
Cdd:TIGR03771 141 FTGLDMPTQELLTELFIELAGAGtAILMTTHDLaQAMATCDRVVLL-NGRVIADGTPQQLQ 200
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
330-567 |
4.32e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.99 E-value: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 330 TSRTPDLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGE----------P 399
Cdd:PRK09452 9 SSLSPLVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenrH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 400 LETytdsswydtigyISQNPYLFAG-TVADNIALG-----ETADEIK--ILEAANAAGLNDV----IAQLPNGihtelge 467
Cdd:PRK09452 88 VNT------------VFQSYALFPHmTVFENVAFGlrmqkTPAAEITprVMEALRMVQLEEFaqrkPHQLSGG------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 468 ggyglsggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAH-RLHTIKQADAIWFMDD 544
Cdd:PRK09452 149 --------QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlgITFVFVTHdQEEALTMSDRIVVMRD 220
|
250 260
....*....|....*....|...
gi 2048238220 545 GKLLAQGTHDELLSVPqyADLFT 567
Cdd:PRK09452 221 GRIEQDGTPREIYEEP--KNLFV 241
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-311 |
4.97e-16 |
|
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: 78.62 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 18 IVGLVIAAVMIGLSILAQAYLIVDIVDQVFLkNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQLL 97
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFV-EKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 98 DRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFIII 177
Cdd:cd18552 80 DKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 178 GIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFISMLSTGV 257
Cdd:cd18552 160 GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2048238220 258 VALeVALQMVVWENLT---FFS--GFLILVLAPeyylaIKDLGGAFHTGRGSMGAADRI 311
Cdd:cd18552 240 VLW-YGGYQVISGELTpgeFISfiTALLLLYQP-----IKRLSNVNANLQRGLAAAERI 292
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
336-561 |
5.74e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.77 E-value: 5.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVL---NVLSGLVkPD---SGRVLVDGEPLetytdsswY 409
Cdd:COG1117 12 IEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLI-PGarvEGEILLDGEDI--------Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 410 DT----------IGYISQNPYLFAGTVADNIALG---------ETADEI--KILEAA----------NAAGLNdviaqLP 458
Cdd:COG1117 82 DPdvdvvelrrrVGMVFQKPNPFPKSIYDNVAYGlrlhgikskSELDEIveESLRKAalwdevkdrlKKSALG-----LS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 459 NGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRLHtikQA-- 536
Cdd:COG1117 157 GG---------------QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQ---QAar 218
|
250 260
....*....|....*....|....*..
gi 2048238220 537 --DAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:COG1117 219 vsDYTAFFYLGELVEFGPTEQIFTNPK 245
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
330-565 |
1.08e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.98 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 330 TSRTPDLELDAvsfayeggRFTLDP------LSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDgeplety 403
Cdd:PTZ00243 656 SAKTPKMKTDD--------FFELEPkvllrdVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 404 tdsswyDTIGYISQNPYLFAGTVADNIALGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQRLALA 483
Cdd:PTZ00243 721 ------RSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLA 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 484 RAFLKRPGIILFDEPTTGLDL-VTEQIVRRSIEELSREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVPQY 562
Cdd:PTZ00243 795 RAVYANRDVYLLDDPLSALDAhVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTSLY 874
|
...
gi 2048238220 563 ADL 565
Cdd:PTZ00243 875 ATL 877
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
352-556 |
1.28e-15 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 77.82 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDG-----EPLE-------TYTDSSWYDTI-GYisQN 418
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvrEPRKvrrsigiVPQYASVDEDLtGR--EN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 419 PYLFAGT--VADNIALGETADEIKILEAANAAglNDVIAQLPNGIhtelgeggyglsggeRQRLALARAFLKRPGIILFD 496
Cdd:TIGR01188 87 LEMMGRLygLPKDEAEERAEELLELFELGEAA--DRPVGTYSGGM---------------RRRLDIAASLIHQPDVLFLD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 497 EPTTGLDLVTEQIVRRSIEELSRE--ATLVTvAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDEL 556
Cdd:TIGR01188 150 EPTTGLDPRTRRAIWDYIRALKEEgvTILLT-THYMEEADKlCDRIAIIDHGRIIAEGTPEEL 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
333-558 |
1.56e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYEGGR-FTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT 411
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 IGYISQNP-YLFAG-TVADNIALG----------------ETADEIKILEAANAAglndviaqlPNGIhtelgeggyglS 473
Cdd:PRK13648 85 IGIVFQNPdNQFVGsIVKYDVAFGlenhavpydemhrrvsEALKQVDMLERADYE---------PNAL-----------S 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 474 GGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEEL--SREATLVTVAHRLHTIKQADAIWFMDDGKLLAQG 551
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
....*..
gi 2048238220 552 THDELLS 558
Cdd:PRK13648 225 TPTEIFD 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
344-561 |
1.81e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.09 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 344 AYEGGRFTLDpLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGE-----PLETYTDSSwydtIGYISQN 418
Cdd:PRK10895 12 AYKGRRVVED-VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARARRG----IGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 419 PYLFAG-TVADNI-ALGETADEI----------KILEAANAAGLNDVIAQLPNGihtelgeggyglsgGERQRLALARAF 486
Cdd:PRK10895 87 ASIFRRlSVYDNLmAVLQIRDDLsaeqredranELMEEFHIEHLRDSMGQSLSG--------------GERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 487 LKRPGIILFDEPTTGLDLVTEQIVRRSIEEL--SREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLrdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
359-529 |
2.56e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.38 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVK--PDSGRVLVDGEPletytdsswydtigyISQNpylfaGTVADNIA-LGET 435
Cdd:COG2401 53 IEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ---------------FGRE-----ASLIDAIGrKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 436 ADEIKILeaaNAAGLNDVI------AQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQI 509
Cdd:COG2401 113 KDAVELL---NAVGLSDAVlwlrrfKELSTG---------------QKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180
....*....|....*....|..
gi 2048238220 510 VRRSIEELSREA--TLVTVAHR 529
Cdd:COG2401 175 VARNLQKLARRAgiTLVVATHH 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
338-503 |
2.75e-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: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 338 LDAVSFAYE-GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDsSWYDTIGYIS 416
Cdd:cd03231 1 LEADELTCErDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 QNPYLFAG-TVADNI----ALGETADEIKILEAANAAGLNDVI-AQLPNGihtelgeggyglsggERQRLALARAFLKRP 490
Cdd:cd03231 80 HAPGIKTTlSVLENLrfwhADHSDEQVEEALARVGLNGFEDRPvAQLSAG---------------QQRRVALARLLLSGR 144
|
170
....*....|...
gi 2048238220 491 GIILFDEPTTGLD 503
Cdd:cd03231 145 PLWILDEPTTALD 157
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
366-547 |
2.87e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 366 ALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLeTYTDSSwyDT----IGYISQNPYLFAG-TVADNIALG------- 433
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPR--DAialgIGMVHQHFMLVPNlTVAENIVLGleptkgg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 434 ----ETADEiKILEAANAAGL----NDVIAQLPNGIhtelgeggyglsggeRQRLALARAFLKRPGIILFDEPTTGLdlv 505
Cdd:COG3845 112 rldrKAARA-RIRELSERYGLdvdpDAKVEDLSVGE---------------QQRVEILKALYRGARILILDEPTAVL--- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2048238220 506 TEQIVR---RSIEELSRE-ATLVTVAHRLHTIKQ-ADAIWFMDDGKL 547
Cdd:COG3845 173 TPQEADelfEILRRLAAEgKSIIFITHKLREVMAiADRVTVLRRGKV 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
361-563 |
2.99e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.89 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 361 TGAHVALVGASGSGKT----TVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwyDTIGYISQNP---YLFAGTVADN---- 429
Cdd:PRK10418 28 RGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRG--RKIATIMQNPrsaFNPLHTMHTHaret 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 430 -IALGETADEIKILEAANAAGLNDVIA-------QLPNGIhtelgeggyglsggeRQRLALARAFLKRPGIILFDEPTTG 501
Cdd:PRK10418 106 cLALGKPADDATLTAALEAVGLENAARvlklypfEMSGGM---------------LQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048238220 502 LDLVTEQIVRRSIEELSREATL--VTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVPQYA 563
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
340-566 |
3.17e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 340 AVSFayeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIGYISQNP 419
Cdd:PRK09536 10 SVEF---GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 420 YL-FAGTVADNIALGET-----------ADEIKILEAANAAGLNDVIAQ----LPNGihtelgeggyglsggERQRLALA 483
Cdd:PRK09536 87 SLsFEFDVRQVVEMGRTphrsrfdtwteTDRAAVERAMERTGVAQFADRpvtsLSGG---------------ERQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 484 RAFLKRPGIILFDEPTTGLDlvteqiVRRSIEELSREATLV----TVAHRLHTIKQA----DAIWFMDDGKLLAQGTHDE 555
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLD------INHQVRTLELVRRLVddgkTAVAAIHDLDLAarycDELVLLADGRVRAAGPPAD 225
|
250
....*....|.
gi 2048238220 556 LLSVPQYADLF 566
Cdd:PRK09536 226 VLTADTLRAAF 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
366-556 |
6.66e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.37 E-value: 6.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 366 ALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLEtytdsswYDT--------IGYISQNPYLFAG-TVADNIALGETA 436
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-------FRSprdaqaagIAIIHQELNLVPNlSVAENIFLGREP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 437 ------DEIKILEAANAA----GLN-DV---IAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGL 502
Cdd:COG1129 107 rrggliDWRAMRRRARELlarlGLDiDPdtpVGDLSVA---------------QQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 503 DlVTE-QIVRRSIEELSRE-ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQG-----THDEL 556
Cdd:COG1129 172 T-EREvERLFRIIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDEL 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
365-561 |
9.86e-15 |
|
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: 75.47 E-value: 9.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 365 VALVGASGSGKTTVLNVLSGLVKP---DSGRVLVDGEPLETYTDSSWYD----TIGYISQNPY-----LFagTVADNIA- 431
Cdd:COG0444 34 LGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDPMtslnpVM--TVGDQIAe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 432 -----LGETADEI--KILEAANAAGLND---VIAQLPN----GIhtelgeggyglsggeRQRLALARAFLKRPGIILFDE 497
Cdd:COG0444 112 plrihGGLSKAEAreRAIELLERVGLPDperRLDRYPHelsgGM---------------RQRVMIARALALEPKLLIADE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2048238220 498 PTTGLDlVTeqiVRRSI----EELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:COG0444 177 PTTALD-VT---IQAQIlnllKDLQRElgLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
336-561 |
1.01e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.74 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYE--GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIG 413
Cdd:PRK13642 5 LEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 414 YISQNP--YLFAGTVADNIALGETADEI-------KILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLALAR 484
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIpreemikRVDEALLAVNMLDFKTREPARL-----------SGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048238220 485 AFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
342-562 |
1.21e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.44 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 342 SFAYEGGRF------TLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLeTYTDSSWYDT-IGY 414
Cdd:PRK15112 13 TFRYRTGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSQrIRM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQ------NPYLFAGTVAD-----NIALGETADEIKILEAANAAGL-NDVIAQLPNGIHTelgeggyglsgGERQRLAL 482
Cdd:PRK15112 92 IFQdpstslNPRQRISQILDfplrlNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAP-----------GQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 483 ARAFLKRPGIILFDEPTTGLDL-VTEQIVRRSIE-ELSREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSV 559
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMsMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLAS 240
|
...
gi 2048238220 560 PQY 562
Cdd:PRK15112 241 PLH 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
336-527 |
1.50e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSS---WYDTI 412
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYLFAG-TVADNIAL-----GETADEIK--ILEAANAAGLNDVIAQLPngihtelgeggYGLSGGERQRLALAR 484
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIpliiaGASGDDIRrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2048238220 485 AFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVA 527
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMA 193
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
365-561 |
1.58e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.14 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 365 VALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDT----IGYISQNPYLFAG-TVADNIA-----LGE 434
Cdd:COG1137 32 VGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI---THLPMHKRarlgIGYLPQEASIFRKlTVEDNILavlelRKL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 435 TADEIK-----ILEAANAAGLNDVIA-QLPNGihtElgeggyglsggeRQRLALARAFLKRPGIILFDEPTTGLDLVTEQ 508
Cdd:COG1137 109 SKKEREerleeLLEEFGITHLRKSKAySLSGG---E------------RRRVEIARALATNPKFILLDEPFAGVDPIAVA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 509 IVRRSIEELsRE---ATLVTvAHRLH-TIKQADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:COG1137 174 DIQKIIRHL-KErgiGVLIT-DHNVReTLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
344-516 |
3.13e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.83 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 344 AYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPletYTDSSWYDTIGYISQ----NP 419
Cdd:PRK13539 10 CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLGHrnamKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 420 YLfagTVADNIA-----LGetADEIKILEAANAAGLNDvIAQLPNGihtelgeggyGLSGGERQRLALARAFL-KRPgII 493
Cdd:PRK13539 87 AL---TVAENLEfwaafLG--GEELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARLLVsNRP-IW 149
|
170 180
....*....|....*....|...
gi 2048238220 494 LFDEPTTGLDLVTEQIVRRSIEE 516
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRA 172
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
336-514 |
3.42e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 71.74 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPD---SGRVLVDGEPLETYtdsswyDT- 411
Cdd:COG4136 2 LSLENLTITL-GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL------PAe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 ---IGYISQNPYLFAG-TVADNIALGeTADEIK-------ILEAANAAGLNDV----IAQLPNGihtelgeggyglsggE 476
Cdd:COG4136 75 qrrIGILFQDDLLFPHlSVGENLAFA-LPPTIGraqrrarVEQALEEAGLAGFadrdPATLSGG---------------Q 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2048238220 477 RQRLALARAFLKRPGIILFDEPTTGLD---------LVTEQIVRRSI 514
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEPFSKLDaalraqfreFVFEQIRQRGI 185
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
336-556 |
4.08e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 73.22 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYegGRFT-LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLeTYTDsswYDTIGY 414
Cdd:COG4152 2 LELKGLTKRF--GDKTaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPED---RRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAG-TVADNIA-LGE----TADEIKI-----LEAANAAG-LNDVIAQLPNGihtelgeggyglsggERQRLAL 482
Cdd:COG4152 76 LPEERGLYPKmKVGEQLVyLARlkglSKAEAKRradewLERLGLGDrANKKVEELSKG---------------NQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 483 ARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE-ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDEL 556
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEI 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
366-551 |
4.17e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.76 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 366 ALVGASGSGKTTVLNVLSGLVKPDSG------RVLVDGE-----PLETytdsswyDTIGYISQNPYLFAG-TVADNIALG 433
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDAEkgiclPPEK-------RRIGYVFQDARLFPHyKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 434 etadeikiLEAANAAGLNDVIAQLpnGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRS 513
Cdd:PRK11144 101 --------MAKSMVAQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2048238220 514 IEELSREATL--VTVAHRLHTIKQ-ADAIWFMDDGKLLAQG 551
Cdd:PRK11144 171 LERLAREINIpiLYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
338-545 |
5.95e-14 |
|
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: 71.31 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 338 LDAVSFAYEGGRFtldplsgmiptgahVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDgepletyTDSSWYD------- 410
Cdd:COG4778 27 LDGVSFSVAAGEC--------------VALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-------HDGGWVDlaqaspr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 --------TIGYISQ---------------NPyLFAGTVADNIALGETADeikILEAANaagLNDVIAQLP-----NGih 462
Cdd:COG4778 86 eilalrrrTIGYVSQflrviprvsaldvvaEP-LLERGVDREEARARARE---LLARLN---LPERLWDLPpatfsGG-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 463 tElgeggyglsggeRQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE-ATLVTVAHRLHTIKQ-ADAIW 540
Cdd:COG4778 157 -E------------QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFHDEEVREAvADRVV 223
|
....*
gi 2048238220 541 FMDDG 545
Cdd:COG4778 224 DVTPF 228
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
365-561 |
9.09e-14 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 71.37 E-value: 9.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 365 VALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSS-------------WYDTIGYISQNPYLFAG-TVADNI 430
Cdd:COG4598 37 ISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvpadrrqlqrIRTRLGMVFQSFNLWSHmTVLENV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 431 ------ALGETADEIkiLEAANA----AGLNDVI----AQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFD 496
Cdd:COG4598 117 ieapvhVLGRPKAEA--IERAEAllakVGLADKRdaypAHLSGG---------------QQQRAAIARALAMEPEVMLFD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 497 EPTTGLD--LVTEqiVRRSIEELSREA-TLVTVAHRL--------HTIkqadaiwFMDDGKLLAQGTHDELLSVPQ 561
Cdd:COG4598 180 EPTSALDpeLVGE--VLKVMRDLAEEGrTMLVVTHEMgfardvssHVV-------FLHQGRIEEQGPPAEVFGNPK 246
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
333-558 |
9.51e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 9.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYEGGRfTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLE-TYTDSSWYDT 411
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 IGYISQN----PYLfagTVADNIALGETADEIKILeaaNAAGLN-DVIAQLPN-GIHTELGEGGYGLSGGERQRLALARA 485
Cdd:PRK11288 81 VAIIYQElhlvPEM---TVAENLYLGQLPHKGGIV---NRRLLNyEAREQLEHlGVDIDPDTPLKYLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 486 FLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVT-VAHRLHTIKQ-ADAIWFMDDGKL------LAQGTHDELL 557
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDGRYvatfddMAQVDRDQLV 234
|
.
gi 2048238220 558 S 558
Cdd:PRK11288 235 Q 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
336-557 |
1.11e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.56 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwYDTIGYI 415
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYL-FAGTVADNIAL-----GETADEIK-----ILEAANAAGLNDV-IAQLPNGIhtelgeggyglsggeRQRLALA 483
Cdd:PRK13536 120 PQFDNLdLEFTVRENLLVfgryfGMSTREIEavipsLLEFARLESKADArVSDLSGGM---------------KRRLTLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 484 RAFLKRPGIILFDEPTTGLD-----LVTEQIvrRSIeeLSREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELL 557
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDpharhLIWERL--RSL--LARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
326-556 |
1.33e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 326 DRMLTSRTPDLELDAVSFAYEGGR------FTLdpLSGMIptgaHvALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEP 399
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQYSGVEvlkgidFTL--HAGEV----H-ALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 400 LETYTDSSWYDT-IGYISQNPYLFAG-TVADNIALGETAdeikilEAANAAGLNDVIAQLpnGIHTELGEGGYGLSGGER 477
Cdd:PRK15439 75 CARLTPAKAHQLgIYLVPQEPLLFPNlSVKENILFGLPK------RQASMQKMKQLLAAL--GCQLDLDSSAGSLEVADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 478 QRLALARAFLKRPGIILFDEPTTGLDLV-TEQIVRRSIEELSREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDE 555
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTAD 226
|
.
gi 2048238220 556 L 556
Cdd:PRK15439 227 L 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
350-563 |
1.36e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.11 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 350 FTLDPlsgmiptGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLV---DGEPLETYTDSS----------WydtiGYIS 416
Cdd:PRK11701 27 FDLYP-------GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEaerrrllrteW----GFVH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 QNPY------LFAGTvadNI-----ALG--------ETA----DEIKIleaaNAAGLNDVIAQLPNGIhtelgeggygls 473
Cdd:PRK11701 96 QHPRdglrmqVSAGG---NIgerlmAVGarhygdirATAgdwlERVEI----DAARIDDLPTTFSGGM------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 474 ggeRQRLALARAFLKRPGIILFDEPTTGLDlVTEQ-----IVRRSIEELSREATLVT----VAHRLhtikqADAIWFMDD 544
Cdd:PRK11701 157 ---QQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQarlldLLRGLVRELGLAVVIVThdlaVARLL-----AHRLLVMKQ 227
|
250
....*....|....*....
gi 2048238220 545 GKLLAQGTHDELLSVPQYA 563
Cdd:PRK11701 228 GRVVESGLTDQVLDDPQHP 246
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
348-552 |
1.45e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 74.28 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 348 GRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwYDTIGYISQNPYLFAG-TV 426
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV-RQSLGMCPQHNILFHHlTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 427 ADNIAL-----GETADEIKI-LEAAnaagLNDviaqlpNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTT 500
Cdd:TIGR01257 1021 AEHILFyaqlkGRSWEEAQLeMEAM----LED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 501 GLDLVTeqivRRSIEEL-----SREATLVTVAHRLHTIKQADAIWFMDDGKLLAQGT 552
Cdd:TIGR01257 1091 GVDPYS----RRSIWDLllkyrSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
349-548 |
1.68e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.99 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 349 RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKP---DSGRVLVDGEPLetytDSSWYDTIGYISQNPyLFAGT 425
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPL----DSSFQRSIGYVQQQD-LHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 426 VADNIALGETA-----------------DE-IKILEAANAAglnDVIAQLPN-GIHTElgeggyglsggERQRLALARAF 486
Cdd:TIGR00956 851 STVRESLRFSAylrqpksvsksekmeyvEEvIKLLEMESYA---DAVVGVPGeGLNVE-----------QRKRLTIGVEL 916
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 487 LKRPGIILF-DEPTTGLDLVTEQIVRRSIEELSREATLVtvahrLHTIKQADAIWFMDDGKLL 548
Cdd:TIGR00956 917 VAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAI-----LCTIHQPSAILFEEFDRLL 974
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
359-572 |
1.86e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.37 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT----IGYISQNPYLFAG-TVADNIALG 433
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHmTVLDNTAFG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 434 ETADEI-------KILEAANAAGLNDVIAQLPNGIhtelgeggyglSGGERQRLALARAFLKRPGIILFDEPTTGLDLVT 506
Cdd:PRK10070 131 MELAGInaeerreKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048238220 507 EQIVRRSIEELS--REATLVTVAHRL-HTIKQADAIWFMDDGKLLAQGTHDELLSVPQYADLFTLQKGV 572
Cdd:PRK10070 200 RTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-560 |
2.01e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.45 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 334 PDLELDAVSFAYEGGRFtLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDsGRVLVDGEpLETYTDSSW----- 408
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGR-VEFFNQNIYerrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 409 ----YDTIGYISQNPYLFAGTVADNIALGetadeIKILEAANAAGLNDVI------AQLPNGIHTELGEGGYGLSGGERQ 478
Cdd:PRK14258 83 lnrlRRQVSMVHPKPNLFPMSVYDNVAYG-----VKIVGWRPKLEIDDIVesalkdADLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 479 RLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIE--ELSREATLVTVAHRLHTIKQ-ADAIWFMDD-----GKLLAQ 550
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEF 237
|
250
....*....|
gi 2048238220 551 GTHDELLSVP 560
Cdd:PRK14258 238 GLTKKIFNSP 247
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
352-555 |
2.02e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.11 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGE---PLETytdsswydTIGYisqNPYLfagTVAD 428
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsaLLEL--------GAGF---HPEL---TGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 429 NI-----ALGETADEI--KILEAANAAGLNDVIAQ----LPNGIhtelgeggyglsggeRQRLALARAFLKRPGIILFDE 497
Cdd:COG1134 108 NIylngrLLGLSRKEIdeKFDEIVEFAELGDFIDQpvktYSSGM---------------RARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 498 PT-TGlDLVTEQIVRRSIEELSREA-TLVTVAHRLHTIKQ-AD-AIWfMDDGKLLAQGTHDE 555
Cdd:COG1134 173 VLaVG-DAAFQKKCLARIRELRESGrTVIFVSHSMGAVRRlCDrAIW-LEKGRLVMDGDPEE 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
365-520 |
2.19e-13 |
|
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: 68.61 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 365 VALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT-IGYISQNPY---LFAG-TVADNIALGEtadei 439
Cdd:cd03215 29 VGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVLDlSVAENIALSS----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 440 kILEAANAaglndviaqlpngihtelgeggyglsggerQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSR 519
Cdd:cd03215 104 -LLSGGNQ------------------------------QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD 152
|
.
gi 2048238220 520 E 520
Cdd:cd03215 153 A 153
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-562 |
3.54e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.56 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVK--PD---SGRVLVDGEPLETYTDSSWYDTIGYISQNPYLFAG-TVADNIAL 432
Cdd:PRK14247 26 IPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNlSIFENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 433 GETADEI----KILEAANAAGLNDviAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQ 508
Cdd:PRK14247 106 GLKLNRLvkskKELQERVRWALEK--AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2048238220 509 IVRRSIEELSREATLVTVAH-RLHTIKQADAIWFMDDGKLLAQGTHDELLSVPQY 562
Cdd:PRK14247 184 KIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
362-562 |
4.73e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.51 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 362 GAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT---IGYISQNPylFAG-----TVADNIA-- 431
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDP--LASlnprmTIGEIIAep 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 432 ---------LGETADEIKILEAAnaAGLndviaqLPNGIHtelgeggyglsggeR----------QRLALARAFLKRPGI 492
Cdd:PRK15079 125 lrtyhpklsRQEVKDRVKAMMLK--VGL------LPNLIN--------------RyphefsggqcQRIGIARALILEPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 493 ILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVPQY 562
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLH 255
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
333-557 |
5.02e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.22 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwYDTI 412
Cdd:PRK13537 5 VAPIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYL---FagTVADNIAL-----GETADEIK-----ILEAANAAGLNDV-IAQLPNGIhtelgeggyglsggeRQ 478
Cdd:PRK13537 83 GVVPQFDNLdpdF--TVRENLLVfgryfGLSAAAARalvppLLEFAKLENKADAkVGELSGGM---------------KR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 479 RLALARAFLKRPGIILFDEPTTGLD-----LVTEQIvrRSIeeLSREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGT 552
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDpqarhLMWERL--RSL--LARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGA 221
|
....*
gi 2048238220 553 HDELL 557
Cdd:PRK13537 222 PHALI 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
336-561 |
5.94e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGE------PLETYTDSSWY 409
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 410 DTIGYISQN----PYLfagTVADNIalgeTADEIKIL----EAANAAGlNDVIAQLpnGIHTELGEGGYGLSGGERQRLA 481
Cdd:COG4161 82 QKVGMVFQQynlwPHL---TVMENL----IEAPCKVLglskEQAREKA-MKLLARL--RLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 482 LARAFLKRPGIILFDEPTTGLD-LVTEQIVrRSIEELSR-EATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHdELLS 558
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDpEITAQVV-EIIRELSQtGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA-SHFT 229
|
...
gi 2048238220 559 VPQ 561
Cdd:COG4161 230 QPQ 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
331-563 |
8.22e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 331 SRTPDLELDAVSFAYEGG---RFTLDPLSGMIPTGAHVALVGASGSGKT-TVLNVLSGLVKPD----SGRVLVDGEPLET 402
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 403 YTDSSWY----DTIGYISQNP-------YLFAGTVADNIAL-----GETA--------DEIKILEAANAagLNDVIAQLP 458
Cdd:PRK15134 81 ASEQTLRgvrgNKIAMIFQEPmvslnplHTLEKQLYEVLSLhrgmrREAArgeilnclDRVGIRQAAKR--LTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 459 NGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLDL-VTEQIVRRsIEELSRE--ATLVTVAHRLHTIKQ 535
Cdd:PRK15134 159 GG---------------ERQRVMIAMALLTRPELLIADEPTTALDVsVQAQILQL-LRELQQElnMGLLFITHNLSIVRK 222
|
250 260
....*....|....*....|....*....
gi 2048238220 536 -ADAIWFMDDGKLLAQGTHDELLSVPQYA 563
Cdd:PRK15134 223 lADRVAVMQNGRCVEQNRAATLFSAPTHP 251
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
367-558 |
9.38e-13 |
|
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: 70.60 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 367 LVGASGSGKTTVLNVLSGLVKPDSGRVLVD-GEPLETYTDSSWYDT------IGYISQNPYLFA-GTVADNI--ALG-ET 435
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDGRgrakryIGILHQEYDLYPhRTVLDNLteAIGlEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 436 ADEIKILEAA---NAAGLNDVIAQ--LPNGIHTelgeggygLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIV 510
Cdd:TIGR03269 395 PDELARMKAVitlKMVGFDEEKAEeiLDKYPDE--------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDV 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 511 RRSI----EELsrEATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLS 558
Cdd:TIGR03269 467 THSIlkarEEM--EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
359-554 |
9.40e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEP--LETYTDSSwydTIGYISQN-----------PYLfagT 425
Cdd:PRK11124 25 CPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDK---AIRELRRNvgmvfqqynlwPHL---T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 426 VADNI------ALGETADE-----IKILEAANAAGLNDVIA-QLPNGihtelgeggyglsggERQRLALARAFLKRPGII 493
Cdd:PRK11124 99 VQQNLieapcrVLGLSKDQalaraEKLLERLRLKPYADRFPlHLSGG---------------QQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 494 LFDEPTTGLD-LVTEQIVrRSIEELSREA-TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHD 554
Cdd:PRK11124 164 LFDEPTAALDpEITAQIV-SIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
333-549 |
1.14e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.52 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYEGGRFTLDPLSGM---IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSW- 408
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVEVLKGIsldIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 409 ---YDTIGYISQNPYLFAG-TVADNI---ALGETADEIKILEAANA----AGLNDVI----AQLPNGihtelgeggygls 473
Cdd:PRK10535 82 qlrREHFGFIFQRYHLLSHlTAAQNVevpAVYAGLERKQRLLRAQEllqrLGLEDRVeyqpSQLSGG------------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 474 ggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEEL-SREATLVTVAHRLHTIKQADAIWFMDDGKLLA 549
Cdd:PRK10535 149 --QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
336-552 |
1.20e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 68.62 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGR-FTLDPLSGM---IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGepLETYTDSSWYD- 410
Cdd:PRK13649 3 INLQNVSYTYQAGTpFEGRALFDVnltIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDD--TLITSTSKNKDi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 -----TIGYISQNP--YLFAGTVADNIALGETADEIKILEAANAA--GLNDViaqlpnGIHTELGEGGYGLSGGER-QRL 480
Cdd:PRK13649 81 kqirkKVGLVFQFPesQLFEETVLKDVAFGPQNFGVSQEEAEALAreKLALV------GISESLFEKNPFELSGGQmRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 481 ALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGT 552
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGmTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
367-570 |
1.52e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.72 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 367 LVGASGSGKTTVLNVLSGLVKPDSGRVLV---------DGEPLETYTDSS-------WYDTIGYISQNP--YLFAGTVAD 428
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNPYSKkiknfkeLRRRVSMVFQFPeyQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 429 NIALGETADEIKILEAANAA-------GLND-VIAQLPNGIhtelgeggyglSGGERQRLALARAFLKRPGIILFDEPTT 500
Cdd:PRK13631 137 DIMFGPVALGVKKSEAKKLAkfylnkmGLDDsYLERSPFGL-----------SGGQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 501 GLDLVTEQIVRRSIEELSREA-TLVTVAHRL-HTIKQADAIWFMDDGKLLAQGTHDELLSVPQYADLFTLQK 570
Cdd:PRK13631 206 GLDPKGEHEMMQLILDAKANNkTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIINSTSIQV 277
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-258 |
1.55e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 68.33 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 22 VIAAVMIGLSILAQAYLIVDIVDQVFLKNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQLLDRYT 101
Cdd:cd18778 5 LLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 102 SNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFIIIGIAT 181
Cdd:cd18778 85 RLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKV 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 182 QKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFISMLSTGVV 258
Cdd:cd18778 165 RPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLV 241
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
352-528 |
1.56e-12 |
|
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: 67.49 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetytDSSWYDTIgYISQNPYLFAG-TVADNI 430
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRM-VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 431 ALG---------ETADEIKILEAANAAGLNDV----IAQLPNGIhtelgeggyglsggeRQRLALARAFLKRPGIILFDE 497
Cdd:TIGR01184 76 ALAvdrvlpdlsKSERRAIVEEHIALVGLTEAadkrPGQLSGGM---------------KQRVAIARALSIRPKVLLLDE 140
|
170 180 190
....*....|....*....|....*....|...
gi 2048238220 498 PTTGLDLVTEQIVRRSIEELSREA--TLVTVAH 528
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEEHrvTVLMVTH 173
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
369-556 |
1.96e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 369 GASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetytDSSWYDT---IGYISQNPYLFAG-TVADNIAL-----GETADEI 439
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DAGDIATrrrVGYMSQAFSLYGElTVRQNLELharlfHLPAAEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 440 K--ILEAANAAGLNDVIAQLPN----GIhtelgeggyglsggeRQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRS 513
Cdd:NF033858 375 AarVAEMLERFDLADVADALPDslplGI---------------RQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2048238220 514 IEELSREATlVTVAHRLHTIKQA---DAIWFMDDGKLLAQGTHDEL 556
Cdd:NF033858 440 LIELSREDG-VTIFISTHFMNEAercDRISLMHAGRVLASDTPAAL 484
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
352-545 |
2.37e-12 |
|
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: 65.73 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLS-----GLVKpdsGRVLVDGEPLetytDSSWYDTIGYISQNPYLFAG-T 425
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVIT---GEILINGRPL----DKNFQRSTGYVEQQDVHSPNlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 426 VADNIALgetadeikileAANAAGLNdvIAQlpngihtelgeggyglsggeRQRLALARAFLKRPGIILFDEPTTGLDLV 505
Cdd:cd03232 96 VREALRF-----------SALLRGLS--VEQ--------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2048238220 506 TEQIVRRSIEELSRE--ATLVTVAHRLHTI-KQADAIWFMDDG 545
Cdd:cd03232 143 AAYNIVRFLKKLADSgqAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
336-562 |
2.89e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 67.55 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGG----RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT 411
Cdd:PRK13641 3 IKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 I----GYISQNP--YLFAGTVADNIALG-------ETADEIKILEAANAAGLN-DVIAQLPngihtelgeggYGLSGGER 477
Cdd:PRK13641 83 LrkkvSLVFQFPeaQLFENTVLKDVEFGpknfgfsEDEAKEKALKWLKKVGLSeDLISKSP-----------FELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 478 QRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDE 555
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGhTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKE 231
|
....*..
gi 2048238220 556 LLSVPQY 562
Cdd:PRK13641 232 IFSDKEW 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
336-558 |
3.07e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGG----RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWY-- 409
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 410 --DTIGYISQNP--YLFAGTVADNIALGETADEIKILEAANAAglNDVIAQLpnGIHTELGEGGYGLSGGERQR-LALAR 484
Cdd:PRK13646 83 vrKRIGMVFQFPesQLFEDTVEREIIFGPKNFKMNLDEVKNYA--HRLLMDL--GFSRDVMSQSPFQMSGGQMRkIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 485 AFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTI-KQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
336-547 |
3.81e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.85 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDTIGYI 415
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 S---QNPYLF------AGTVADNiALGETAdeIKILEAANAAGLND---VIAQLPNGihtelgeggyglsggERQRLALA 483
Cdd:PRK10522 400 SavfTDFHLFdqllgpEGKPANP-ALVEKW--LERLKMAHKLELEDgriSNLKLSKG---------------QKKRLALL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 484 RAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHTIKQADAIWFMDDGKL 547
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMgkTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
350-558 |
4.14e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 350 FTLDPLSGmiptgahvaLVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLEtYTDS---SWYDTIGYISQNP--YLFAG 424
Cdd:PRK13638 24 FSLSPVTG---------LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRgllALRQQVATVFQDPeqQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 425 TVADNIA-----LGETADEI-----KILEAANAAGL-NDVIAQLPNGihtelgeggyglsggERQRLALARAFLKRPGII 493
Cdd:PRK13638 94 DIDSDIAfslrnLGVPEAEItrrvdEALTLVDAQHFrHQPIQCLSHG---------------QKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 494 LFDEPTTGLDLVTEQ----IVRRSIEELSReatLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLS 558
Cdd:PRK13638 159 LLDEPTAGLDPAGRTqmiaIIRRIVAQGNH---VIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
365-547 |
4.19e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.96 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 365 VALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWY----DTIGYISQNPYLFAGTVA-DNIAL-----GE 434
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklraKHVGFVFQSFMLIPTLNAlENVELpallrGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 435 TADE-----IKILEAAN-AAGLNDVIAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQ 508
Cdd:PRK10584 119 SSRQsrngaKALLEQLGlGKRLDHLPAQLSGG---------------EQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2048238220 509 IVRRSIEELSRE--ATLVTVAHRLHTIKQADAIWFMDDGKL 547
Cdd:PRK10584 184 KIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
352-546 |
5.09e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.26 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDTIGYIS---QNPylFAGT--- 425
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV---TKLPEYKRAKYIGrvfQDP--MMGTaps 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 426 --VADNIAL------------GETADEIKILEAANAA---GL----NDVIAQLPNGihtelgeggyglsggERQRLALAR 484
Cdd:COG1101 97 mtIEENLALayrrgkrrglrrGLTKKRRELFRELLATlglGLenrlDTKVGLLSGG---------------QRQALSLLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048238220 485 AFLKRPGIILFDEPTTGLD-----LV---TEQIVRRsiEELSreaTL-VTvahrlHTIKQA----DAIWFMDDGK 546
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDpktaaLVlelTEKIVEE--NNLT---TLmVT-----HNMEQAldygNRLIMMHEGR 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
362-571 |
6.05e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.15 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 362 GAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDS-------------SWYDTIGYISQNPYLFAG-TVA 427
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrLLRTRLTMVFQHFNLWSHmTVL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 428 DNI------ALGETADEIK--ILEAANAAGLNDViAQLPNGIHtelgeggygLSGGERQRLALARAFLKRPGIILFDEPT 499
Cdd:PRK10619 111 ENVmeapiqVLGLSKQEARerAVKYLAKVGIDER-AQGKYPVH---------LSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 500 TGLD--LVTEqiVRRSIEELSREA-TLVTVAHRLHTIKQADA-IWFMDDGKLLAQGTHDELLSVPQYADLFTLQKG 571
Cdd:PRK10619 181 SALDpeLVGE--VLRIMQQLAEEGkTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
365-530 |
6.26e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 365 VALVGASGSGKTTVLNVLSGLVKPDSGRVlvDGEP-----LETYTDSSWYD--------------TIGYISQNPYLFAGT 425
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDY--EEEPswdevLKRFRGTELQNyfkklyngeikvvhKPQYVDLIPKVFKGK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 426 VADniaLGETADEIKIL-EAANAAGLNDV----IAQLPNGihtELgeggyglsggerQRLALARAFLKRPGIILFDEPTT 500
Cdd:PRK13409 180 VRE---LLKKVDERGKLdEVVERLGLENIldrdISELSGG---EL------------QRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|.
gi 2048238220 501 GLDlVTEQI-VRRSIEELSREATLVTVAHRL 530
Cdd:PRK13409 242 YLD-IRQRLnVARLIRELAEGKYVLVVEHDL 271
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
356-565 |
6.49e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 356 SGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPD---SGRVLVDGEPLetytDSSWYDTI-GYISQNPyLFAGTVadnia 431
Cdd:TIGR00955 45 SGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI----DAKEMRAIsAYVQQDD-LFIPTL----- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 432 lgeTADEIKILEA-----------ANAAGLNDVIAQ--LPNGIHTELGEGGYGLSGG--ERQRLALARAFLKRPGIILFD 496
Cdd:TIGR00955 115 ---TVREHLMFQAhlrmprrvtkkEKRERVDEVLQAlgLRKCANTRIGVPGRVKGLSggERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2048238220 497 EPTTGLDLVTEQIVRRSIEELS-REATLVTVAHR--LHTIKQADAIWFMDDGKLLAQGTHDELlsVPQYADL 565
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAqKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQA--VPFFSDL 261
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
336-530 |
8.19e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.96 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSfAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVL---NVLSGLVkpDSGRVlvDGEPleTYTDSSWYDT- 411
Cdd:PRK14243 11 LRTENLN-VYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLI--PGFRV--EGKV--TFHGKNLYAPd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 ---------IGYISQNPYLFAGTVADNIALGETADEIKileaanaAGLNDVI------AQLPNGIHTELGEGGYGLSGGE 476
Cdd:PRK14243 84 vdpvevrrrIGMVFQKPNPFPKSIYDNIAYGARINGYK-------GDMDELVerslrqAALWDEVKDKLKQSGLSLSGGQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 477 RQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHRL 530
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
334-558 |
8.98e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 334 PDLELDAVSfAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETY-TDSSWYDTI 412
Cdd:PRK11614 4 VMLSFDKVS-AHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNPYLFAG-TVADNIALGET-ADEIKILEAanaagLNDVIAQLPNgIHTELGEGGYGLSGGERQRLALARAFLKRP 490
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGGFfAERDQFQER-----IKWVYELFPR-LHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 491 GIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRLH-TIKQADAIWFMDDGKLLAQGTHDELLS 558
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGmTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-562 |
1.46e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.86 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPD-----SGRVLVDGE--------PLETYTDsswydtIGYISQNPYLFAG- 424
Cdd:PRK14267 27 IPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRniyspdvdPIEVRRE------VGMVFQYPNPFPHl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 425 TVADNIALG-------ETADEI-KILEAA--NAA-------GLNDVIAQLPNGihtelgeggyglsggERQRLALARAFL 487
Cdd:PRK14267 101 TIYDNVAIGvklnglvKSKKELdERVEWAlkKAAlwdevkdRLNDYPSNLSGG---------------QRQRLVIARALA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 488 KRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHR-LHTIKQADAIWFMDDGKLLAQGTHDELLSVPQY 562
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
336-509 |
1.54e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 64.72 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwydtiGYI 415
Cdd:PRK11248 2 LQISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFA-GTVADNIALG-------ETADEIKILEAANAAGL----NDVIAQLPNGihtelgeggyglsggERQRLALA 483
Cdd:PRK11248 76 FQNEGLLPwRNVQDNVAFGlqlagveKMQRLEIAHQMLKKVGLegaeKRYIWQLSGG---------------QRQRVGIA 140
|
170 180
....*....|....*....|....*..
gi 2048238220 484 RAFLKRPGIILFDEPTTGLDLVT-EQI 509
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTrEQM 167
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
336-533 |
2.96e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFayeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDgEPLEtytdsswydtIGYI 415
Cdd:PRK09544 7 LENVSVSF---GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-GKLR----------IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAG---TVADNIALG---ETADEIKILEAANAAGLNDVIAQLPNGIHTelgeggyglsggerQRLALARAFLKR 489
Cdd:PRK09544 73 PQKLYLDTTlplTVNRFLRLRpgtKKEDILPALKRVQAGHLIDAPMQKLSGGET--------------QRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2048238220 490 PGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTI 533
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDLHLV 184
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
359-551 |
3.15e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 63.32 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPletytdsSWYDTIGYiSQNPYLfagTVADNI-----ALG 433
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-------SSLLGLGG-GFNPEL---TGRENIylngrLLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 434 ETADEI--KILEAANAAGLNDVIaQLP-----NGIhtelgeggyglsggeRQRLALARAFLKRPGIILFDEPTTGLDLVT 506
Cdd:cd03220 114 LSRKEIdeKIDEIIEFSELGDFI-DLPvktysSGM---------------KARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2048238220 507 EQIVRRSIEELSREA-TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQG 551
Cdd:cd03220 178 QEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
333-551 |
3.59e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwydTI 412
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN---LV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQNP---YLFAGTVADNIALGE----------TADEIKILEAANA-AGLNDV----IAQLPNGihtelgeggyglsg 474
Cdd:PRK15056 81 AYVPQSEevdWSFPVLVEDVVMMGRyghmgwlrraKKRDRQIVTAALArVDMVEFrhrqIGELSGG-------------- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 475 gERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRLHTIKQADAIWFMDDGKLLAQG 551
Cdd:PRK15056 147 -QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGkTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
336-559 |
4.43e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.55 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFT--------LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSS 407
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 408 W-----------YDTIGYIsqNPylfAGTVADNIA--------LGETADEIKILEAANAAGLNDVIA-----QLPNGiht 463
Cdd:PRK10419 84 RkafrrdiqmvfQDSISAV--NP---RKTVREIIReplrhllsLDKAERLARASEMLRAVDLDDSVLdkrppQLSGG--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 464 elgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQ-ADAIW 540
Cdd:PRK10419 156 ------------QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfgTACLFITHDLRLVERfCQRVM 223
|
250
....*....|....*....
gi 2048238220 541 FMDDGKLLAQGTHDELLSV 559
Cdd:PRK10419 224 VMDNGQIVETQPVGDKLTF 242
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
338-561 |
5.70e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.98 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 338 LDAVSFAyeggrftldplsgmIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYD---TIGY 414
Cdd:COG4608 34 VDGVSFD--------------IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYlfaG------TVADniALGE--------TADEI--KILEAANAAGLN-DVIAQLPN----Gihtelgeggygls 473
Cdd:COG4608 100 VFQDPY---AslnprmTVGD--IIAEplrihglaSKAERreRVAELLELVGLRpEHADRYPHefsgG------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 474 ggERQRLALARAFLKRPGIILFDEPTTGLDL-VTEQIVRRsIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLA 549
Cdd:COG4608 162 --QRQRIGIARALALNPKLIVCDEPVSALDVsIQAQVLNL-LEDLQDElgLTYLFISHDLSVVRHiSDRVAVMYLGKIVE 238
|
250
....*....|..
gi 2048238220 550 QGTHDELLSVPQ 561
Cdd:COG4608 239 IAPRDELYARPL 250
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
362-530 |
7.36e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.81 E-value: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 362 GAHVALVGASGSGKTTVLNVLSGLVKPDSGRVlvDGEP-----LETYTDSSWYD--------------TIGYISQNPYLF 422
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEPswdevLKRFRGTELQDyfkklangeikvahKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 423 AGTVADniaLGETADEIKIL-EAANAAGLNDV----IAQLPNGihtELgeggyglsggerQRLALARAFLKRPGIILFDE 497
Cdd:COG1245 177 KGTVRE---LLEKVDERGKLdELAEKLGLENIldrdISELSGG---EL------------QRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*
gi 2048238220 498 PTTGLDlVTEQI-VRRSIEELSREA-TLVTVAHRL 530
Cdd:COG1245 239 PSSYLD-IYQRLnVARLIRELAEEGkYVLVVEHDL 272
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-528 |
7.66e-11 |
|
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: 62.43 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 345 YEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGepletytdsswyDTIGYISQnpYL--- 421
Cdd:cd03237 8 KTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL------------DTVSYKPQ--YIkad 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 422 FAGTVAD---NIALGETADEIKILEAANAAGLNDVI-AQLPNGIHTElgeggyglsggeRQRLALARAFLKRPGIILFDE 497
Cdd:cd03237 74 YEGTVRDllsSITKDFYTHPYFKTEIAKPLQIEQILdREVPELSGGE------------LQRVAIAACLSKDADIYLLDE 141
|
170 180 190
....*....|....*....|....*....|....*
gi 2048238220 498 PTTGLD----LVTEQIVRRSIEElsREATLVTVAH 528
Cdd:cd03237 142 PSAYLDveqrLMASKVIRRFAEN--NEKTAFVVEH 174
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
359-557 |
1.61e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVdGEPLETYTDSS-----WYDTIGYISQNP--YLFAGTVADNIA 431
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQkeikpVRKKVGVVFQFPesQLFEETVLKDVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 432 LGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGgerQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVR 511
Cdd:PRK13643 108 FGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQM---RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2048238220 512 RSIEELSREA-TLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELL 557
Cdd:PRK13643 185 QLFESIHQSGqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
366-561 |
1.78e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.72 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 366 ALVGASGSGKTTVLNVLS--GLVKPD---SGRVLVDGEPLetYTDSSwyDT------IGYISQNPYLFAGTVADNIALGE 434
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNI--YSPRT--DTvdlrkeIGMVFQQPNPFPMSIYENVVYGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 435 TADEIK---ILEAANAAGLNDviAQLPNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVR 511
Cdd:PRK14239 111 RLKGIKdkqVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIE 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2048238220 512 RSIEELSREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:PRK14239 189 ETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
365-560 |
2.48e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.16 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 365 VALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTdSSWYDTIGYIS--QNPYLFAG-TVADNI----------- 430
Cdd:PRK11300 34 VSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVRtfQHVRLFREmTVIENLlvaqhqqlktg 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 431 -----------------ALGETA---DEIKILEAANAAGLNDVIAQlpngihtelgeggyglsggeRQRLALARAFLKRP 490
Cdd:PRK11300 113 lfsgllktpafrraeseALDRAAtwlERVGLLEHANRQAGNLAYGQ--------------------QRRLEIARCMVTQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2048238220 491 GIILFDEPTTGLDLVTEQIVRRSIEELSREATlVTVAHRLHTIKQ----ADAIWFMDDGKLLAQGTHDELLSVP 560
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHN-VTVLLIEHDMKLvmgiSDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
336-503 |
5.86e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.01 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDG------EPLETytdsswy 409
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnelEPADR------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 410 dTIGYISQN----PYLfagTVADNIALG-----ETADEI--KILEAANAAGLNDVI----AQLPNGihtelgeggyglsg 474
Cdd:PRK11650 77 -DIAMVFQNyalyPHM---SVRENMAYGlkirgMPKAEIeeRVAEAARILELEPLLdrkpRELSGG-------------- 138
|
170 180
....*....|....*....|....*....
gi 2048238220 475 gERQRLALARAFLKRPGIILFDEPTTGLD 503
Cdd:PRK11650 139 -QRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
359-561 |
7.22e-10 |
|
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: 61.62 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVkPDSGRVLVDGEPLETYTDS---SWYDTIGYISQNPYlfaG------TVADN 429
Cdd:COG4172 309 LRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDPF---GslsprmTVGQI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 430 IA---------LGETADEIKILEAANAAGLN-DVIAQLPN----GihtelgeggyglsggERQRLALARAFLKRPGIILF 495
Cdd:COG4172 385 IAeglrvhgpgLSAAERRARVAEALEEVGLDpAARHRYPHefsgG---------------QRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 496 DEPTTGLDlVTeqiVRRSIEELSRE------ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:COG4172 450 DEPTSALD-VS---VQAQILDLLRDlqrehgLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
336-559 |
1.51e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.59 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRfTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGL--VKPDSGRVLV----------------DG 397
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 398 EP-------LETYTDSSW----------YDTIGYISQNPYLFAG--TVADNIalgetadeIKILEAANAAGLNDV--IAQ 456
Cdd:TIGR03269 80 EPcpvcggtLEPEEVDFWnlsdklrrriRKRIAIMLQRTFALYGddTVLDNV--------LEALEEIGYEGKEAVgrAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 457 LPNGIHTELGEGGYGLSGG--ERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVAHRLHT 532
Cdd:TIGR03269 152 LIEMVQLSHRITHIARDLSggEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|....*....
gi 2048238220 533 IKQ-AD-AIWfMDDGKLLAQGTHDELLSV 559
Cdd:TIGR03269 232 IEDlSDkAIW-LENGEIKEEGTPDEVVAV 259
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
341-561 |
1.98e-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: 60.08 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 341 VSFAYEGGRFT-LDPLSGMIPTGAHVALVGASGSGKT-TVLNVL----SGLVKPdSGRVLVDGEPLETYTDSSWY----D 410
Cdd:COG4172 14 VAFGQGGGTVEaVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHP-SGSILFDGQDLLGLSERELRrirgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 TIGYISQ------NPYLfagTVADNIA--------LGETADEIKILEAANAAGLNDVIA-------QLPNGihtelgegg 469
Cdd:COG4172 93 RIAMIFQepmtslNPLH---TIGKQIAevlrlhrgLSGAAARARALELLERVGIPDPERrldayphQLSGG--------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 470 yglsggERQRLALARAFLKRPGIILFDEPTTGLDlVTeqiVRRSIEELSREAT--------LVTvaHRLHTIKQ-ADAIW 540
Cdd:COG4172 161 ------QRQRVMIAMALANEPDLLIADEPTTALD-VT---VQAQILDLLKDLQrelgmallLIT--HDLGVVRRfADRVA 228
|
250 260
....*....|....*....|.
gi 2048238220 541 FMDDGKLLAQGTHDELLSVPQ 561
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAAPQ 249
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
350-503 |
2.20e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 350 FTLDPlsgmiptGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSswydtigYISQNPYL--FAG--- 424
Cdd:PRK13538 22 FTLNA-------GELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYLghQPGikt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 425 --TVADNI----ALGETADE---IKILEAANAAGLNDV-IAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIIL 494
Cdd:PRK13538 88 elTALENLrfyqRLHGPGDDealWEALAQVGLAGFEDVpVRQLSAG---------------QQRRVALARLWLTRAPLWI 152
|
....*....
gi 2048238220 495 FDEPTTGLD 503
Cdd:PRK13538 153 LDEPFTAID 161
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
337-528 |
2.33e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 337 ELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVdGEPLEtytdsswydtIGYIS 416
Cdd:PRK11147 321 EMENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE----------VAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 417 Q-----NPylfAGTVADNIALGETADEIKILEAANAAGLND-----------VIAqLPNGihtelgeggyglsggERQRL 480
Cdd:PRK11147 389 QhraelDP---EKTVMDNLAEGKQEVMVNGRPRHVLGYLQDflfhpkramtpVKA-LSGG---------------ERNRL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2048238220 481 ALARAFLKRPGIILFDEPTTGLDLVTEQIvrrsIEEL--SREATLVTVAH 528
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDVETLEL----LEELldSYQGTVLLVSH 495
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
352-556 |
2.41e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.94 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRV---LVDGEPLETYTDSSWYDT----------------- 411
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEKVLEklviqktrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 ----IGYISQ-NPY-LFAGTVADNIALGETADEIKILEAANAA-------GLNDVIAQ-----LPNGihtelgeggygls 473
Cdd:PRK13651 103 irrrVGVVFQfAEYqLFEQTIEKDIIFGPVSMGVSKEEAKKRAakyielvGLDESYLQrspfeLSGG------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 474 ggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRL-HTIKQADAIWFMDDGKLLAQG 551
Cdd:PRK13651 170 --QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLdNVLEWTKRTIFFKDGKIIKDG 247
|
....*.
gi 2048238220 552 -THDEL 556
Cdd:PRK13651 248 dTYDIL 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
318-516 |
4.81e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.79 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 318 PDERLtwGDRMLtsrtpdlELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVdG 397
Cdd:TIGR03719 314 PGPRL--GDKVI-------EAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-G 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 398 EPLEtytdsswydtIGYISQNPYLFAG--TVADNIALGetADEIKI----------LEAANAAGlND---VIAQLPNGih 462
Cdd:TIGR03719 383 ETVK----------LAYVDQSRDALDPnkTVWEEISGG--LDIIKLgkreipsrayVGRFNFKG-SDqqkKVGQLSGG-- 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2048238220 463 telgeggyglsggERQRLALARAfLKRPG-IILFDEPTTGLDLVTeqivRRSIEE 516
Cdd:TIGR03719 448 -------------ERNRVHLAKT-LKSGGnVLLLDEPTNDLDVET----LRALEE 484
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-311 |
5.86e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 57.52 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 18 IVGLVIAAVMIGLSiLAQAYLIVDIVDQVFL---KNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRL 94
Cdd:cd18563 2 ILGFLLMLLGTALG-LVPPYLTKILIDDVLIqlgPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 95 QLLDRYTsnpiETSLSGQSGKKVSVFMDAV----DEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFI 170
Cdd:cd18563 81 DLYEHLQ----RLSLSFFDKRQTGSLMSRVtsdtDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 171 PIFFIIIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLMLEFI 250
Cdd:cd18563 157 VWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 251 SMLSTGVVALeVALQMVVWENLTF-----FSGFLILVLAPeyylaIKDLGGAFHTGRGSMGAADRI 311
Cdd:cd18563 237 TSLGTLIVWY-FGGRQVLSGTMTLgtlvaFLSYLGMFYGP-----LQWLSRLNNWITRALTSAERI 296
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
359-557 |
8.20e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.40 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGE----------------------------PLETYTdssWYD 410
Cdd:COG4586 45 IEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvpfkrrkefarrigvvfgqrsqlwwdlpAIDSFR---LLK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 TIGYISQNPYLfagtvadnialgETADE-IKILEaanaagLNDVIA----QLPNGihtelgeggyglsggERQRLALARA 485
Cdd:COG4586 122 AIYRIPDAEYK------------KRLDElVELLD------LGELLDtpvrQLSLG---------------QRMRCELAAA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048238220 486 FLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELL 557
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErgTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELK 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
333-558 |
1.28e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.55 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYEGG---RF-TLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDS-- 406
Cdd:PRK13645 4 SKDIILDNVSYTYAKKtpfEFkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 407 ---SWYDTIGYISQNP--YLFAGTVADNIA-----LGETADEI--KILEAANaaglndvIAQLPngiHTELGEGGYGLSG 474
Cdd:PRK13645 84 evkRLRKEIGLVFQFPeyQLFQETIEKDIAfgpvnLGENKQEAykKVPELLK-------LVQLP---EDYVKRSPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 475 GERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVTVAHRL-HTIKQADAIWFMDDGKLLAQG 551
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMdQVLRIADEVIVMHEGKVISIG 233
|
....*..
gi 2048238220 552 THDELLS 558
Cdd:PRK13645 234 SPFEIFS 240
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
359-536 |
2.56e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.40 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPDS---------GRVLVDGEPLETYTDSSWYDTiGYISQNPYLFAG-TVAD 428
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRKSRANT-GYIFQQFNLVNRlSVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 429 NI---ALGET------------ADEIKILEAANAAGL----NDVIAQLPNGihtelgeggyglsggERQRLALARAFLKR 489
Cdd:PRK09984 106 NVligALGSTpfwrtcfswftrEQKQRALQALTRVGMvhfaHQRVSTLSGG---------------QQQRVAIARALMQQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2048238220 490 PGIILFDEPTTGLDLVTEQIVRRSIEELSREATlVTVAHRLHTIKQA 536
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNDG-ITVVVTLHQVDYA 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
359-551 |
2.86e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 54.07 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGL--VKPDSGRVLVDGEPLetyTDSSWYDT----IGYISQNPYLFAG-TVAD--- 428
Cdd:cd03217 23 IKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDI---TDLPPEERarlgIFLAFQYPPEIPGvKNADflr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 429 NIALGETADEIKILEaanaaglndvIAQLpngihtelgeggyglsggerqrlalaraFLKRPGIILFDEPTTGLDLVTEQ 508
Cdd:cd03217 100 YVNEGFSGGEKKRNE----------ILQL----------------------------LLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2048238220 509 IVRRSIEELSREAT---LVTVAHRLHTIKQADAIWFMDDGKLLAQG 551
Cdd:cd03217 142 LVAEVINKLREEGKsvlIITHYQRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
326-525 |
3.04e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 326 DRMLTSRTPDLELDAVSFAyEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTD 405
Cdd:PRK13543 2 IEPLHTAPPLLAAHALAFS-RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 406 SSWydtIGYISQNPYLFAGTVA-DNIAL-----GETADEI--KILEAANAAGLND-VIAQLPNGihtelgeggyglsggE 476
Cdd:PRK13543 81 SRF---MAYLGHLPGLKADLSTlENLHFlcglhGRRAKQMpgSALAIVGLAGYEDtLVRQLSAG---------------Q 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2048238220 477 RQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE--ATLVT 525
Cdd:PRK13543 143 KKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGggAALVT 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
341-503 |
4.11e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.10 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 341 VSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLvdgePLETYTdsswydtIGYISQNPY 420
Cdd:TIGR03719 10 VSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR----PQPGIK-------VGYLPQEPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 421 LFAG-TVADNI--ALGETADEIKILEAANA----------------AGLNDVIAQ------------------LPNGiht 463
Cdd:TIGR03719 79 LDPTkTVRENVeeGVAEIKDALDRFNEISAkyaepdadfdklaaeqAELQEIIDAadawdldsqleiamdalrCPPW--- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2048238220 464 elGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLD 503
Cdd:TIGR03719 156 --DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
352-537 |
4.41e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLEtyTDSSWYDT----IGYISQ-NPYLfagTV 426
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK--KDLCTYQKqlcfVGHRSGiNPYL---TL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 427 ADN--IALGETADEIKILEAANAAGLNDVIaQLPNGIhtelgeggygLSGGERQRLALARAFLKRPGIILFDEPTTGLDL 504
Cdd:PRK13540 92 RENclYDIHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2048238220 505 VTEQIVRRSIEELSRE--ATLVTvAHRLHTIKQAD 537
Cdd:PRK13540 161 LSLLTIITKIQEHRAKggAVLLT-SHQDLPLNKAD 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
336-516 |
4.68e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFTLDPLS-----GMIptgahVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYD 410
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSlevraGEI-----LGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRR 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 411 T-IGYISQNPY---LFAG-TVADNIALGETADE-------IKILEAANAAglNDVIAQL---PNGIHTElgeggyglsgg 475
Cdd:COG3845 333 LgVAYIPEDRLgrgLVPDmSVAENLILGRYRRPpfsrggfLDRKAIRAFA--EELIEEFdvrTPGPDTP----------- 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2048238220 476 ER-------QRLALARAFLKRPGIILFDEPTTGLDL-VTEQIVRRSIEE 516
Cdd:COG3845 400 ARslsggnqQKVILARELSRDPKLLIAAQPTRGLDVgAIEFIHQRLLEL 448
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
352-514 |
5.25e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.01 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPD--SGRVLVDGEP--LETYTDSSwydtiGYISQN----PYLfa 423
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPkkQETFARIS-----GYCEQNdihsPQV-- 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 424 gTVADNIALG-------ETADEIK------ILEAANAAGLNDVIAQLP--NGIHTELgeggyglsggeRQRLALARAFLK 488
Cdd:PLN03140 969 -TVRESLIYSaflrlpkEVSKEEKmmfvdeVMELVELDNLKDAIVGLPgvTGLSTEQ-----------RKRLTIAVELVA 1036
|
170 180
....*....|....*....|....*.
gi 2048238220 489 RPGIILFDEPTTGLDLVTEQIVRRSI 514
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTV 1062
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
316-528 |
7.68e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 316 DAPDERLTwgdrmLTSRTPDLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGlVKPDS----- 390
Cdd:PRK10938 246 DEPSARHA-----LPANEPRIVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndl 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 391 ---GRVLVDGEPLetytdssWyDT---IGYISQNPYL--FAGTVADNIALGETADEIKILEAANAA------------GL 450
Cdd:PRK10938 319 tlfGRRRGSGETI-------W-DIkkhIGYVSSSLHLdyRVSTSVRNVILSGFFDSIGIYQAVSDRqqklaqqwldilGI 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 451 NDVIAQLPngIHTelgeggyglSGGERQRLAL-ARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA--TLVTVA 527
Cdd:PRK10938 391 DKRTADAP--FHS---------LSWGQQRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGetQLLFVS 459
|
.
gi 2048238220 528 H 528
Cdd:PRK10938 460 H 460
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
338-562 |
8.07e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.20 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 338 LDAVSFAYEGGRfTLdplsgmiptgahvALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYD---TIGY 414
Cdd:PRK11308 31 LDGVSFTLERGK-TL-------------AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLlrqKIQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPY-----------LFAGTVADNIALGETADEIKILEAANAAGLNDVIAQ-----LPNGihtelgeggyglsggERQ 478
Cdd:PRK11308 97 VFQNPYgslnprkkvgqILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDryphmFSGG---------------QRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 479 RLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATL--VTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDE 555
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQ 241
|
....*..
gi 2048238220 556 LLSVPQY 562
Cdd:PRK11308 242 IFNNPRH 248
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
354-526 |
8.47e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.52 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 354 PLSGMIptgahVALVGASGSGKTTVLNVLSGLVKPDSGRVlvDGEP-------------LETYTDSSWYDTIG------Y 414
Cdd:cd03236 23 PREGQV-----LGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPPdwdeildefrgseLQNYFTKLLEGDVKvivkpqY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 415 ISQNPYLFAGTVADNIalgETADE-------IKILEAANAagLNDVIAQLPNGihtelgeggyglsggERQRLALARAFL 487
Cdd:cd03236 96 VDLIPKAVKGKVGELL---KKKDErgkldelVDQLELRHV--LDRNIDQLSGG---------------ELQRVAIAAALA 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2048238220 488 KRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTV 526
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLV 194
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
334-547 |
1.53e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 334 PDLELDAVSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDTIG 413
Cdd:PLN03073 507 PIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 414 yISQNPYLFAGTVADNIAlgetadEIKILEAANAAGLNDVIAQLPngIHTelgeggygLSGGERQRLALARAFLKRPGII 493
Cdd:PLN03073 587 -LSSNPLLYMMRCFPGVP------EQKLRAHLGSFGVTGNLALQP--MYT--------LSGGQKSRVAFAKITFKKPHIL 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 494 LFDEPTTGLDLvteQIVRRSIEELSR-EATLVTVAHRLHTIK-QADAIWFMDDGKL 547
Cdd:PLN03073 650 LLDEPSNHLDL---DAVEALIQGLVLfQGGVLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
348-533 |
2.48e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 348 GRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDgepletytdsswyDTIGYISQnpYL---FAG 424
Cdd:PRK13409 351 GDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQ--YIkpdYDG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 425 TVADNiaLGETADEIK----ILEAANAAGLNDV----IAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFD 496
Cdd:PRK13409 416 TVEDL--LRSITDDLGssyyKSEIIKPLQLERLldknVKDLSGG---------------ELQRVAIAACLSRDADLYLLD 478
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2048238220 497 EPTTGLD----LVTEQIVRRSIEElsREATLVTVAHRLHTI 533
Cdd:PRK13409 479 EPSAHLDveqrLAVAKAIRRIAEE--REATALVVDHDIYMI 517
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
352-551 |
2.73e-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: 51.11 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPD---SGRVLVDGEPLETYTDSSWYDTIgYISQN----PYLfag 424
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEII-YVSEEdvhfPTL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 425 TVadnialGETADEikileAANAAGlNDVIAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLDL 504
Cdd:cd03233 99 TV------RETLDF-----ALRCKG-NEFVRGISGG---------------ERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 505 VTE-QIVrRSIEELSREATLVTVAhrlhTIKQA--------DAIWFMDDGKLLAQG 551
Cdd:cd03233 152 STAlEIL-KCIRTMADVLKTTTFV----SLYQAsdeiydlfDKVLVLYEGRQIYYG 202
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
21-285 |
2.84e-07 |
|
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: 52.43 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 21 LVIAAVMIGLSILAQA---YLIVDIVDQVfLKNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQLL 97
Cdd:cd18542 1 YLLAILALLLATALNLlipLLIRRIIDSV-IGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 98 DRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHW----ISGVIMMVTAPFIPIF 173
Cdd:cd18542 80 DHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWkltlISLAIIPFIALFSYVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 174 FIIIGIATQKKSEqQMEKMNqfsgkflDVLQ----GLTTLKLYGRTEREAQAIEKSSLDFRDATMvvlKTAFLSGL---M 246
Cdd:cd18542 160 FKKVRPAFEEIRE-QEGELN-------TVLQenltGVRVVKAFAREDYEIEKFDKENEEYRDLNI---KLAKLLAKywpL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2048238220 247 LEFISMLSTGVVALeVALQMVVWENLTF-----FSGFLILVLAP 285
Cdd:cd18542 229 MDFLSGLQIVLVLW-VGGYLVINGEITLgelvaFISYLWMLIWP 271
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
361-539 |
3.57e-07 |
|
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: 50.06 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 361 TGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVL-VDGEPLETYTDSSWYDTIGYISQNPYLFAgtvadnialgetadei 439
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLIIVGGKKASGSGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 440 kileaanaaglndviaqlpngihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSR 519
Cdd:smart00382 65 ------------------------------------LRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180
....*....|....*....|....*..
gi 2048238220 520 E-------ATLVTVAHRLHTIKQADAI 539
Cdd:smart00382 109 LllkseknLTVILTTNDEKDLGPALLR 135
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
21-260 |
4.51e-07 |
|
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: 51.64 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 21 LVIAAVMIGLSILAQA---YLIVDIVDQVFL-----KNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTL 92
Cdd:cd18547 1 LILVIILAIISTLLSVlgpYLLGKAIDLIIEglgggGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 93 RLQLLDRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPi 172
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 173 ffIIIGI---ATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMvvlKTAFLSGLM--- 246
Cdd:cd18547 160 --LVTKFiakRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASF---KAQFYSGLLmpi 234
|
250
....*....|....
gi 2048238220 247 LEFISMLSTGVVAL 260
Cdd:cd18547 235 MNFINNLGYVLVAV 248
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
359-561 |
4.59e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.34 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSwyDTIGYISQN----PYLfagTVADNIALG- 433
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSyalyPHL---SVAENMSFGl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 434 --ETADEIKILEAANAAG----LNDVIAQLPNGIhtelgeggyglSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTE 507
Cdd:PRK11000 101 klAGAKKEEINQRVNQVAevlqLAHLLDRKPKAL-----------SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 508 QIVRRSIEELSR--EATLVTVAH-RLHTIKQADAIWFMDDGKLLAQGTHDELLSVPQ 561
Cdd:PRK11000 170 VQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
478-556 |
4.61e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.09 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 478 QRLALARAFLKR---PGIILFDEPTTGLDLvteQIVRRSIEELSREA----TLVTVAHRLHTIKQADaiWFMD------- 543
Cdd:TIGR00630 836 QRIKLAKELSKRstgRTLYILDEPTTGLHF---DDIKKLLEVLQRLVdkgnTVVVIEHNLDVIKTAD--YIIDlgpeggd 910
|
90
....*....|....
gi 2048238220 544 -DGKLLAQGTHDEL 556
Cdd:TIGR00630 911 gGGTVVASGTPEEV 924
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
333-547 |
5.28e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRV-LVDGEPLetytdsswydt 411
Cdd:PRK10636 310 NPLLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKL----------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 iGYISQNPYLFagTVADNIALGETAdeiKILEAANAAGLNDVIAQLpnGIHTELGEGGYGLSGG-ERQRLALARAFLKRP 490
Cdd:PRK10636 378 -GYFAQHQLEF--LRADESPLQHLA---RLAPQELEQKLRDYLGGF--GFQGDKVTEETRRFSGgEKARLVLALIVWQRP 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2048238220 491 GIILFDEPTTGLDLVTEQIVRRSIEELsrEATLVTVAHRLHTIKQ-ADAIWFMDDGKL 547
Cdd:PRK10636 450 NLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
477-556 |
8.36e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 477 RQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSRE-ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHD 554
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVD 229
|
..
gi 2048238220 555 EL 556
Cdd:NF000106 230 EL 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
336-516 |
9.35e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVdGEPLEtytdsswydtIGYI 415
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQNPYLFAG--TVADNIALGetADEIKI----------LEAANAAGlND---VIAQLPNGihtelgeggyglsggERQRL 480
Cdd:PRK11819 393 DQSRDALDPnkTVWEEISGG--LDIIKVgnreipsrayVGRFNFKG-GDqqkKVGVLSGG---------------ERNRL 454
|
170 180 190
....*....|....*....|....*....|....*..
gi 2048238220 481 ALARAfLKRPG-IILFDEPTTGLDLVTeqivRRSIEE 516
Cdd:PRK11819 455 HLAKT-LKQGGnVLLLDEPTNDLDVET----LRALEE 486
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
349-559 |
1.24e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.42 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 349 RFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDS--GRVLVDGEPLETYTdsswYDTIGYISQNPYLF---- 422
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQI----LKRTGFVTQDDILYphlt 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 423 ---------------AGTVADNIALGETA-DEIKILEAANAAGLNDVIAQLPNGihtelgeggyglsggERQRLALARAF 486
Cdd:PLN03211 157 vretlvfcsllrlpkSLTKQEKILVAESViSELGLTKCENTIIGNSFIRGISGG---------------ERKRVSIAHEM 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 487 LKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRLHT--IKQADAIWFMDDGKLLAQGTHDELLSV 559
Cdd:PLN03211 222 LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGkTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMAY 297
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
355-543 |
1.35e-06 |
|
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: 51.29 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 355 LSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEpletytdsswyDTIGYISQNPYLFAGTVADNIALGE 434
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLGTLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 435 TADE-----------IKILEAANaagLNDVIAQlpNGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLD 503
Cdd:TIGR00954 540 SSEDmkrrglsdkdlEQILDNVQ---LTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2048238220 504 LVTEQivrrSIEELSREA--TLVTVAHRLHTIKQADAIWFMD 543
Cdd:TIGR00954 615 VDVEG----YMYRLCREFgiTLFSVSHRKSLWKYHEYLLYMD 652
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
18-311 |
1.35e-06 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 50.12 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 18 IVGLVIAAVMIGLSiLAQAYLIVDIVDQVFLKNASFESIVPTLGWLILALVTRAGFGYMSGRIGaslsEKAKRTLRLQLL 97
Cdd:cd18551 2 ILALLLSLLGTAAS-LAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTG----ERVVLDLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 98 DRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFIII 177
Cdd:cd18551 77 RRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 178 GIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLK-TAFLS-----GLMLEFIS 251
Cdd:cd18551 157 GRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKiEALIGplmglAVQLALLV 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048238220 252 MLSTGVV-----ALEVAlqmvvweNLTFFSGFLILVLAPeyylaIKDLGGAFHTGRGSMGAADRI 311
Cdd:cd18551 237 VLGVGGArvasgALTVG-------TLVAFLLYLFQLITP-----LSQLSSFFTQLQKALGALERI 289
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
341-503 |
1.63e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 341 VSFAYEGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLvdgePLETYTdsswydtIGYISQNPY 420
Cdd:PRK11819 12 VSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR----PAPGIK-------VGYLPQEPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 421 LFAG-TVADNI--ALGETADEIK----------------------------ILEAANAAGLND----------------V 453
Cdd:PRK11819 81 LDPEkTVRENVeeGVAEVKAALDrfneiyaayaepdadfdalaaeqgelqeIIDAADAWDLDSqleiamdalrcppwdaK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2048238220 454 IAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGLD 503
Cdd:PRK11819 161 VTKLSGG---------------ERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
336-557 |
1.96e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGGRFtLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVlvdgepletytdsSWYD--TIG 413
Cdd:PRK15064 320 LEVENLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------------KWSEnaNIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 414 YISQNPYL-FAG--TVADNIA---------------LGE---TADEIKilEAANaaglndVIAQLPNGihtelgeggygl 472
Cdd:PRK15064 386 YYAQDHAYdFENdlTLFDWMSqwrqegddeqavrgtLGRllfSQDDIK--KSVK------VLSGGEKG------------ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 473 sggerqRLALARAFLKRPGIILFDEPTTGLDLvteqivrRSIEELSR-----EATLVTVAH-RLHTIKQADAIWFMDDGK 546
Cdd:PRK15064 446 ------RMLFGKLMMQKPNVLVMDEPTNHMDM-------ESIESLNMalekyEGTLIFVSHdREFVSSLATRIIEITPDG 512
|
250
....*....|..
gi 2048238220 547 LLA-QGTHDELL 557
Cdd:PRK15064 513 VVDfSGTYEEYL 524
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
333-551 |
2.05e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 333 TPDLELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT- 411
Cdd:PRK09700 3 TPYISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 412 IGYISQNPYLFAG-TVADNIALGEtadeikiLEAANAAGLNDV----------IAQLPNGIHTELGEGGYGLSGGERQRL 480
Cdd:PRK09700 82 IGIIYQELSVIDElTVLENLYIGR-------HLTKKVCGVNIIdwremrvraaMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 481 ALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREAT-LVTVAHRLHTIKQ-ADAIWFMDDGKLLAQG 551
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
347-546 |
2.99e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 347 GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGlVKPD---SGRVLVDGEPLETYTDSswyDT----IGYISQN- 418
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNIR---DTeragIAIIHQEl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 419 ---PYLfagTVADNIALGETADEIKILE-AANAAGLNDVIAQLpnGIHTELGEGGYGLSGGERQRLALARAFLKRPGIIL 494
Cdd:PRK13549 92 alvKEL---SVLENIFLGNEITPGGIMDyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 495 FDEPTTGLdlvTEQ---IVRRSIEEL-SREATLVTVAHRLHTIKQ-ADAIWFMDDGK 546
Cdd:PRK13549 167 LDEPTASL---TESetaVLLDIIRDLkAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
478-552 |
3.57e-06 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.76 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 478 QRLALARAFLKR---PGIILFDEPTTGLDLvteQIVRRSIEELSR--EA--TLVTVAHRLHTIKQADaiWFMD------- 543
Cdd:cd03271 176 QRIKLAKELSKRstgKTLYILDEPTTGLHF---HDVKKLLEVLQRlvDKgnTVVVIEHNLDVIKCAD--WIIDlgpeggd 250
|
90
....*....|
gi 2048238220 544 -DGKLLAQGT 552
Cdd:cd03271 251 gGGQVVASGT 260
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
365-520 |
4.28e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.63 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 365 VALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETytdSSWYDT----IGYISQNPY---LFAG-TVADNIALGETA 436
Cdd:COG1129 281 LGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI---RSPRDAiragIAYVPEDRKgegLVLDlSIRENITLASLD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 437 --------DEIKILEAAN---------AAGLNDVIAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPT 499
Cdd:COG1129 358 rlsrggllDRRRERALAEeyikrlrikTPSPEQPVGNLSGG---------------NQQKVVLAKWLATDPKVLILDEPT 422
|
170 180
....*....|....*....|.
gi 2048238220 500 TGLDLVTEQIVRRSIEELSRE 520
Cdd:COG1129 423 RGIDVGAKAEIYRLIRELAAE 443
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
358-565 |
4.53e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 358 MIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGR--------VLVDGEPLETYTDSSWYD-TIGYISQNPYLFAGTVAD 428
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDEWQRnNTDMLSPGEDDTGRTTAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 429 nIALGETADEIKILEAANAAGLNDVIA----QLPNGihtelgeggyglsgGERQRLaLARAFLKRPGIILFDEPTTGLDL 504
Cdd:PRK10938 105 -IIQDEVKDPARCEQLAQQFGITALLDrrfkYLSTG--------------ETRKTL-LCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 505 VTEQIVRRSIEELSREA-TLVTVAHRLHTI-KQADAIWFMDDGKLLAQGTHDELLSVPQYADL 565
Cdd:PRK10938 169 ASRQQLAELLASLHQSGiTLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQALVAQL 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
350-563 |
4.77e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.32 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 350 FTLDPlsgmiptGAHVALVGASGSGKTTVLNVLSGLVkPDSGRVLVDGEPLETYTDSS-----------WYDTigYISQN 418
Cdd:PRK15134 307 FTLRP-------GETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQllpvrhriqvvFQDP--NSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 419 PYLfagTVADNIA---------LGETADEIKILEAANAAGLNDVI-----AQLPNGihtelgeggyglsggERQRLALAR 484
Cdd:PRK15134 377 PRL---NVLQIIEeglrvhqptLSAAQREQQVIAVMEEVGLDPETrhrypAEFSGG---------------QRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 485 AFLKRPGIILFDEPTTGLD-LVTEQIVR--RSIEELSREATLVtVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLSVP 560
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDkTVQAQILAllKSLQQKHQLAYLF-ISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAP 517
|
...
gi 2048238220 561 QYA 563
Cdd:PRK15134 518 QQE 520
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
366-549 |
4.78e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 366 ALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDSSWYDT-IGYISQNPYLFAG-TVADNIALGET------AD 437
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELNLVLQrSVMDNMWLGRYptkgmfVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 438 EIKILEAANAaglndVIAQLpnGIHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLdlvTEQIVR---RSI 514
Cdd:PRK10982 108 QDKMYRDTKA-----IFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVNhlfTII 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 2048238220 515 EEL-SREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLA 549
Cdd:PRK10982 178 RKLkERGCGIVYISHKMEEIFQlCDEITILRDGQWIA 214
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
366-550 |
5.41e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 366 ALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETY-TDSSWYDTIGYISQNPYLFAG-TVADNIALGE-------TA 436
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgPKSSQEAGIGIIHQELNLIPQlTIAENIFLGRefvnrfgRI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 437 DEIKILEAANA--AGLN------DVIAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPTTGL-DLVTE 507
Cdd:PRK10762 114 DWKKMYAEADKllARLNlrfssdKLVGELSIG---------------EQQMVEIAKVLSFESKVIIMDEPTDALtDTETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2048238220 508 QIVrRSIEELSREAT-LVTVAHRLHTIKQ-ADAIWFMDDGKLLAQ 550
Cdd:PRK10762 179 SLF-RVIRELKSQGRgIVYISHRLKEIFEiCDDVTVFRDGQFIAE 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
316-539 |
6.37e-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: 49.63 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 316 DAPDERltwgDRMLT--SRTPDLELDAVSFAYEGGRF-TLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGR 392
Cdd:TIGR01257 1920 DVAEER----QRIISggNKTDILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD 1995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 393 VLVDGEPLETyTDSSWYDTIGYISQ------------NPYLFAGTvadniaLGETADEIKilEAANAAglndvIAQLpnG 460
Cdd:TIGR01257 1996 ATVAGKSILT-NISDVHQNMGYCPQfdaiddlltgreHLYLYARL------RGVPAEEIE--KVANWS-----IQSL--G 2059
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048238220 461 IHTELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATLVTVAHrlHTIKQADAI 539
Cdd:TIGR01257 2060 LSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTS--HSMEECEAL 2136
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
336-533 |
8.37e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.63 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 336 LELDAVSFAYEGgrFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDgepletytdsswyDTIGYI 415
Cdd:COG1245 342 VEYPDLTKSYGG--FSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 416 SQnpYL---FAGTVADnialgetadeikILEAANAAGLNDVIAQL----PNGIHTELGEGGYGLSGGERQRLALARAFLK 488
Cdd:COG1245 407 PQ--YIspdYDGTVEE------------FLRSANTDDFGSSYYKTeiikPLGLEKLLDKNVKDLSGGELQRVAIAACLSR 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2048238220 489 RPGIILFDEPTTGLD----LVTEQIVRRSIEElsREATLVTVAHRLHTI 533
Cdd:COG1245 473 DADLYLLDEPSAHLDveqrLAVAKAIRRFAEN--RGKTAMVVDHDIYLI 519
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
347-549 |
9.28e-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: 48.28 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 347 GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGlVKPD---SGRVLVDGEPLETytdSSWYDT----IGYISQNP 419
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKA---SNIRDTeragIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 420 YLFAG-TVADNIALGE--------TADEIKILEAANaaglndVIAQLPNGIhTELGEGGYGLSGGERQRLALARAFLKRP 490
Cdd:TIGR02633 88 TLVPElSVAENIFLGNeitlpggrMAYNAMYLRAKN------LLRELQLDA-DNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2048238220 491 GIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRLHTIKQ-ADAIWFMDDGKLLA 549
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGvACVYISHKLNEVKAvCDTICVIRDGQHVA 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
348-552 |
1.86e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.74 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 348 GRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSG-LVKPD-------SGRVLVDGEPLETYTDSSWYDTIGYISQnp 419
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQ-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 420 ylfagtvADNIALGETADEIKILEAANAAGLNDVIAQLPNGIHTELGEGGYGLSGGERQ----------RLALARAFLK- 488
Cdd:PRK13547 91 -------AAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDvttlsggelaRVQFARVLAQl 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2048238220 489 --------RPGIILFDEPTTGLDLVTEQIVRRSIEELSREATL--VTVAHRLH-TIKQADAIWFMDDGKLLAQGT 552
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
359-551 |
2.27e-05 |
|
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: 45.01 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNvlSGLVKPDSGRvLVDGEPLETYTDSSWYDTIGYISQN--PYLFAGTVADNIALGEta 436
Cdd:cd03238 18 IPLNVLVVVTGVSGSGKSTLVN--EGLYASGKAR-LISFLPKFSRNKLIFIDQLQFLIDVglGYLTLGQKLSTLSGGE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 437 deikileaanaaglndviaqlpngihtelgeggyglsggeRQRLALARAFLKRPG--IILFDEPTTGLDLVTEQIVRRSI 514
Cdd:cd03238 93 ----------------------------------------LQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2048238220 515 EELSREA-TLVTVAHRLHTIKQADAIWFM------DDGKLLAQG 551
Cdd:cd03238 133 KGLIDLGnTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
21-239 |
2.31e-05 |
|
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: 46.41 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 21 LVIAAVMIGLSILAQ---AYLIVDIVDQVFLKNASFESIVP--------------TLGWLILALVTRAGFGYMSGRIGAS 83
Cdd:cd18565 1 LVLGLLASILNRLFDlapPLLIGVAIDAVFNGEASFLPLVPaslgpadprgqlwlLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 84 LSEKAKRTLRLQLLDRYTSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIM 163
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048238220 164 MVTAPFIPIFFIIIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKT 239
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRL 236
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
478-561 |
4.22e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 478 QRLALARAFLKRPG---IILFDEPTTGL---DlvteqiVRRSIEELSR--EA--TLVTVAHRLHTIKQADaiWFMD---- 543
Cdd:COG0178 833 QRVKLASELSKRSTgktLYILDEPTTGLhfhD------IRKLLEVLHRlvDKgnTVVVIEHNLDVIKTAD--WIIDlgpe 904
|
90 100
....*....|....*....|..
gi 2048238220 544 --D--GKLLAQGTHDELLSVPQ 561
Cdd:COG0178 905 ggDggGEIVAEGTPEEVAKVKA 926
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
341-562 |
5.16e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 341 VSFAYEGGRF-TLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGE----------PLETYTDSSWY 409
Cdd:PRK10261 20 IAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 410 DTIG----------YISQNPYLFAG-TVADNIALGETA-------------DEIKILEAAnaAGLNDVIAQLPNGIhtel 465
Cdd:PRK10261 100 HVRGadmamifqepMTSLNPVFTVGeQIAESIRLHQGAsreeamveakrmlDQVRIPEAQ--TILSRYPHQLSGGM---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 466 geggyglsggeRQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREATL--VTVAHRLHTIKQ-ADAIWFM 542
Cdd:PRK10261 174 -----------RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEiADRVLVM 242
|
250 260
....*....|....*....|
gi 2048238220 543 DDGKLLAQGTHDELLSVPQY 562
Cdd:PRK10261 243 YQGEAVETGSVEQIFHAPQH 262
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
359-552 |
5.52e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 45.06 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGL--VKPDSGRVLVDGEPLetyTDSSWYDT----IGYISQNPYLFAG-TVAD--N 429
Cdd:COG0396 23 IKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDI---LELSPDERaragIFLAFQYPVEIPGvSVSNflR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 430 IALGETAD-EIKILEAanaagLNDVIAQLpngihtelgeggyglsggerQRLALARAFLKR------------------- 489
Cdd:COG0396 100 TALNARRGeELSAREF-----LKLLKEKM--------------------KELGLDEDFLDRyvnegfsggekkrneilqm 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 490 ----PGIILFDEPTTGLDLVTEQIVRRSIEEL-SREATLVTVAH--RLHTIKQADAIWFMDDGKLLAQGT 552
Cdd:COG0396 155 lllePKLAILDETDSGLDIDALRIVAEGVNKLrSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
359-506 |
5.93e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 359 IPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPletytdsswydTIGYISQNP-YLFAGTVADNIA--LGET 435
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDL-----------IVARLQQDPpRNVEGTVYDFVAegIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 436 ADEIK--------------------------ILEAANAAGL----NDVIAQLpnGIHTELGEGGYGLSGGerQRLALARA 485
Cdd:PRK11147 95 AEYLKryhdishlvetdpseknlnelaklqeQLDHHNLWQLenriNEVLAQL--GLDPDAALSSLSGGWL--RKAALGRA 170
|
170 180
....*....|....*....|.
gi 2048238220 486 FLKRPGIILFDEPTTGLDLVT 506
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
337-565 |
1.53e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 337 ELDAVSFAYeGGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDT----I 412
Cdd:NF033858 3 RLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM---ADARHRRAvcprI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 413 GYISQ----NPY--LfagTVADNIA-------LGETADEIKILEAANAAGLN---DVIA-QLPNGIhtelgeggyglsgg 475
Cdd:NF033858 79 AYMPQglgkNLYptL---SVFENLDffgrlfgQDAAERRRRIDELLRATGLApfaDRPAgKLSGGM-------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 476 eRQRLALARAFLKRPGIILFDEPTTGLD---------LVtEQIVRRS-----------IEELSREATLVTvahrlhtikq 535
Cdd:NF033858 142 -KQKLGLCCALIHDPDLLILDEPTTGVDplsrrqfweLI-DRIRAERpgmsvlvatayMEEAERFDWLVA---------- 209
|
250 260 270
....*....|....*....|....*....|
gi 2048238220 536 adaiwfMDDGKLLAQGTHDELLSVPQYADL 565
Cdd:NF033858 210 ------MDAGRVLATGTPAELLARTGADTL 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
477-530 |
2.61e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.56 E-value: 2.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2048238220 477 RQRLALARAFLKRPGIILFDEPTTGLDL-VTEQIVRRsIEELSRE--ATLVTVAHRL 530
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVtVQAQIMTL-LNELKREfnTAIIMITHDL 222
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
18-258 |
4.68e-04 |
|
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: 42.37 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 18 IVGLVIAAVMIGLSiLAQAYLIVDIVDQVFLKNAS-FESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQL 96
Cdd:cd18544 2 ILALLLLLLATALE-LLGPLLIKRAIDDYIVPGQGdLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 97 LDR--------YTSNPIetslsgqsGKKVSVF---MDAVDEVdayFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMV 165
Cdd:cd18544 81 FSHiqrlplsfFDRTPV--------GRLVTRVtndTEALNEL---FTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 166 T---APFIPIFFIIIGIATQKKSEQQMEKMNQFsgkFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFL 242
Cdd:cd18544 150 VlplLLLATYLFRKKSRKAYREVREKLSRLNAF---LQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFAL 226
|
250
....*....|....*.
gi 2048238220 243 SGLMLEFISMLSTGVV 258
Cdd:cd18544 227 FRPLVELLSSLALALV 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
362-510 |
5.90e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.92 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 362 GAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLETYTDS---SWYDTIGYISQNPYLFAG---TVADNIA---- 431
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQDPYASLDprqTVGDSIMeplr 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 432 -----LGETAdeikileAANAAGLNDVIAQLPNgihtELGEGGYGLSGGERQRLALARAFLKRPGIILFDEPTTGLDL-V 505
Cdd:PRK10261 430 vhgllPGKAA-------AARVAWLLERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVsI 498
|
....*
gi 2048238220 506 TEQIV 510
Cdd:PRK10261 499 RGQII 503
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
347-504 |
7.16e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 347 GGRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGepletytdsSWydTIGYISQNPYLFAGTV 426
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---------NW--QLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 427 ADNIALGETadEIKILEA--------------ANAAGLNDVI---------AQLPNGI---HTELGEGGYGLSGGERQRL 480
Cdd:PRK10636 81 LEYVIDGDR--EYRQLEAqlhdanerndghaiATIHGKLDAIdawtirsraASLLHGLgfsNEQLERPVSDFSGGWRMRL 158
|
170 180
....*....|....*....|....
gi 2048238220 481 ALARAFLKRPGIILFDEPTTGLDL 504
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDL 182
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
15-291 |
9.39e-04 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 41.28 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 15 KRHIVGLVIAAVMIGLSILAQAYLIVDIVDQVfLKNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKakrtLRL 94
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDI-IPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQK----LDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 95 QLLDRYTSN----PIETSLSGQSGKKVSVFMDAVDEVDAyFSQywpqVIQTSIIPLLILVVV----FSQHWISGVIMMVT 166
Cdd:cd18570 76 RLILGYFKHllklPLSFFETRKTGEIISRFNDANKIREA-ISS----TTISLFLDLLMVIISgiilFFYNWKLFLITLLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 167 APFIPIFFIIIGIATQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDATMVVLKTAFLSGLM 246
Cdd:cd18570 151 IPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2048238220 247 LEFISMLSTgVVALEVALQMVVWENLT------------FFSGFL--ILVLAPEYYLAI 291
Cdd:cd18570 231 KGLISLIGS-LLILWIGSYLVIKGQLSlgqliafnallgYFLGPIenLINLQPKIQEAK 288
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
24-269 |
1.07e-03 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 41.32 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 24 AAVMIGLS---ILAQAYLIVDIVDQVFLkNASFESIVPTLGWLILALVTRAGFGYMSGRIGASLSEKAKRTLRLQLLDRY 100
Cdd:cd18576 1 GLILLLLSsaiGLVFPLLAGQLIDAALG-GGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 101 TSNPIETSLSGQSGKKVSVFMDAVDEVDAYFSQYWPQVIQTSIIPLLILVVVFSQHWISGVIMMVTAPFIPIFFIIIGIA 180
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 181 TQKKSEQQMEKMNQFSGKFLDVLQGLTTLKLYGRTEREAQAIEKSSLDFRDatmVVLKTAFLSGLMLEFISMLSTGVVAL 260
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVK---LALKRARIRALFSSFIIFLLFGAIVA 236
|
....*....
gi 2048238220 261 evalqmVVW 269
Cdd:cd18576 237 ------VLW 239
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
350-562 |
1.10e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 350 FTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEpletytdsswydtIGYISQNPYLFAG-TVAD 428
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIAISAGLSGQlTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 429 NI-----ALGETADEIKIL--EAANAAGLNDVIAQlpngihtelgeGGYGLSGGERQRLALARAFLKRPGIILFDEP-TT 500
Cdd:PRK13546 105 NIefkmlCMGFKRKEIKAMtpKIIEFSELGEFIYQ-----------PVKKYSSGMRAKLGFSINITVNPDILVIDEAlSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048238220 501 GLDLVTEQIVRRSIEELSREATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHDELLsvPQY 562
Cdd:PRK13546 174 GDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVL--PKY 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
352-555 |
1.21e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 352 LDPLSGMIPTGAHVALVGASGSGKTTVLNVLS----GLVKPDSGRVLVDGEPLETYTDSSWYDTIgYISQN----PYL-- 421
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVV-YNAETdvhfPHLtv 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 422 -----FA------GTVADNIALGETADEIKILEAAnAAGL---------NDVIAQLPNGihtelgeggyglsggERQRLA 481
Cdd:TIGR00956 156 getldFAarcktpQNRPDGVSREEYAKHIADVYMA-TYGLshtrntkvgNDFVRGVSGG---------------ERKRVS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 482 LARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAhrlhtIKQA--------DAIWFMDDGKLLAQGT 552
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILdTTPLVA-----IYQCsqdayelfDKVIVLYEGYQIYFGP 294
|
...
gi 2048238220 553 HDE 555
Cdd:TIGR00956 295 ADK 297
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
478-561 |
1.54e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 478 QRLALARAFLKRP-G--IILFDEPTTGL---DlvteqiVRRSIEELSReatLV----TVA---HRLHTIKQADaiWFMD- 543
Cdd:PRK00349 837 QRVKLAKELSKRStGktLYILDEPTTGLhfeD------IRKLLEVLHR---LVdkgnTVVvieHNLDVIKTAD--WIIDl 905
|
90 100
....*....|....*....|....*
gi 2048238220 544 -------DGKLLAQGTHDELLSVPQ 561
Cdd:PRK00349 906 gpeggdgGGEIVATGTPEEVAKVEA 930
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
479-520 |
1.94e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 1.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2048238220 479 RLALARAFLKRPGIILFDEPTTGLDlvtEQIVRRSIEELSRE 520
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEE 167
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
478-562 |
2.11e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 478 QRLALARAFLKRPGIILFDEPTTGLDLVTE-QIVRRSIEELSRE-ATLVTVAHRLHTIKQ-ADAIWFMDDGKLLAQGTHD 554
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQaQIIELLLELQQKEnMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAH 239
|
....*...
gi 2048238220 555 ELLSVPQY 562
Cdd:PRK11022 240 DIFRAPRH 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
477-556 |
2.83e-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: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 477 RQRLALARAFLKRPGIILFDEPTTGLDLVTEQIVRRSIEELSREA-TLVTVAHRL-HTIKQADAIWFMDDGKLLAQGTHD 554
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELaEVLGLSDRVLVIGEGKLKGDFVNH 488
|
..
gi 2048238220 555 EL 556
Cdd:TIGR02633 489 AL 490
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
369-526 |
3.58e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 369 GASGSGKTTVLNVLSGLVKPDSGRVLVDGEPLetyTDSSWYDT----IGYISQ----NPYLFAGTVADNIALG------- 433
Cdd:PRK09700 296 GLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI---SPRSPLDAvkkgMAYITEsrrdNGFFPNFSIAQNMAISrslkdgg 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 434 --------------ETADEIKILEAANAAGLNDVIAQLPNGihtelgeggyglsggERQRLALARAFLKRPGIILFDEPT 499
Cdd:PRK09700 373 ykgamglfhevdeqRTAENQRELLALKCHSVNQNITELSGG---------------NQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180
....*....|....*....|....*..
gi 2048238220 500 TGLDLVTEQIVRRSIEELSREATLVTV 526
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGKVILM 464
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
348-530 |
5.90e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 37.94 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 348 GRFTLDPLSGMIPTGAHVALVGASGSGKTTVLNVLSGLVKPDSGRVLVDGEpletytdsswydTIGYISQNPYLFAGTVa 427
Cdd:cd03222 11 GVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQYIDLSGGEL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048238220 428 dnialgetadeikileaanaaglndviaqlpngihtelgeggyglsggerQRLALARAFLKRPGIILFDEPTTGLDLVTE 507
Cdd:cd03222 78 --------------------------------------------------QRVAIAAALLRNATFYLFDEPSAYLDIEQR 107
|
170 180
....*....|....*....|....*
gi 2048238220 508 QIVRRSIEELSREA--TLVTVAHRL 530
Cdd:cd03222 108 LNAARAIRRLSEEGkkTALVVEHDL 132
|
|
| |
