|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-566 |
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: 522.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 5 KTVMKAWTRAQSRLGRRQAMPVVLLGLAISAIAVGQVWCIATALACVLVPGGMPV-VAWPLAGLVGLAVARAGLQAASDT 83
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSaLLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 84 LAARAGMKGRARLRGGVIEAIMRGGPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLAAFVQPGS 163
Cdd:COG4988 81 AAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 164 ALIMAVCGIAVPFGQALFGIGAAVASRNQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRV 243
Cdd:COG4988 161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 244 AFLSSASIDCAMVVALVLVALRNGAHLMDlheqgvpaaimaGQV--ARGLFVVLVVPEFFAPFRSLALAYQDRAHASGAA 321
Cdd:COG4988 241 AFLSSAVLEFFASLSIALVAVYIGFRLLG------------GSLtlFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 322 SAM-RILPDATPVRVGGQAVCDMTGGVAVAFEHVSFAWDiARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFI 400
Cdd:COG4988 309 EKIfALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 401 QPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFI 480
Cdd:COG4988 388 PPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 481 GEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGAVTGFEGQRIDLAQG 560
Cdd:COG4988 468 GEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDG 547
|
....*.
gi 1154151804 561 HVVTSG 566
Cdd:COG4988 548 RIVEQG 553
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-544 |
1.86e-122 |
|
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: 370.85 E-value: 1.86e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 20 RRQAMPVVLLGLAISAIAVGQVWCIATALACVLVPG-GMPVVAWPLAGLVGLAVARAGLQAASDTLAARAGMKGRARLRG 98
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAWLLARVVDGLISAGePLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 99 GVIEAIMRGGPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLAAFVQPGSALIMAVCGIAVPFGQ 178
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 179 ALFGIGAAVASRNQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLSSASIDCAMVVA 258
Cdd:TIGR02857 162 ILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 259 LVLVALRNGAHLMdlheqgvpaaimAGQV--ARGLFVVLVVPEFFAPFRSLALAYQDRAHASGAASAMRILPDATPVRVG 336
Cdd:TIGR02857 242 VALVAVYIGFRLL------------AGDLdlATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 337 GQAVCDMTGGVAVAFEHVSFAWDiARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTT 416
Cdd:TIGR02857 310 GKAPVTAAPASSLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 417 LAPEALVAMTSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVA 496
Cdd:TIGR02857 389 ADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLA 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1154151804 497 IARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHS 544
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHR 516
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-543 |
7.93e-105 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 327.19 E-value: 7.93e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 4 DKTVMK---AWTRAQSRLGRRQAMPVVLLGLAISAIAVGQVWCIATALACVLVpGGMPVVA--WPLAGLVGLAVARAGLQ 78
Cdd:PRK11174 2 DKSRQKeltRWLKQQSKPAKRWLNLSILLGFLSGLLLIAQAWLLATILQALII-ENIPREAllPPFILLILLFVLRALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 79 AASDTLAARAGMKGRARLRGGVIEAIMRGGPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIgVLAAF 158
Cdd:PRK11174 81 WLRERVGFKAGQHIRQQIRQQVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLI-LIAVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 159 -VQPGSALIMAVCGIAVPFGQALFGIGAAVASRNQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRT 237
Cdd:PRK11174 160 pINWAAGLILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 238 MKVLRVAFLSSASIDCAMVVALVLVALRNG-AHLMDLH--EQGVPAAIMAGqvargLFVVLVVPEFFAPFRSLALAYQDR 314
Cdd:PRK11174 240 MEVLRMAFLSSAVLEFFASISIALVAVYFGfSYLGELNfgHYGTGVTLFAG-----FFVLILAPEFYQPLRDLGTFYHAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 315 AHASGAASA-MRILP-DATPVRVGGQAVCDMTGGVAVAFEHVSFAWDIARgmAVDDVSFSVPAGQTLLLCGASGSGKSTI 392
Cdd:PRK11174 315 AQAVGAAESlVTFLEtPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKT--LAGPLNFTLPAGQRIALVGPSGAGKTSL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 393 IELLLGFIqPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASL 472
Cdd:PRK11174 393 LNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLL 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 473 PQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:PRK11174 472 PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTH 542
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-543 |
1.31e-91 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 292.84 E-value: 1.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 20 RRQAMPVVLLGLAISAIAVGQVWCIATALACVLVPGGMPVVAWPLAGLVGLAVARAGLQAASDTLAARAGMKGRARLRGG 99
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 100 VIEAIMRGGPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLAAFVQPGSALIMAVCGIAVPFGQA 179
Cdd:COG1132 100 LFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 180 LFGIGAAVASRNQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLSSASIDCAMVVAL 259
Cdd:COG1132 180 LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 260 VLVALRnGAHLmdlheqgvpaaIMAGQVARGLFVVLV--VPEFFAPFRSLALAYQDRAHASGAASAMRILPDATP-VRVG 336
Cdd:COG1132 260 ALVLLV-GGLL-----------VLSGSLTVGDLVAFIlyLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPeIPDP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 337 GQAVCDMTGGVAVAFEHVSFAWDIARgMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTT 416
Cdd:COG1132 328 PGAVPLPPVRGEIEFENVSFSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 417 LAPEALVAMTSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVA 496
Cdd:COG1132 407 LTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIA 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1154151804 497 IARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
94-566 |
4.49e-89 |
|
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: 285.89 E-value: 4.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 94 ARLRGGVIEAIMRGGPGLLRQHHTGELTALAVDRIEALDGFFARWL-PASVLWVAAPLVIGVLAAFVqPGSALIMAVC-- 170
Cdd:COG4987 88 ADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLlPLLVALLVILAAVAFLAFFS-PALALVLALGll 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 171 --GIAVPfgqALFGIGAAVASRNQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLSS 248
Cdd:COG4987 167 laGLLLP---LLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 249 ASIDCAMVVALVLVALRnGAHLMDLHEQGVPAAIMAgqvargLFVVLVVPEFFAPfrsLALAYQDRAHASGAASAMRILP 328
Cdd:COG4987 244 ALLQLAAGLAVVAVLWL-AAPLVAAGALSGPLLALL------VLAALALFEALAP---LPAAAQHLGRVRAAARRLNELL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 329 DATPVRVGGQAVCDMTGGVAVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIM 408
Cdd:COG4987 314 DAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 409 FNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLS 488
Cdd:COG4987 394 LGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLS 473
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154151804 489 GGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGAVTGFEGQRIDLAQGHVVTSG 566
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
26-324 |
7.48e-82 |
|
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: 257.72 E-value: 7.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 26 VVLLGLAISAIAVGQVWCIATALACVLVPG-GMPVVAWPLAGLVGLAVARAGLQAASDTLAARAGMKGRARLRGGVIEAI 104
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGaGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 105 MRGGPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLAAFVQPGSALIMAVCGIAVPFGQALFGIG 184
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 185 AAVASRNQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLSSASIDCAMVVALVLVAL 264
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154151804 265 RNGAHLMDlheqgvpaaimaGQV--ARGLFVVLVVPEFFAPFRSLALAYQDRAHASGAASAM 324
Cdd:cd18584 241 YIGFRLLG------------GSLtlFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-566 |
5.65e-67 |
|
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: 230.49 E-value: 5.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 20 RRQAMPVVLLGLAISAIAvgqvwcIATALA------CVLVPGGMPVVaWPLA-GLVGLAVARAGLQAASDTLAARAGMKG 92
Cdd:COG2274 155 RRLLLQVLLASLLINLLA------LATPLFtqvvidRVLPNQDLSTL-WVLAiGLLLALLFEGLLRLLRSYLLLRLGQRI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 93 RARLRGGVIEAIMRGGPGLLRQHHTGELTALAVDrIEALDGFFARWLPASVLwvAAPLVIGVLA--AFVQPGSALIMAVC 170
Cdd:COG2274 228 DLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALL--DLLFVLIFLIvlFFYSPPLALVVLLL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 171 GIAVPFGQALFGIGAAVASRNQFLAMTRLQARFLDRVRGIATIVLSGRTED---ETRRLAASAEELRLRTMKVLRVAFLS 247
Cdd:COG2274 305 IPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRfrrRWENLLAKYLNARFKLRRLSNLLSTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 248 SASIDCAMVVALVLValrnGAHLmdlheqgvpaaIMAGQVARGLFV--VLVVPEFFAPFRSLALAYQDRAHAsgAASAMR 325
Cdd:COG2274 385 SGLLQQLATVALLWL----GAYL-----------VIDGQLTLGQLIafNILSGRFLAPVAQLIGLLQRFQDA--KIALER 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 326 I-----LPDATPVRVGGQAVCDMTGgvAVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFI 400
Cdd:COG2274 448 LddildLPPEREEGRSKLSLPRLKG--DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 401 QPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFI 480
Cdd:COG2274 526 EPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVV 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 481 GEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGAVTGFEGQRIDLAQG 560
Cdd:COG2274 606 GEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKG 685
|
....*.
gi 1154151804 561 HVVTSG 566
Cdd:COG2274 686 RIVEDG 691
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
349-543 |
1.55e-56 |
|
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: 187.59 E-value: 1.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW 428
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKPVLFAGTLRENIlfarpdatqeqlgaavaaaaagdfvasLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLV 508
Cdd:cd03228 81 VPQDPFLFSGTIRENI---------------------------LSGG---------------QRQRIAIARALLRDPPIL 118
|
170 180 190
....*....|....*....|....*....|....*
gi 1154151804 509 VLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAH 153
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-544 |
2.18e-54 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 192.58 E-value: 2.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 13 RAQSRLGRRQAMPVVLLGLAI-SAIAVGQV--WCIATAlacVLVPGGMPVVAwPLAGLVGLAVARAGLQAASDTLAARAG 89
Cdd:TIGR02868 6 PLLKPRRRRLALAVLLGALALgSAVALLGVsaWLISRA---AEMPPVLYLSV-AAVAVRAFGIGRAVFRYLERLVGHDAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 90 MKGRARLRGGVIEAIMRGGPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLAAFVQPGSALIMAV 169
Cdd:TIGR02868 82 LRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 170 C-GIAVPFGQALFGIGAAVASRNQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLSS 248
Cdd:TIGR02868 162 GlLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 249 ASIDCAMVVALVLVALRNGAHLMDLHEQGVPAAImagqvarglfVVLVVPEFFAPFRSLALAYQDRAHASGAASAMRILP 328
Cdd:TIGR02868 242 ALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAV----------LVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 329 DATPVRVGGQAVCDMT---GGVAVAFEHVSFAWDIARgMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASG 405
Cdd:TIGR02868 312 DAAGPVAEGSAPAAGAvglGKPTLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 406 RIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGF 485
Cdd:TIGR02868 391 EVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGA 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154151804 486 GLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHS 544
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
349-543 |
2.28e-51 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 176.27 E-value: 2.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARgMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW 428
Cdd:cd03253 1 IEFENVTFAYDPGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLV 508
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1154151804 509 VLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAH 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
349-543 |
4.46e-51 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 175.11 E-value: 4.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW 428
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLV 508
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1154151804 509 VLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
349-543 |
4.37e-50 |
|
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: 172.72 E-value: 4.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAV-DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTS 427
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPIlKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 WIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPL 507
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 508 VVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
349-566 |
3.58e-49 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 170.10 E-value: 3.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARgMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW 428
Cdd:cd03254 3 IEFENVNFSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLV 508
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154151804 509 VLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGAVTGFEGQRIDLAQGHVVTSG 566
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEG 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
348-543 |
2.14e-48 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 167.77 E-value: 2.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTS 427
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 WIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPL 507
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 508 VVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITH 197
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
328-543 |
3.49e-47 |
|
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: 174.24 E-value: 3.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 328 PDATPVRVGGqavcdmtggVAVAFEHVSFAWDIARGMaVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRI 407
Cdd:COG5265 346 PDAPPLVVGG---------GEVRFENVSFGYDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 408 MFNGVDMTTLAPEALVAMtswIG---QKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGG 484
Cdd:COG5265 416 LIDGQDIRDVTQASLRAA---IGivpQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERG 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154151804 485 FGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:COG5265 493 LKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAH 551
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
26-324 |
2.18e-44 |
|
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: 158.98 E-value: 2.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 26 VVLLGLAISAIAVGQVWCIATALACVLVPGGMPVVAWPLAGLVGLAVARAGLQAASDTLAARAGMKGRARLRGGVIEAIM 105
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 106 RGGPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLAAFVQPGSALIMAVCGIAVPFGQALFGIGA 185
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 186 AVASRNQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLSSASIDCAMVVALVLVALR 265
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 266 NGAHLmdlheqgvpaaiMAGQVA--RGLFVVLVVPEFFAPFRSLALAYQDRAHASGAASAM 324
Cdd:cd18561 241 GALRV------------LGGQLTlsSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
348-568 |
7.73e-42 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 160.03 E-value: 7.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTS 427
Cdd:TIGR03375 463 EIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 WIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPL 507
Cdd:TIGR03375 543 YVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPI 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 508 VVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGAVTGFEGQRIDLAQGHVVTSGEK 568
Cdd:TIGR03375 623 LLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPK 683
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
30-566 |
2.93e-40 |
|
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: 154.10 E-value: 2.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 30 GLAISAIAVGQVWCIATALACVLVP-------GGMPVVAWPL-AGLVGLAVARAGLQAASDTLAARAGMKGRARLRGGVI 101
Cdd:TIGR02203 15 GLVLAGVAMILVAATESTLAALLKPllddgfgGRDRSVLWWVpLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 102 EAIMRGGPGLLRQHHTGEL-----------TALAVDRIEAL--DGFFARWLPASVLWVAAPLVIGVLAAFvqPGSALIMA 168
Cdd:TIGR02203 95 EKLLGLPVSFFDRQPTGTLlsritfdseqvASAATDAFIVLvrETLTVIGLFIVLLYYSWQLTLIVVVML--PVLSILMR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 169 VcgiavpFGQALFGIgaavaSRNQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLSS 248
Cdd:TIGR02203 173 R------VSKRLRRI-----SKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 249 ASIDCAMVVALVLVALrngahlMDLHEQGvpaaimAGQVARGLFVVLVVP--EFFAPFRSLA-LAYQDRAHASGAASAMR 325
Cdd:TIGR02203 242 PITQLIASLALAVVLF------IALFQAQ------AGSLTAGDFTAFITAmiALIRPLKSLTnVNAPMQRGLAAAESLFT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 326 ILPDATPVRVGGQAVCDMTGgvAVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASG 405
Cdd:TIGR02203 310 LLDSPPEKDTGTRAIERARG--DVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 406 RIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENILFARP-DATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGG 484
Cdd:TIGR02203 388 QILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 485 FGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGAVTGFEGQRIDLAQGHVVT 564
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
..
gi 1154151804 565 SG 566
Cdd:TIGR02203 548 RG 549
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
348-566 |
1.54e-38 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 149.34 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAWDiARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTS 427
Cdd:PRK13657 334 AVEFDDVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 WIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPL 507
Cdd:PRK13657 413 VVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 508 VVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGAvTGFEGQRI-DLAQGHVVTSG 566
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLS-TVRNADRIlVFDNGRVVESG 551
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
146-566 |
6.80e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 147.28 E-value: 6.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 146 VAAPLVIGVLA---AFVQPGSALIMavCGIAV---------------PFGQALfgigaaVASRNQFlamtRLQarFLDRV 207
Cdd:PRK11160 142 VAALVVILVLTiglSFFDLTLALTL--GGILLllllllpllfyrlgkKPGQDL------THLRAQY----RVQ--LTEWL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 208 RGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLSSASIDCAMVVALVLVaLRNGAHLMDLHEQgvPAAIMAgqv 287
Cdd:PRK11160 208 QGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLM-LWLAAGGVGGNAQ--PGALIA--- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 288 argLFV--VLVVPEFFAPfrsLALAYQdraHASGA-ASAMRI--LPDATP-VRVGGQAVcDMTGGVAVAFEHVSFAWDIA 361
Cdd:PRK11160 282 ---LFVfaALAAFEALMP---VAGAFQ---HLGQViASARRIneITEQKPeVTFPTTST-AAADQVSLTLNNVSFTYPDQ 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 362 RGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLR 441
Cdd:PRK11160 352 PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLR 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 442 ENILFARPDATQEQLGAAVAAAAAGDFVASlPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDT 521
Cdd:PRK11160 432 DNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1154151804 522 EADVFESLRRLAARRTVILATHSgaVTGFEgqRID----LAQGHVVTSG 566
Cdd:PRK11160 511 ERQILELLAEHAQNKTVLMITHR--LTGLE--QFDricvMDNGQIIEQG 555
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
349-566 |
1.64e-37 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 138.77 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW 428
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLV 508
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154151804 509 VLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGAVTGFEGQRIDLAQGHVVTSG 566
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQG 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
94-543 |
2.69e-37 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 147.18 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 94 ARLRGGVIEAIMRGGPGLLRQHHTGELTAlavdRIEALDGFFARWLP--ASVLWVAAPLVIGVLAaFVQPGSALIMAVCG 171
Cdd:TIGR00958 234 LRIREDLFRSLLRQDLGFFDENKTGELTS----RLSSDTQTMSRSLSlnVNVLLRNLVMLLGLLG-FMLWLSPRLTMVTL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 172 IAVPFgqaLFGIGAAVASRNQFLAmTRLQ---ARFLDRVR----GIATIVLSGRTEDETRRLAASAEELR-LRTMKVLRV 243
Cdd:TIGR00958 309 INLPL---VFLAEKVFGKRYQLLS-EELQeavAKANQVAEealsGMRTVRSFAAEEGEASRFKEALEETLqLNKRKALAY 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 244 AFLSSASIDCAMVVaLVLVaLRNGAHLmdlheqgvpaaIMAGQVARGLFV--VLVVPEFFAPFRSLALAYQDRAHASGAA 321
Cdd:TIGR00958 385 AGYLWTTSVLGMLI-QVLV-LYYGGQL-----------VLTGKVSSGNLVsfLLYQEQLGEAVRVLSYVYSGMMQAVGAS 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 322 SAMRILPDATPV--RVGGQAVCDMTGgvAVAFEHVSFAWDIARGMAV-DDVSFSVPAGQTLLLCGASGSGKSTIIELLLG 398
Cdd:TIGR00958 452 EKVFEYLDRKPNipLTGTLAPLNLEG--LIEFQDVSFSYPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 399 FIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDT 478
Cdd:TIGR00958 530 LYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDT 609
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154151804 479 FIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESlrRLAARRTVILATH 543
Cdd:TIGR00958 610 EVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAH 672
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
365-543 |
2.55e-35 |
|
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: 132.23 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENI 444
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 445 lfarpD----ATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPD 520
Cdd:cd03244 99 -----DpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
170 180
....*....|....*....|...
gi 1154151804 521 TEADVFESLRRLAARRTVILATH 543
Cdd:cd03244 174 TDALIQKTIREAFKDCTVLTIAH 196
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
351-562 |
1.13e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.94 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 351 FEHVSFAWDIARGmaVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG 430
Cdd:COG4619 3 LEGLSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 431 QKPVLFAGTLRENilFARPDATQEQLGAAVAAAaagDFVASLpqGLDTFIGEGGFGLSGG-QAQRVAIARAFLKDAPLVV 509
Cdd:COG4619 81 QEPALWGGTVRDN--LPFPFQLRERKFDRERAL---ELLERL--GLPPDILDKPVERLSGgERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154151804 510 LDEPTAHLDPDTEADVFESLRRLAAR--RTVILATHSGA-VTGFEGQRIDLAQGHV 562
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
351-567 |
1.61e-34 |
|
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: 138.72 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 351 FEHVSFAWDIARGmAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG 430
Cdd:TIGR01193 476 INDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 431 QKPVLFAGTLRENILF-ARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVV 509
Cdd:TIGR01193 555 QEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLI 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154151804 510 LDEPTAHLDPDTEADVFESLRRLaARRTVILATHSGAVTGFEGQRIDLAQGHVVTSGE 567
Cdd:TIGR01193 635 LDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGS 691
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
349-543 |
1.48e-33 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 127.59 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAV-DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTS 427
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 WIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPL 507
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 508 VVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAH 207
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
349-543 |
1.89e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 134.76 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW 428
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKPVLFAGTLRENILFARPDA-TQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPL 507
Cdd:PRK11176 422 VSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 508 VVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:PRK11176 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
365-543 |
1.22e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 125.18 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALvAMTSWIGQKPVLFAG-TLREN 443
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIGYVPQEPALYPDlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 ILF-------------ARPDATQEQLGAAVAAaaaGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVL 510
Cdd:COG1131 94 LRFfarlyglprkearERIDELLELFGLTDAA---DRKVGTLSGG---------------MKQRLGLALALLHDPELLIL 155
|
170 180 190
....*....|....*....|....*....|....
gi 1154151804 511 DEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEgKTVLLSTH 189
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
362-543 |
5.74e-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: 121.35 E-value: 5.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 362 RGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTlAPEALVAMTSWIGQKPVLFAG-TL 440
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENIlfarpdatqeqlgaavaaaaagdfvaSLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPD 520
Cdd:cd03230 91 RENL--------------------------KLSGG---------------MKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180
....*....|....*....|....
gi 1154151804 521 TEADVFESLRRLAAR-RTVILATH 543
Cdd:cd03230 130 SRREFWELLRELKKEgKTILLSSH 153
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
307-567 |
5.82e-32 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 130.22 E-value: 5.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 307 LALAYQDRAHASGAASAMRI---LPDATPVRVGGQAVCDMTGGVAVAFEHvsFAWDIARGMAVDDVSFSVPAGQTLLLCG 383
Cdd:PRK10789 271 LALAWMFNIVERGSAAYSRIramLAEAPVVKDGSEPVPEGRGELDVNIRQ--FTYPQTDHPALENVNFTLKPGQMLGICG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 384 ASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAA 463
Cdd:PRK10789 349 PTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLA 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 464 AAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:PRK10789 429 SVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
250 260
....*....|....*....|....
gi 1154151804 544 SGAVTGFEGQRIDLAQGHVVTSGE 567
Cdd:PRK10789 509 RLSALTEASEILVMQHGHIAQRGN 532
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
365-563 |
3.43e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 120.92 E-value: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAM----TSWIGQKPVLFAG-T 439
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLrrrhIGFVFQFFNLLPElT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 LRENILF-----------ARPDATQ--EQLGAavaaaaaGDFVASLPQ----GldtfigeggfglsggQAQRVAIARAFL 502
Cdd:COG1136 103 ALENVALplllagvsrkeRRERAREllERVGL-------GDRLDHRPSqlsgG---------------QQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 503 KDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR--RTVILATHSGAVTGFEGQRIDLAQGHVV 563
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
349-543 |
4.52e-31 |
|
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: 118.95 E-value: 4.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLApEALVAMTSW 428
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKPVLFAGTLRENIlfARPDATQEQlgaavaaaaagdfvaslpqgldtfigeggfglsggqaQRVAIARAFLKDAPLV 508
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--GRRFSGGER-------------------------------------QRLALARILLQDAPIV 120
|
170 180 190
....*....|....*....|....*....|....*
gi 1154151804 509 VLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITH 155
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
349-543 |
6.72e-31 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 126.79 E-value: 6.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALvamTSW 428
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL---GRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IG---QKPVLFAGTLRENIlfAR-PDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKD 504
Cdd:COG4618 408 IGylpQDVELFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154151804 505 APLVVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITH 525
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
351-543 |
4.96e-30 |
|
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: 115.42 E-value: 4.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 351 FEHVSFAwdIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG 430
Cdd:cd00267 2 IENLSFR--YGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 431 QkpvlfagtlrenilfarpdatqeqlgaavaaaaagdfvasLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVL 510
Cdd:cd00267 80 Q----------------------------------------LSGG---------------QRQRVALARALLLNPDLLLL 104
|
170 180 190
....*....|....*....|....*....|....
gi 1154151804 511 DEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTH 138
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
352-543 |
9.21e-30 |
|
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: 115.01 E-value: 9.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 352 EHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQ 431
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 432 KPVLFAGTLRENILfarpdatqeqlgaavaaaaagdfvaslpqgldtfigeggfglSGGQAQRVAIARAFLKDAPLVVLD 511
Cdd:cd03246 84 DDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190
....*....|....*....|....*....|...
gi 1154151804 512 EPTAHLDPDTEADVFESLRRL-AARRTVILATH 543
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAH 154
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
349-544 |
2.09e-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: 115.26 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWD---IARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdmttlaPEALVAM 425
Cdd:cd03250 1 ISVEDASFTWDsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------SIAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 426 TSWIgqkpvlFAGTLRENILFARP----------DATQEQLgaavaaaaagDFvASLPQGLDTFIGEGGFGLSGGQAQRV 495
Cdd:cd03250 74 EPWI------QNGTIRENILFGKPfdeeryekviKACALEP----------DL-EILPDGDLTEIGEKGINLSGGQKQRI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 496 AIARAFLKDAPLVVLDEPTAHLDPDTEADVFES--LRRLAARRTVILATHS 544
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQ 187
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
349-549 |
7.05e-29 |
|
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: 120.53 E-value: 7.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW 428
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLV 508
Cdd:TIGR01842 397 LPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154151804 509 VLDEPTAHLDPDTEADVFESLRRLAARR-TVILATHSGAVTG 549
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLG 518
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
351-543 |
8.78e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 113.72 E-value: 8.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 351 FEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG 430
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 431 QKP--VLFAGTLRENILFArpdatQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLV 508
Cdd:cd03225 82 QNPddQFFGPTVEEEVAFG-----LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 509 VLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTH 192
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
349-562 |
7.89e-28 |
|
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: 111.04 E-value: 7.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGM--AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAM- 425
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 426 ---TSWIGQK----PVLfagTLRENILF-----------ARPDATQ--EQLGAAVAAaaaGDFVASLPQGldtfigeggf 485
Cdd:cd03255 81 rrhIGFVFQSfnllPDL---TALENVELplllagvpkkeRRERAEEllERVGLGDRL---NHYPSELSGG---------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154151804 486 glsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLA--ARRTVILATHSGAVTGFEGQRIDLAQGHV 562
Cdd:cd03255 145 -----QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
365-543 |
1.20e-27 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 111.06 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMT---SWIGQK------PVL 435
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRkeiQMVFQDpmsslnPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 436 FAGT-LRENILFARPDATQEQLGAAVAAAAAG-----DFVASLPQGLdtfigeggfglSGGQAQRVAIARAFLKDAPLVV 509
Cdd:cd03257 100 TIGEqIAEPLRIHGKLSKKEARKEAVLLLLVGvglpeEVLNRYPHEL-----------SGGQRQRVAIARALALNPKLLI 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 510 LDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLLKKLQEELglTLLFITH 204
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
349-568 |
1.44e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.53 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARgMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW 428
Cdd:COG2884 2 IRFENVSKRYPGGR-EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGqkpVLFAG-------TLRENILFA-------------RPDATQEQLGAavaaaaaGDFVASLPQ----Gldtfigegg 484
Cdd:COG2884 81 IG---VVFQDfrllpdrTVYENVALPlrvtgksrkeirrRVREVLDLVGL-------SDKAKALPHelsgG--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 485 fglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR-TVILATH-SGAVTGFEGQRIDLAQGHV 562
Cdd:COG2884 142 ------EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGtTVLIATHdLELVDRMPKRVLELEDGRL 215
|
....*.
gi 1154151804 563 VTSGEK 568
Cdd:COG2884 216 VRDEAR 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
366-515 |
2.12e-27 |
|
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: 107.73 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAG-TLRENI 444
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 445 LFARPDATqeqLGAAVAAAAAGDFVASLPQG--LDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTA 515
Cdd:pfam00005 81 RLGLLLKG---LSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
367-543 |
6.17e-27 |
|
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: 108.34 E-value: 6.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTlAPEALVAMTSWIGQKPVLFAG-TLRENIL 445
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 446 FArpdatQEQLGAAVAAAAAGDFVASLpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADV 525
Cdd:COG4133 98 FW-----AALYGLRADREAIDEALEAV--GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170
....*....|....*....
gi 1154151804 526 FESLRR-LAARRTVILATH 543
Cdd:COG4133 171 AELIAAhLARGGAVLLTTH 189
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
343-543 |
2.33e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.87 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 343 MTGGVAVAFEHVSFAWDiaRGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP--- 419
Cdd:COG1121 1 MMMMPAIELENLTVSYG--GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRrig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 420 ----------------EALVAMtswigqkpvlfaGTLRENILFARPDATQ--------EQLGAavaaaaaGDF----VAS 471
Cdd:COG1121 79 yvpqraevdwdfpitvRDVVLM------------GRYGRRGLFRRPSRADreavdealERVGL-------EDLadrpIGE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 472 LPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:COG1121 140 LSGG---------------QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTH 197
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
365-544 |
2.50e-26 |
|
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: 106.83 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAL-VAMtswIGQKPVLFAG-TLRE 442
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRnIGM---VFQDYALFPHlTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 NILFA------RPDATQEQLGAAVAAAAAGDFVASLPQGLDTfigeggfglsgGQAQRVAIARAFLKDAPLVVLDEPTAH 516
Cdd:cd03259 92 NIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPHELSG-----------GQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190
....*....|....*....|....*....|
gi 1154151804 517 LDPDTEADVFESLRRL--AARRTVILATHS 544
Cdd:cd03259 161 LDAKLREELREELKELqrELGITTIYVTHD 190
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
370-544 |
6.74e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.99 E-value: 6.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 370 SFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPealvamtswiGQKPV--------LFAG-TL 440
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----------AERPVsmlfqennLFPHlTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFA-----RPDATQ-EQLGAAVAAAAAGDFVASLPQGLdtfigeggfglSGGQAQRVAIARAFLKDAPLVVLDEPT 514
Cdd:COG3840 89 AQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|..
gi 1154151804 515 AHLDPDTEADVFESLRRLAARR--TVILATHS 544
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRERglTVLMVTHD 189
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
351-544 |
2.62e-25 |
|
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: 102.65 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 351 FEHVSfaWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW-- 428
Cdd:cd03229 3 LKNVS--KRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKPVLFAG-TLRENILFArpdatqeqlgaavaaaaagdfvasLPQGldtfigeggfglsggQAQRVAIARAFLKDAPL 507
Cdd:cd03229 81 VFQDFALFPHlTVLENIALG------------------------LSGG---------------QQQRVALARALAMDPDV 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154151804 508 VVLDEPTAHLDPDTEADVFESLRRLAAR--RTVILATHS 544
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHD 160
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
349-543 |
1.12e-24 |
|
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: 102.41 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARgMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAL---VAM 425
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 426 tswIGQKPV--LFAGTLRENILF-------------ARPDATQEQLGAAvaaaaagDF----VASLPQGldtfigeggfg 486
Cdd:COG1122 80 ---VFQNPDdqLFAPTVEEDVAFgpenlglpreeirERVEEALELVGLE-------HLadrpPHELSGG----------- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154151804 487 lsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:COG1122 139 ----QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTH 192
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
348-543 |
1.37e-24 |
|
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: 102.81 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAWDiaRGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTS 427
Cdd:COG1120 1 MLEAENLSVGYG--GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 WIGQKPVL-FAGTLRENILFAR-P-------------DATQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQA 492
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyPhlglfgrpsaedrEAVEEALERTGLEHLADRPVDELSGG---------------ER 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 493 QRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR--RTVILATH 543
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLH 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
348-566 |
1.84e-24 |
|
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: 106.91 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPA---SGRIMFNGVDMTTLAPEALVA 424
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 425 MTSWIGQKP--VLFAGTLRENILFARpdatqeQLGAAVAAAAAGDFVASLPQ-GLDTFIGEGGFGLSGGQAQRVAIARAF 501
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAL------ENLGLSRAEARARVLELLEAvGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154151804 502 LKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATHSGAVTGFEGQRID-LAQGHVVTSG 566
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVvMDDGRIVEDG 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
352-543 |
2.43e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 100.20 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 352 EHVSFAWDiaRGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALvamtswigq 431
Cdd:cd03214 3 ENLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 432 kpvlfagtlrenilfARpdatqeqlgaavaaaaagdFVASLPQ-----GLDTFIGEGGFGLSGGQAQRVAIARAFLKDAP 506
Cdd:cd03214 72 ---------------AR-------------------KIAYVPQalellGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154151804 507 LVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLH 156
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
365-543 |
7.36e-24 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 99.79 E-value: 7.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG----QKPVLFAGTL 440
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGvvfqDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFA------RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEPT 514
Cdd:cd03292 96 YENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRALPAELS-----------GGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190
....*....|....*....|....*....|
gi 1154151804 515 AHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKAgTTVVVATH 194
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
365-543 |
1.65e-23 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 98.64 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENi 444
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 445 LFARPDATQEQLGAAVAAAAAGDfvaSLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEAD 524
Cdd:cd03369 102 LDPFDEYSDEEIYGALRVSEGGL---NLSQG---------------QRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170
....*....|....*....
gi 1154151804 525 VFESLRRLAARRTVILATH 543
Cdd:cd03369 164 IQKTIREEFTNSTILTIAH 182
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
343-544 |
1.93e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 99.78 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 343 MTG-GVAVAFEHVSFAWDIARG--MAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP 419
Cdd:COG1116 1 MSAaAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 420 EalVAMtswIGQKPVLFA-GTLRENILFA-------RPDATQ------EQLGAavaaaaaGDFVASLPQ----Gldtfig 481
Cdd:COG1116 81 D--RGV---VFQEPALLPwLTVLDNVALGlelrgvpKAERRErarellELVGL-------AGFEDAYPHqlsgG------ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154151804 482 eggfglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAA--RRTVILATHS 544
Cdd:COG1116 143 ---------MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHD 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
365-566 |
3.63e-23 |
|
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: 97.96 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALvAMTSWIGQKPVLFAG-TLREN 443
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-QSLGYCPQFDALFDElTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 I-LFAR----PDATQEQLGAAVAAAAagdfvaSLPQGLDTFIgeggFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLD 518
Cdd:cd03263 96 LrFYARlkglPKSEIKEEVELLLRVL------GLTDKANKRA----RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154151804 519 PDTEADVFESLRRLAARRTVILATHSGAVTGFEGQRID-LAQGHVVTSG 566
Cdd:cd03263 166 PASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAiMSDGKLRCIG 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
349-544 |
4.17e-23 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 97.93 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARG--MAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMt 426
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 427 swigQKPVLFA-GTLRENILF-------------ARPDATQEQLGaavaaaaAGDFVASLPQGLdtfigeggfglSGGQA 492
Cdd:cd03293 80 ----QQDALLPwLTVLDNVALglelqgvpkaearERAEELLELVG-------LSGFENAYPHQL-----------SGGMR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154151804 493 QRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRL--AARRTVILATHS 544
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHD 191
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
344-543 |
4.37e-23 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 98.13 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 344 TGGVAVAFEHVSFAWDiarGMAV-DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAL 422
Cdd:COG1127 1 MSEPMIEVRNLTKSFG---DRVVlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 423 VAMTSWIGqkpVLFAG-------TLRENILF------------ARpDATQEQLGAAVAAAAAGDFVASLPQGldtfigeg 483
Cdd:COG1127 78 YELRRRIG---MLFQGgalfdslTVFENVAFplrehtdlseaeIR-ELVLEKLELVGLPGAADKMPSELSGG-------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 484 gfglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTeADVFESL-RRLAARR--TVILATH 543
Cdd:COG1127 146 -------MRKRVALARALALDPEILLYDEPTAGLDPIT-SAVIDELiRELRDELglTSVVVTH 200
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
344-543 |
4.98e-23 |
|
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: 102.67 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 344 TGGVAVAFEHVSFAWDIARG---MAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPE 420
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 421 ALVAMTSWIG---QKPV--LFAG-TLRENILF-----------ARPDATQEQLGAAVAAAAAGD-FVASLPQGldtfige 482
Cdd:COG1123 336 SLRELRRRVQmvfQDPYssLNPRmTVGDIIAEplrlhgllsraERRERVAELLERVGLPPDLADrYPHELSGG------- 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 483 ggfglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:COG1123 409 --------QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISH 463
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
349-543 |
1.15e-22 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 96.16 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWdiARGM-AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTS 427
Cdd:TIGR02673 2 IEFHNVSKAY--PGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 WIGqkpVLF-------AGTLRENILFA------RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQR 494
Cdd:TIGR02673 80 RIG---VVFqdfrllpDRTVYENVALPlevrgkKEREIQRRVGAALRQVGLEHKADAFPEQLS-----------GGEQQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154151804 495 VAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:TIGR02673 146 VAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRgTTVIVATH 195
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
353-563 |
1.75e-22 |
|
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: 96.80 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 353 HVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAL---VAMtswI 429
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFrrrVQM---V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 430 GQKPVL-------FAGTLRENILFARPDATQEQLGAAVAAAAAGD-----FVASLPQGldtfigeggfglsggQAQRVAI 497
Cdd:COG1124 85 FQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGLPPsfldrYPHQLSGG---------------QRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154151804 498 ARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATHSGAVTGFEGQRI-DLAQGHVV 563
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVaVMQNGRIV 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
365-543 |
3.55e-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: 94.59 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLApEALVAMTSWIgQKPVLFAG-TLREN 443
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALI-EAPGFYPNlTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 I-----LFARPDATQEQ-LGAAVAAAAAGDFVASLPQGLdtfigeggfglsggqAQRVAIARAFLKDAPLVVLDEPTAHL 517
Cdd:cd03268 93 LrllarLLGIRKKRIDEvLDVVGLKDSAKKKVKGFSLGM---------------KQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180
....*....|....*....|....*..
gi 1154151804 518 DPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:cd03268 158 DPDGIKELRELILSLRDQgITVLISSH 184
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
366-544 |
3.63e-22 |
|
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: 95.48 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAlvAMTSWIGQKPVLFAG-TLRENI 444
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 445 LFARPDATQEQLGAAVAAAAAGDFVaslpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEAD 524
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180
....*....|....*....|....
gi 1154151804 525 VFESLRRlaARR----TVILATHS 544
Cdd:cd03299 168 LREELKK--IRKefgvTVLHVTHD 189
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
351-566 |
4.07e-22 |
|
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: 94.52 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 351 FEHVSFAWDiaRGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMT--------------- 415
Cdd:cd03235 2 VEDLTVSYG--GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEkerkrigyvpqrrsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 416 -TLAP---EALVAMTSWigQKPVLFAGTLRENilFARPDATQEQLGAavaaaaaGDF----VASLPQGldtfigeggfgl 487
Cdd:cd03235 80 dRDFPisvRDVVLMGLY--GHKGLFRRLSKAD--KAKVDEALERVGL-------SELadrqIGELSGG------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 488 sggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATHS-GAVTGFeGQRIDLAQGHVVTS 565
Cdd:cd03235 137 ---QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDlGLVLEY-FDRVLLLNRTVVAS 212
|
.
gi 1154151804 566 G 566
Cdd:cd03235 213 G 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
365-563 |
4.33e-22 |
|
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: 95.33 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGqkpVLFAG------ 438
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIG---MIFQQfnlier 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 439 -TLRENILFARpdatqeqLGAAVaaaaagdFVASLPQ-----------------GLDTFIGEGGFGLSGGQAQRVAIARA 500
Cdd:cd03256 93 lSVLENVLSGR-------LGRRS-------TWRSLFGlfpkeekqralaalervGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 501 FLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATHS-GAVTGFeGQRI-DLAQGHVV 563
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQvDLAREY-ADRIvGLKDGRIV 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
370-544 |
5.02e-22 |
|
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: 94.54 E-value: 5.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 370 SFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP-EALVAMtswIGQKPVLFAG-TLRENI-LF 446
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPyQRPVSM---LFQENNLFAHlTVRQNIgLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 447 ARPD-----ATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDT 521
Cdd:TIGR01277 95 LHPGlklnaEQQEKVVDAAQQVGIADYLDRLPEQLS-----------GGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180
....*....|....*....|....*
gi 1154151804 522 EADVFESLRRLAA--RRTVILATHS 544
Cdd:TIGR01277 164 REEMLALVKQLCSerQRTLLMVTHH 188
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
367-543 |
5.64e-22 |
|
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: 94.88 E-value: 5.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG---QKPVLFAG-TLRE 442
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGmlfQSGALFDSlTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 NILF------ARPDAT-----QEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLD 511
Cdd:cd03261 97 NVAFplrehtRLSEEEireivLEKLEAVGLRGAEDLYPAELSGG---------------MKKRVALARALALDPELLLYD 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1154151804 512 EPTAHLDPDTeADVFESL-RRLAARR--TVILATH 543
Cdd:cd03261 162 EPTAGLDPIA-SGVIDDLiRSLKKELglTSIMVTH 195
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
365-543 |
7.52e-22 |
|
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: 94.43 E-value: 7.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTswIG---QKPVLFAG-TL 440
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG--IGrtfQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFARpdatQEQLGAAVAAAAAGDFVASLPQ---------GLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLD 511
Cdd:cd03219 93 LENVMVAA----QARTGSGLLLARARREEREAREraeellervGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190
....*....|....*....|....*....|...
gi 1154151804 512 EPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERgITVLLVEH 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
365-543 |
1.62e-21 |
|
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: 91.34 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdmttlapealvamtswigqKPVLFAGTLreni 444
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFASPR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 445 lfarpDAtqEQLGAAvaaaaagdFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEAD 524
Cdd:cd03216 71 -----DA--RRAGIA--------MVYQLSVG---------------ERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180
....*....|....*....|
gi 1154151804 525 VFESLRRLAAR-RTVILATH 543
Cdd:cd03216 121 LFKVIRRLRAQgVAVIFISH 140
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
349-543 |
2.02e-21 |
|
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: 93.41 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVS--FAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMT 426
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 427 SWIG---QKPVLFAG-TLRENILFARPDATQEQLGAAVAAAAAGDFVaslpqGLDTFIGEGGFGLSGGQAQRVAIARAfL 502
Cdd:cd03258 82 RRIGmifQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELV-----GLEDKADAYPAQLSGGQKQRVGIARA-L 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154151804 503 KDAPLVVL-DEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:cd03258 156 ANNPKVLLcDEATSALDPETTQSILALLRDINRELglTIVLITH 199
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
365-544 |
2.03e-21 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 93.01 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELL-----LGFIQPASGRIMFNGVDMTTLAPEAL-----VAMtswIGQKPV 434
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVLelrrrVGM---VFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 435 LFAGTLRENILFA----------RPDATQEQ-LGAAVAAAAAGD--FVASLPQGldtfigeggfglsggQAQRVAIARAF 501
Cdd:cd03260 92 PFPGSIYDNVAYGlrlhgiklkeELDERVEEaLRKAALWDEVKDrlHALGLSGG---------------QQQRLCLARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154151804 502 LKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHS 544
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHN 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
368-566 |
2.70e-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: 92.17 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAL-VAMtswIGQKPVLFAG-TLRENIL 445
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRpVSM---LFQENNLFAHlTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 446 FARPDA---TQEQLGAAVaaaaagdfVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTE 522
Cdd:cd03298 93 LGLSPGlklTAEDRQAIE--------VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154151804 523 ADVFESLRRLAARR--TVILATHSGAVTGFEGQR-IDLAQGHVVTSG 566
Cdd:cd03298 165 AEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQRvVFLDNGRIAAQG 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
343-543 |
1.03e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 95.94 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 343 MTGGvAVAFEHVSFAWDIARgMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAL 422
Cdd:PRK10790 336 LQSG-RIDIDNVSFAYRDDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 423 ---VAMtswIGQKPVLFAGTLRENILFARpDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIAR 499
Cdd:PRK10790 414 rqgVAM---VQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154151804 500 AFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
349-543 |
1.64e-20 |
|
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: 90.82 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDiARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW 428
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKPVLFAG-TLRENI-----LFARPDATQEQLgaavaaaaagdfVASLPQ--GLD--TFIGEGGFGLSGGQAQRVAIA 498
Cdd:cd03295 80 VIQQIGLFPHmTVEENIalvpkLLKWPKEKIRER------------ADELLAlvGLDpaEFADRYPHELSGGQQQRVGVA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154151804 499 RAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRL--AARRTVILATH 543
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTH 194
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
365-540 |
2.43e-20 |
|
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: 90.87 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMtswiG-----QKPVLFAG- 438
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL----GiartfQNPRLFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 439 TLRENILFARPDATQEQLGAAVAAAAA-------------------------GDFVASLPQGldtfigeggfglsggQAQ 493
Cdd:COG0411 95 TVLENVLVAAHARLGRGLLAALLRLPRarreereareraeellervgladraDEPAGNLSYG---------------QQR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154151804 494 RVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVIL 540
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILL 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
366-544 |
3.25e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.77 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENIL 445
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 446 FA---RPDATQEQlgaavaaaaagDFVASLPQ-GL-DTFIGEGGFGLSGGQAQRVAIARAfLKDAPLV-VLDEPTAHLDP 519
Cdd:PRK10247 103 FPwqiRNQQPDPA-----------IFLDDLERfALpDTILTKNIAELSGGEKQRISLIRN-LQFMPKVlLLDEITSALDE 170
|
170 180
....*....|....*....|....*..
gi 1154151804 520 DTEADVFESLRRLAARR--TVILATHS 544
Cdd:PRK10247 171 SNKHNVNEIIHRYVREQniAVLWVTHD 197
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
349-543 |
5.42e-20 |
|
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: 89.22 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDiaRGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP-EALVAMts 427
Cdd:cd03300 1 IELENVSKFYG--GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPhKRPVNT-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 wIGQKPVLFAG-TLRENILFA------RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARA 500
Cdd:cd03300 77 -VFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPSQLS-----------GGQQQRVAIARA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1154151804 501 FLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTH 189
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
365-561 |
9.36e-20 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 88.96 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG---QKPVLfAGTLR 441
Cdd:COG3638 18 ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRIGmifQQFNL-VPRLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 442 --ENIL----------------FARPDATQ-----EQLGAavaaaaaGDF----VASLPQGldtfigeggfglsggQAQR 494
Cdd:COG3638 97 vlTNVLagrlgrtstwrsllglFPPEDRERalealERVGL-------ADKayqrADQLSGG---------------QQQR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154151804 495 VAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATHSgavtgfegqrIDLAQGH 561
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQ----------VDLARRY 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
365-540 |
1.04e-19 |
|
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: 87.87 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTswIGQKP---VLFAG-TL 440
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAG--IGYVPegrRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFA----RPDATQEQLgaavaaaaagDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAH 516
Cdd:cd03224 93 EENLLLGayarRRAKRKARL----------ERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180
....*....|....*....|....
gi 1154151804 517 LDPDTEADVFESLRRLAARRTVIL 540
Cdd:cd03224 163 LAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
365-543 |
1.56e-19 |
|
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: 89.73 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQP---ASGRIMFNGVDMTTLAPEAL-------VAMtswIGQ--- 431
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELrkirgreIQM---IFQdpm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 432 ---KPVL-----FAGTLRENILFARPDATQ------EQLGAAVAAaaagDFVASLP-Q---GldtfigeggfglsggQAQ 493
Cdd:COG0444 97 tslNPVMtvgdqIAEPLRIHGGLSKAEAREraiellERVGLPDPE----RRLDRYPhElsgG---------------MRQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154151804 494 RVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITH 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
365-543 |
1.67e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.16 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPE----ALVAmtswigQKPVLFAG-T 439
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEkrnvGMVF------QDYALFPHlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 LRENILF----------ARPDATQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVV 509
Cdd:COG3842 94 VAENVAFglrmrgvpkaEIRARVAELLELVGLEGLADRYPHQLSGG---------------QQQRVALARALAPEPRVLL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 510 LDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELgiTFIYVTH 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
362-566 |
5.92e-19 |
|
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: 85.71 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 362 RGMAVDDVSFSVPAGQTLLLcGASGSGKSTIIELLLGFIQPASGRIMFNGVDmTTLAPEALVAMTSWIGQKPVLFAG-TL 440
Cdd:cd03264 12 KKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGYLPQEFGVYPNfTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFA----------RPDATQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVL 510
Cdd:cd03264 90 REFLDYIawlkgipskeVKARVDEVLELVNLGDRAKKKIGSLSGG---------------MRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 511 DEPTAHLDPDTEADVFESLRRLAARRTVILATH-SGAVTGFEGQRIDLAQGHVVTSG 566
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEDRIVILSTHiVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
365-543 |
9.38e-19 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 85.00 E-value: 9.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP-EALVAMtswIGQKPVLFAG-TLRE 442
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPkDRDIAM---VFQNYALYPHmTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 NILF------ARPDATQEQLGAavaaaaagdfVASLPQgLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAH 516
Cdd:cd03301 92 NIAFglklrkVPKDEIDERVRE----------VAELLQ-IEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180
....*....|....*....|....*....
gi 1154151804 517 LDPDTEADVFESLRRLAAR--RTVILATH 543
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRlgTTTIYVTH 189
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
366-543 |
1.03e-18 |
|
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: 84.62 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDmttLAPEALVAMTSWIGQKP--VLFAGTLREN 443
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQDVdyQLFTDSVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 ILFA--RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDT 521
Cdd:cd03226 93 LLLGlkELDAGNEQAETVLKDLDLYALKERHPLSLS-----------GGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180
....*....|....*....|...
gi 1154151804 522 EADVFESLRRLAAR-RTVILATH 543
Cdd:cd03226 162 MERVGELIRELAAQgKAVIVITH 184
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
368-543 |
1.12e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 90.47 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGF------------------------------------------------ 399
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkegg 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 400 ------IQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLP 473
Cdd:PTZ00265 1266 sgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLP 1345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154151804 474 QGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRL--AARRTVILATH 543
Cdd:PTZ00265 1346 NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAH 1417
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
348-543 |
1.32e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.44 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAWDIARgmAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAL-VAMT 426
Cdd:COG3839 3 SLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 427 SwigQKPVLF-AGTLRENILFA-----RPDATQEQ--------LGAavaaaaaGDFVASLPQGLDtfigeggfglsGGQA 492
Cdd:COG3839 81 F---QSYALYpHMTVYENIAFPlklrkVPKAEIDRrvreaaelLGL-------EDLLDRKPKQLS-----------GGQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 493 QRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLgtTTIYVTH 192
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
367-548 |
1.40e-18 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 84.20 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTL-APEALVAMTSWIGqkpVLFAG------- 438
Cdd:TIGR03608 15 DDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLnSKKASKFRREKLG---YLFQNfaliene 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 439 TLRENILFA-----RPDATQEQLgaavaaaaagdFVASLPQ-GLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDE 512
Cdd:TIGR03608 92 TVEENLDLGlkykkLSKKEKREK-----------KKEALEKvGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1154151804 513 PTAHLDPDTEADVFESLRRLAAR-RTVILATHSGAVT 548
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPEVA 197
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
368-542 |
1.53e-18 |
|
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: 86.06 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdMTTLAPEalvamTSWIgqkpvlFAGTLRENILFA 447
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQ-----FSWI------MPGTIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 448 RPDATQEQLGAAVAAAAAGDfVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFE 527
Cdd:cd03291 122 VSYDEYRYKSVVKACQLEED-ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
170
....*....|....*.
gi 1154151804 528 S-LRRLAARRTVILAT 542
Cdd:cd03291 201 ScVCKLMANKTRILVT 216
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
349-543 |
1.92e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 85.56 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdMTTLAPEALVAMTSW 428
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IG---QKP--VLFAGTLRENILFA-------------RPDATQEQLGAAvaaaaagDFVASLPQGLdtfigeggfglSGG 490
Cdd:TIGR04520 79 VGmvfQNPdnQFVGATVEDDVAFGlenlgvpreemrkRVDEALKLVGME-------DFRDREPHLL-----------SGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154151804 491 QAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITH 195
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
351-544 |
2.26e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 85.58 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 351 FEHVSFAWDIARGM---AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTS 427
Cdd:TIGR04521 3 LKNVSYIYQPGTPFekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 WIG---QKP--VLFAGTLRENILF-------ARPDATQ------EQLGAAVAAAAAGDFvaSLPQGldtfigeggfglsg 489
Cdd:TIGR04521 83 KVGlvfQFPehQLFEETVYKDIAFgpknlglSEEEAEErvkealELVGLDEEYLERSPF--ELSGG-------------- 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 490 gQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATHS 544
Cdd:TIGR04521 147 -QMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHS 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
349-543 |
4.51e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.42 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTtlaPEALVAMTSW 428
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IG---QKPV-LFAGTL--------RENilFARP-DATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRV 495
Cdd:PRK13648 85 IGivfQNPDnQFVGSIvkydvafgLEN--HAVPyDEMHRRVSEALKQVDMLERADYEPNALS-----------GGQKQRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154151804 496 AIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITH 201
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
346-566 |
4.61e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 82.60 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 346 GVAVAFEHVSFAWDIARGMA----VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPA--SGRIMFNGVDMTTLAP 419
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 420 EALVAMtswIGQKPVLFAG-TLRENILFArpdatqeqlgaavaaaaagdfvASLpQGLDTfigeggfglsgGQAQRVAIA 498
Cdd:cd03213 81 RKIIGY---VPQDDILHPTlTVRETLMFA----------------------AKL-RGLSG-----------GERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 499 RAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATHSGAVTGFEG--QRIDLAQGHVVTSG 566
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSEIFELfdKLLLLSQGRVIYFG 194
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
376-543 |
5.75e-18 |
|
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: 83.80 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 376 GQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENiLFARPDATQEQ 455
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN-LDPECKCTDDR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 456 LGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR 535
Cdd:cd03288 126 LWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD 205
|
....*...
gi 1154151804 536 RTVILATH 543
Cdd:cd03288 206 RTVVTIAH 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
365-543 |
7.76e-18 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 82.19 E-value: 7.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTtLAPEALVAMTSWIG---QKPVLFAG-TL 440
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELRQKVGmvfQQFNLFPHlTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFA------RPDATQEQLGAAVaaaaagdfvasLPQ-GLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEP 513
Cdd:cd03262 94 LENITLApikvkgMSKAEAEERALEL-----------LEKvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190
....*....|....*....|....*....|.
gi 1154151804 514 TAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEgMTMVVVTH 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
368-542 |
8.24e-18 |
|
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: 87.66 E-value: 8.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdMTTLAPEalvamTSWIgqkpvlFAGTLRENILFA 447
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQ-----TSWI------MPGTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 448 RPDATQEQLGAAVAAAAAGDfVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFE 527
Cdd:TIGR01271 511 LSYDEYRYTSVIKACQLEED-IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
170
....*....|....*.
gi 1154151804 528 S-LRRLAARRTVILAT 542
Cdd:TIGR01271 590 ScLCKLMSNKTRILVT 605
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
352-543 |
1.21e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 83.14 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 352 EHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdmTTLAPEalvamTSW--- 428
Cdd:PRK13635 9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEE-----TVWdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 --IG---QKP-VLFAG-TLRENILFA-------------RPDATQEQLGAAvaaaaagDFVASLPQGLDtfigeggfgls 488
Cdd:PRK13635 81 rqVGmvfQNPdNQFVGaTVQDDVAFGlenigvpreemveRVDQALRQVGME-------DFLNREPHRLS----------- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 489 GGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITH 199
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
365-543 |
1.38e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP-EAL---VAMtswIGQKPVLFAG-T 439
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQaagIAI---IHQELNLVPNlS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 LRENILFARP-------------DATQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAP 506
Cdd:COG1129 96 VAENIFLGREprrgglidwramrRRARELLARLGLDIDPDTPVGDLSVA---------------QQQLVEIARALSRDAR 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154151804 507 LVVLDEPTAHLDPDtEADV-FESLRRLAAR-RTVILATH 543
Cdd:COG1129 161 VLILDEPTASLTER-EVERlFRIIRRLKAQgVAIIYISH 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
369-559 |
1.53e-17 |
|
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: 81.39 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 369 VSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMtSWIGQKPVLFAG-TLRENILFA 447
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL-LYLGHAPGIKTTlSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 448 RPDATQEQLgaavaaaaagdFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFE 527
Cdd:cd03231 98 HADHSDEQV-----------EEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170 180 190
....*....|....*....|....*....|....
gi 1154151804 528 SLRRLAAR-RTVILATH-SGAVTGFEGQRIDLAQ 559
Cdd:cd03231 167 AMAGHCARgGMVVLTTHqDLGLSEAGARELDLGF 200
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
368-544 |
1.74e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.07 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAmtsWIGQ----KPVLfagTLREN 443
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH---YLGHrnamKPAL---TVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 ILFARPDATQEQLGAAVAAAAAG-DFVASLPQG-LDTfigeggfglsgGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDT 521
Cdd:PRK13539 94 LEFWAAFLGGEELDIAAALEAVGlAPLAHLPFGyLSA-----------GQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....*
gi 1154151804 522 EAdVFESL--RRLAARRTVILATHS 544
Cdd:PRK13539 163 VA-LFAELirAHLAQGGIVIAATHI 186
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
365-543 |
2.29e-17 |
|
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: 82.31 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAM----TSWIGQKPVLFAG-T 439
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPHrT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 LRENILF----------ARPDATQEQLgaavAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVV 509
Cdd:cd03294 119 VLENVAFglevqgvpraEREERAAEAL----ELVGLEGWEHKYPDELS-----------GGMQQRVGLARALAVDPDILL 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 510 LDEPTAHLDPDTEADVFESLRRLAA--RRTVILATH 543
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAelQKTIVFITH 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
367-543 |
2.79e-17 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 81.19 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTtLAPEALVAMTSWIG---QKPVLFAG-TLRE 442
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRKVGmvfQQFNLFPHlTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 NILFA--------RPDATQ------EQLGAavaaaaaGDFVASLPQ----GldtfigeggfglsggQAQRVAIARAfLKD 504
Cdd:COG1126 97 NVTLApikvkkmsKAEAEEramellERVGL-------ADKADAYPAqlsgG---------------QQQRVAIARA-LAM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1154151804 505 APLVVL-DEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:COG1126 154 EPKVMLfDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTH 194
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
365-541 |
3.00e-17 |
|
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: 80.94 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFN----GVDMTTLAPEALVAM----TSWIGQ----- 431
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREILALrrrtIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 432 ----------KPVLFAGTLRENilfARPDATQ--EQLGaavaaaaagdfvasLPQGL-----DTFigeggfglSGGQAQR 494
Cdd:COG4778 106 prvsaldvvaEPLLERGVDREE---ARARAREllARLN--------------LPERLwdlppATF--------SGGEQQR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154151804 495 VAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILA 541
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIG 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
366-543 |
3.98e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.22 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQP---ASGRIMFNGVDMTTLAPEAlvamtSWIG---QKPVLFAG- 438
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ-----RRIGilfQDDLLFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 439 TLRENILFA---------RPDATQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVV 509
Cdd:COG4136 92 SVGENLAFAlpptigraqRRARVEQALEEAGLAGFADRDPATLSGG---------------QRARVALLRALLAEPRALL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154151804 510 LDEPTAHLDPDTEAD----VFESLRRLAArrTVILATH 543
Cdd:COG4136 157 LDEPFSKLDAALRAQfrefVFEQIRQRGI--PALLVTH 192
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
365-543 |
4.83e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.43 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG---QKPVLFAG-TL 440
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGmifQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFA-----RPDATQEQ-----LgaavaaaaagDFV----------ASLPQGldtfigeggfglsggQAQRVAIARA 500
Cdd:COG1135 100 AENVALPleiagVPKAEIRKrvaelL----------ELVglsdkadaypSQLSGG---------------QKQRVGIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1154151804 501 fLKDAPLVVL-DEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:COG1135 155 -LANNPKVLLcDEATSALDPETTRSILDLLKDINRELglTIVLITH 199
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
370-544 |
6.08e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.40 E-value: 6.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 370 SFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPealvamtswiGQKPV--------LFAG-TL 440
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP----------SRRPVsmlfqennLFSHlTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENI-LFARP-----DATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEPT 514
Cdd:PRK10771 89 AQNIgLGLNPglklnAAQREKLHAIARQMGIEDLLARLPGQLS-----------GGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|..
gi 1154151804 515 AHLDPDTEADVFESLRRLAARR--TVILATHS 544
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHS 189
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
364-543 |
6.78e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.58 E-value: 6.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 364 MAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP-EALVAMtswIGQKPVLFAG-TLR 441
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPyQRPINM---MFQSYALFPHmTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 442 ENILFArpdATQEQLGAAVAAAAAGDFVASLpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPD- 520
Cdd:PRK11607 110 QNIAFG---LKQDKLPKAEIASRVNEMLGLV--HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKl 184
|
170 180
....*....|....*....|....*.
gi 1154151804 521 ---TEADVFESLRRLAArrTVILATH 543
Cdd:PRK11607 185 rdrMQLEVVDILERVGV--TCVMVTH 208
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
365-566 |
9.73e-17 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 80.03 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG---QKPVLFAG-TL 440
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRIGmifQHYNLIERlTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFARPDAT---QEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHL 517
Cdd:TIGR02315 97 LENVLHGRLGYKptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154151804 518 DPDTEADVFESLRRLAARR--TVILATHS-GAVTGFEGQRIDLAQGHVVTSG 566
Cdd:TIGR02315 177 DPKTSKQVMDYLKRINKEDgiTVIINLHQvDLAKKYADRIVGLKAGEIVFDG 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
367-543 |
2.08e-16 |
|
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: 78.63 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVA----MTSWIGQKPVLFAG-TLR 441
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlrarHVGFVFQSFQLLPTlTAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 442 ENI-----LFARPDATQ------EQLGAavaaaaaGDFVASLPQGLdtfigeggfglSGGQAQRVAIARAFLKDAPLVVL 510
Cdd:COG4181 109 ENVmlpleLAGRRDARArarallERVGL-------GHRLDHYPAQL-----------SGGEQQRVALARAFATEPAILFA 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1154151804 511 DEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:COG4181 171 DEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTH 205
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
356-543 |
2.41e-16 |
|
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: 78.14 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 356 FAWdiARGMA-VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMT----SWIG 430
Cdd:cd03290 8 FSW--GSGLAtLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysvAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 431 QKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGDfVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVL 510
Cdd:cd03290 86 QKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPD-IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154151804 511 DEPTAHLDPD-----TEADVFESLRRlaARRTVILATH 543
Cdd:cd03290 165 DDPFSALDIHlsdhlMQEGILKFLQD--DKRTLVLVTH 200
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
365-543 |
2.79e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.77 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAlvamtswIG---------QKpvl 435
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR-------IGylpeerglyPK--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 436 faGTLRENIL-FAR------PDATQ------EQLGaavAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFL 502
Cdd:COG4152 86 --MKVGEQLVyLARlkglskAEAKRradewlERLG---LGDRANKKVEELSKG---------------NQQKVQLIAALL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154151804 503 KDAPLVVLDEPTAHLDPDTeADVFES-LRRLAAR-RTVILATH 543
Cdd:COG4152 146 HDPELLILDEPFSGLDPVN-VELLKDvIRELAAKgTTVIFSSH 187
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
366-566 |
3.55e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.52 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAG-TLRE-- 442
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRElv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 -------NILFARPDATQEQLGAavaaaaagdfVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTA 515
Cdd:PRK11231 98 aygrspwLSLWGRLSAEDNARVN----------QAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 516 HLDPDTEADVFESLRRLAAR-RTVILATHS-GAVTGFEGQRIDLAQGHVVTSG 566
Cdd:PRK11231 168 YLDINHQVELMRLMRELNTQgKTVVTVLHDlNQASRYCDHLVVLANGHVMAQG 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
365-540 |
3.97e-16 |
|
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: 77.71 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTswIGQKP---VLFAG-TL 440
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLG--IGYVPegrRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENIL---FARPDATQEQlgaavaaaaagdfvASLPQGLDTFIGEGGFGLSGG------QAQRVAIARAFLKDAPLVVLD 511
Cdd:COG0410 96 EENLLlgaYARRDRAEVR--------------ADLERVYELFPRLKERRRQRAgtlsggEQQMLAIGRALMSRPKLLLLD 161
|
170 180
....*....|....*....|....*....
gi 1154151804 512 EPTAHLDPDTEADVFESLRRLAARRTVIL 540
Cdd:COG0410 162 EPSLGLAPLIVEEIFEIIRRLNREGVTIL 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
365-543 |
4.74e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAlvAMTSWIG---QKPVLFAG-TL 440
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD--AIALGIGmvhQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFARPDATQEQLGAAVAAAAAGDF-------------VASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPL 507
Cdd:COG3845 98 AENIVLGLEPTKGGRLDRKAARARIRELserygldvdpdakVEDLSVG---------------EQQRVEILKALYRGARI 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154151804 508 VVLDEPTAHLDPDtEAD-VFESLRRLAAR-RTVILATH 543
Cdd:COG3845 163 LILDEPTAVLTPQ-EADeLFEILRRLAAEgKSIIFITH 199
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
363-543 |
6.05e-16 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 78.36 E-value: 6.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 363 GMAV-DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQpASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLR 441
Cdd:cd03289 16 GNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 442 ENiLFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDT 521
Cdd:cd03289 95 KN-LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180
....*....|....*....|..
gi 1154151804 522 EADVFESLRRLAARRTVILATH 543
Cdd:cd03289 174 YQVIRKTLKQAFADCTVILSEH 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
365-544 |
6.38e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.55 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTtlapEALVAMTSW---IG---QKP--VLF 436
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT----DKKVKLSDIrkkVGlvfQYPeyQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 437 AGTLRENILFArpdatQEQLGAAVAAAAAGDFVASLPQGLD--TFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPT 514
Cdd:PRK13637 98 EETIEKDIAFG-----PINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190
....*....|....*....|....*....|..
gi 1154151804 515 AHLDPDTEADVFESLRRLAARR--TVILATHS 544
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYnmTIILVSHS 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
347-543 |
7.44e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.72 E-value: 7.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 347 VAVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTlapEALVAMT 426
Cdd:PRK13632 6 VMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 427 SWIG---QKP-VLFAG-TLRENILFA------RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRV 495
Cdd:PRK13632 83 KKIGiifQNPdNQFIGaTVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQNLS-----------GGQKQRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154151804 496 AIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITH 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
363-543 |
7.49e-16 |
|
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: 81.50 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 363 GMAV-DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQpASGRIMFNGVDMTTlapealVAMTSW------IGQKPVL 435
Cdd:TIGR01271 1231 GRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNS------VTLQTWrkafgvIPQKVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 436 FAGTLRENiLFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTA 515
Cdd:TIGR01271 1304 FSGTFRKN-LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180
....*....|....*....|....*...
gi 1154151804 516 HLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
365-543 |
7.63e-16 |
|
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: 76.55 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLA-------PE--ALVAMTSWIGQkpVL 435
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEerGLYPKMKVIDQ--LV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 436 FAGTLRE-NILFARPDATQ--EQLGAAVAAAAAgdfVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDE 512
Cdd:cd03269 93 YLAQLKGlKKEEARRRIDEwlERLELSEYANKR---VEELSKG---------------NQQKVQFIAAVIHDPELLILDE 154
|
170 180 190
....*....|....*....|....*....|....
gi 1154151804 513 PTAHLDP---DTEADVFESLRRlaARRTVILATH 543
Cdd:cd03269 155 PFSGLDPvnvELLKDVIRELAR--AGKTVILSTH 186
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
352-543 |
9.97e-16 |
|
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: 76.25 E-value: 9.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 352 EHVSFAWDIARG--MAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWI 429
Cdd:cd03266 5 DALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 430 GQKPVLFAGTLRENIL-FAR-----PDATQEQLGAAVAAAAAGDF----VASLPQGldtfigeggfglsggQAQRVAIAR 499
Cdd:cd03266 85 DSTGLYDRLTARENLEyFAGlyglkGDELTARLEELADRLGMEELldrrVGGFSTG---------------MRQKVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1154151804 500 AFLKDAPLVVLDEPTAHLDPDTEADVFESLRRL-AARRTVILATH 543
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTH 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
365-543 |
1.42e-15 |
|
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: 76.22 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQK-------PVLFA 437
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKtqlwwdlPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 438 GTLRENILFARPDATQEQLGAAVAAAAAGDF----VASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDEP 513
Cdd:cd03267 116 FYLLAAIYDLPPARFKKRLDELSELLDLEELldtpVRQLSLG---------------QRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190
....*....|....*....|....*....|..
gi 1154151804 514 TAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERgtTVLLTSH 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
368-543 |
1.47e-15 |
|
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: 80.37 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENiLFA 447
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN-LDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 448 RPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFE 527
Cdd:TIGR00957 1383 FSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQS 1462
|
170
....*....|....*.
gi 1154151804 528 SLRRLAARRTVILATH 543
Cdd:TIGR00957 1463 TIRTQFEDCTVLTIAH 1478
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
327-543 |
1.47e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.41 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 327 LP-DATPVRVGGQAVCDMTGGVAVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASG 405
Cdd:PLN03232 1212 LPsEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKG 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 406 RIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENIlfarpDATQEQ----LGAAVAAAAAGDFVASLPQGLDTFIG 481
Cdd:PLN03232 1292 RIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI-----DPFSEHndadLWEALERAHIKDVIDRNPFGLDAEVS 1366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154151804 482 EGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:PLN03232 1367 EGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAH 1428
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
368-543 |
1.62e-15 |
|
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: 75.77 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPA---SGRIMFNGVDMTtlaPEALVAMTSWIGQKPVLFAG-TLREN 443
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRK---PDQFQKCVAYVRQDDILLPGlTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 ILFARPDATQEQLGAAVAAAAAGDFvaSLPQGLDTFIGEGGFGLSGG-QAQRVAIARAFLKDAPLVVLDEPTAHLDPDTE 522
Cdd:cd03234 102 LTYTAILRLPRKSSDAIRKKRVEDV--LLRDLALTRIGGNLVKGISGgERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180
....*....|....*....|..
gi 1154151804 523 ADVFESLRRLAAR-RTVILATH 543
Cdd:cd03234 180 LNLVSTLSQLARRnRIVILTIH 201
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
365-425 |
1.62e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 77.85 E-value: 1.62e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAM 425
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPL 93
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
348-560 |
1.77e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.47 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAwdIARGMA-VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFngvdmttlaPEALVAMt 426
Cdd:COG4178 362 ALALEDLTLR--TPDGRPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVL- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 427 sWIGQKPVLFAGTLRENILFARP--DATQEQLGAAVAAAAAGDFVASLPQGLDTfigegGFGLSGGQAQRVAIARAFLKD 504
Cdd:COG4178 430 -FLPQRPYLPLGTLREALLYPATaeAFSDAELREALEAVGLGHLAERLDEEADW-----DQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154151804 505 APLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGAVTGFEGQRIDLAQG 560
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
364-543 |
1.87e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.88 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 364 MAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTT-LAPE----ALVAmtswigQKPVLFAG 438
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRerrvGFVF------QHYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 439 -TLRENILFA----RPDATQ------EQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPL 507
Cdd:COG1118 90 mTVAENIAFGlrvrPPSKAEirarveELLELVQLEGLADRYPSQLSGG---------------QRQRVALARALAVEPEV 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154151804 508 VVLDEPTAHLDPDTEADVFESLRRL--AARRTVILATH 543
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTH 192
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
348-569 |
1.91e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.76 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQP---ASGRIMFNGVDMTtlapealvA 424
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLT--------A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 425 MTSWigqkpvlfagTLREN--ILFARPD-----ATQE----------QLGAAVAAAAAGDFVASLpqGLDTFIGEGGFGL 487
Cdd:PRK13640 77 KTVW----------DIREKvgIVFQNPDnqfvgATVGddvafglenrAVPRPEMIKIVRDVLADV--GMLDYIDSEPANL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 488 SGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATHSGAVTGFEGQRIDLAQGHVVTS 565
Cdd:PRK13640 145 SGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQ 224
|
....
gi 1154151804 566 GEKV 569
Cdd:PRK13640 225 GSPV 228
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
38-307 |
3.27e-15 |
|
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: 76.42 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 38 VGQVWCIATALACVLVPGGMPVVAWPLAGLVGLAVAragLQAASDTLAARAGMKGRAR----LRGGVIEAIMRGGPGLLR 113
Cdd:cd18781 13 IAFVFSIANLLQKLLEGKLTTASLLIVLGILAIAII---VRFICTRLASRASYRASADvkktLREKIYDKLLRLGPSYQE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 114 QHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLAAFVQPGSALIMAVCgiaVPFGQALFGIGAAVASR--- 190
Cdd:cd18781 90 KVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLIC---VPLIPISIIAVQKIAKKlls 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 191 NQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAfLSSASIdcaM-VVA---------LV 260
Cdd:cd18781 167 KYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQ-LNSITV---MdLVAyggaalgiiLA 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1154151804 261 LVALRNGaHLmdlheqgvpaaimagQVARGLFVVLVVPEFFAPFRSL 307
Cdd:cd18781 243 LLQFANG-SI---------------SLAGALFIILLSAEFFLPLRLL 273
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
359-540 |
3.42e-15 |
|
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: 74.01 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 359 DIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTswIG------QK 432
Cdd:cd03215 9 GLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG--IAyvpedrKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 433 PVLFAG-TLRENILFARpdatqeqlgaavaaaaagdfvaSLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLD 511
Cdd:cd03215 87 EGLVLDlSVAENIALSS----------------------LLSGG---------------NQQKVVLARWLARDPRVLILD 129
|
170 180
....*....|....*....|....*....
gi 1154151804 512 EPTAHLDPDTEADVFESLRRLAARRTVIL 540
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVL 158
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
365-543 |
3.94e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.93 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKP--VLFAGTLRE 442
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 NILFA------RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEPTAH 516
Cdd:PRK13647 100 DVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPYHLS-----------YGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180
....*....|....*....|....*...
gi 1154151804 517 LDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQgKTVIVATH 196
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
365-543 |
5.40e-15 |
|
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: 74.33 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTlAPEALVAMTSWIGQKPVLFAG-TLREN 443
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 I-LFAR----PDA-----TQEQLGAAVAAAAAGDFVASLPQGLdtfigeggfglsggqAQRVAIARAFLKDAPLVVLDEP 513
Cdd:cd03265 94 LyIHARlygvPGAerrerIDELLDFVGLLEAADRLVKTYSGGM---------------RRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 1154151804 514 TAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFgmTILLTTH 190
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
353-544 |
5.69e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 74.90 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 353 HVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMtswigQK 432
Cdd:COG4525 10 SVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVF-----QK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 433 PVLFAG-TLRENILF----------ARPDATQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAF 501
Cdd:COG4525 85 DALLPWlNVLDNVAFglrlrgvpkaERRARAEELLALVGLADFARRRIWQLSGG---------------MRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1154151804 502 LKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR--RTVILATHS 544
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITHS 194
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
313-543 |
7.17e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 313 DRAHASGAASAMRILPDATPVRVGGQAVCDMTGGVA-VAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKST 391
Cdd:PRK13536 3 TRAVAEEAPRRLELSPIERKHQGISEAKASIPGSMStVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 392 IIELLLGFIQPASGRIMFNGVDMttlaPEALVAMTSWIGQKPVL----FAGTLRENIL-FAR--------PDATQEQLGA 458
Cdd:PRK13536 83 IARMILGMTSPDAGKITVLGVPV----PARARLARARIGVVPQFdnldLEFTVRENLLvFGRyfgmstreIEAVIPSLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 459 AVAAAAAGDF-VASLPQGLDtfigeggfglsggqaQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR-R 536
Cdd:PRK13536 159 FARLESKADArVSDLSGGMK---------------RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgK 223
|
....*..
gi 1154151804 537 TVILATH 543
Cdd:PRK13536 224 TILLTTH 230
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
26-297 |
7.41e-15 |
|
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: 74.99 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 26 VVLLGLAISAIAVGQVWCIATALAcVLVPGGMPV---VAWPLAGLVGLAVARAGLQAASDTLAARAGMKGRARLRGGVIE 102
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILD-VLLPDGDPEtqaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 103 AIMRGGPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLAAFVQPGSALIMAVCGIAVPFGQALFG 182
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 183 IGAAVASRNQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLSSASIDcAMVVALVLV 262
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQ-FIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|....*
gi 1154151804 263 ALRNGAHLmdlheqgvpaaIMAGQVARGLFVVLVV 297
Cdd:pfam00664 242 ALWFGAYL-----------VISGELSVGDLVAFLS 265
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
346-535 |
8.79e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 74.46 E-value: 8.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 346 GVAVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAM 425
Cdd:TIGR02769 7 DVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 426 --------------------TSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVaaaaagDFVASLPQGLDtfigeggf 485
Cdd:TIGR02769 87 rrdvqlvfqdspsavnprmtVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS------EDADKLPRQLS-------- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154151804 486 glsGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR 535
Cdd:TIGR02769 153 ---GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQA 199
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
362-540 |
8.82e-15 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 73.71 E-value: 8.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 362 RGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAM-TSWIGQKPVLFAG-T 439
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 LRENI---LFARPDATQEqlgaavaaaaAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAH 516
Cdd:TIGR03410 92 VEENLltgLAALPRRSRK----------IPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEG 161
|
170 180
....*....|....*....|....*.
gi 1154151804 517 LDPDTEADVFESLRRLAARR--TVIL 540
Cdd:TIGR03410 162 IQPSIIKDIGRVIRRLRAEGgmAILL 187
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
349-541 |
1.22e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARGMAV-DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNgvDMTTLAPEALVAMTS 427
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 WIG---QKPVLFAGTLRENI---LFARPD-------------ATQEQLGAAVAAAAAG---------------------- 466
Cdd:PTZ00265 461 KIGvvsQDPLLFSNSIKNNIkysLYSLKDlealsnyynedgnDSQENKNKRNSCRAKCagdlndmsnttdsneliemrkn 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 467 -------------------DFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFE 527
Cdd:PTZ00265 541 yqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250
....*....|....*..
gi 1154151804 528 SLRRLAA---RRTVILA 541
Cdd:PTZ00265 621 TINNLKGnenRITIIIA 637
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
365-543 |
1.50e-14 |
|
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: 72.07 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNG--VDMTTLAPEALVAMTSWIGQKP--VLFAGTL 440
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGepLDYSRKGLLERRQRVGLVFQDPddQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFA------RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEPT 514
Cdd:TIGR01166 87 DQDVAFGplnlglSEAEVERRVREALTAVGASGLRERPTHCLS-----------GGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 1154151804 515 AHLDPDTEADVFESLRRL-AARRTVILATH 543
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLrAEGMTVVISTH 185
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
348-568 |
1.68e-14 |
|
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: 73.58 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSfawdIARG--MAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASG---RIM---FNGVDMTTLAP 419
Cdd:COG1119 3 LLELRNVT----VRRGgkTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 420 E-ALV--AMTSWI-GQKPVL------FAGTLReniLFARPDATQEQ-----LGAAVAAAAAGDFVASLPQGldtfigegg 484
Cdd:COG1119 79 RiGLVspALQLRFpRDETVLdvvlsgFFDSIG---LYREPTDEQRErarelLELLGLAHLADRPFGTLSQG--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 485 fglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR--RTVILATH--SGAVTGFEgQRIDLAQG 560
Cdd:COG1119 147 ------EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHhvEEIPPGIT-HVLLLKDG 219
|
....*...
gi 1154151804 561 HVVTSGEK 568
Cdd:COG1119 220 RVVAAGPK 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
349-557 |
1.74e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.42 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDiARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRImfngvDMTTLAPEALVAmtsw 428
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----GMPEGEDLLFLP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 igQKPVLFAGTLRENILFA-----RPDatqEQlgaavaaaaagdfvaslpqgldtfigeggfglsggqaQRVAIARAFLK 503
Cdd:cd03223 71 --QRPYLPLGTLREQLIYPwddvlSGG---EQ-------------------------------------QRLAFARLLLH 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154151804 504 DAPLVVLDEPTAHLDPDTEADVFESLRRLAArrTVILATHSGAVTGFEGQRIDL 557
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHRPSLWKFHDRVLDL 160
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
364-543 |
3.32e-14 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 72.05 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 364 MAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTlapEALVAMTSWIGQKPVLFAGTLREN 443
Cdd:TIGR03740 14 TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR---KDLHKIGSLIESPPLYENLTAREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 I-----LFARPDAT-QEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsggqaQRVAIARAFLKDAPLVVLDEPTAHL 517
Cdd:TIGR03740 91 LkvhttLLGLPDSRiDEVLNIVDLTNTGKKKAKQFSLGMK---------------QRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180
....*....|....*....|....*..
gi 1154151804 518 DPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:TIGR03740 156 DPIGIQELRELIRSFPEQgITVILSSH 182
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
381-543 |
3.74e-14 |
|
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: 73.68 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 381 LCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWigQKPVLFAG-TLRENILFA-----RPDAT-Q 453
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVF--QSYALFPHmTVEENVAFGlkmrkVPRAEiK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 454 EQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLA 533
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKPHQLS-----------GGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170
....*....|..
gi 1154151804 534 ARR--TVILATH 543
Cdd:TIGR01187 148 EQLgiTFVFVTH 159
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
352-543 |
4.05e-14 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 72.54 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 352 EHVSfaWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQ 431
Cdd:TIGR03873 5 SRVS--WSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVEQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 432 K-PVLFAGTLRENILFAR-PDATQEQLGAAVAAAAAGDFVASLpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVV 509
Cdd:TIGR03873 83 DsDTAVPLTVRDVVALGRiPHRSLWAGDSPHDAAVVDRALART--ELSHLADRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1154151804 510 LDEPTAHLDPDTEADVFESLRRLAARR-TVILATH 543
Cdd:TIGR03873 161 LDEPTNHLDVRAQLETLALVRELAATGvTVVAALH 195
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
349-563 |
4.28e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.83 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARgMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW 428
Cdd:PRK10908 2 IRFEHVSKAYLGGR-QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQ------------------KPVLFAGTLRENILfARPDATQEQLGAAvaaaaagDFVASLPQGLDtfigeggfglsGG 490
Cdd:PRK10908 81 IGMifqdhhllmdrtvydnvaIPLIIAGASGDDIR-RRVSAALDKVGLL-------DKAKNFPIQLS-----------GG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 491 QAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADV---FESLRRLAArrTVILATHSGAVTGFEGQRI-DLAQGHVV 563
Cdd:PRK10908 142 EQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlFEEFNRVGV--TVLMATHDIGLISRRSYRMlTLSDGHLH 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
231-544 |
4.89e-14 |
|
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: 75.75 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 231 EELRLRTMKVLRVAFLSSASIDCAMVVALVLVALRNGAHLMDLHEQGVPAAIMAgQVARGLFVVLVVPeffapFRSLALA 310
Cdd:TIGR00957 523 EGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKA-FVSLALFNILRFP-----LNILPMV 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 311 YQDRAHASGAASAMRIL-------PDAT---PVRVGGqavcdmtgGVAVAFEHVSFAWdiARGM--AVDDVSFSVPAGQT 378
Cdd:TIGR00957 597 ISSIVQASVSLKRLRIFlsheelePDSIerrTIKPGE--------GNSITVHNATFTW--ARDLppTLNGITFSIPEGAL 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 379 LLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdmttlaPEALVAMTSWIGQKpvlfagTLRENILFARPDATQEQLGA 458
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------SVAYVPQQAWIQND------SLRENILFGKALNEKYYQQV 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 459 AVAAAAAGDfVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESL---RRLAAR 535
Cdd:TIGR00957 734 LEACALLPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKN 812
|
....*....
gi 1154151804 536 RTVILATHS 544
Cdd:TIGR00957 813 KTRILVTHG 821
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
368-562 |
5.49e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.77 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTS----WIGQKPVLFAG-TLRE 442
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqklgFIYQFHHLLPDfTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 NILF------ARPDATQEQlgaavaaaaAGDFVASLpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAH 516
Cdd:PRK11629 107 NVAMplligkKKPAEINSR---------ALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154151804 517 LDPDTEADVFESLRRLAARR--TVILATHSGAVTGFEGQRIDLAQGHV 562
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
26-308 |
5.85e-14 |
|
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: 72.58 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 26 VVLLGLAISAIAVGQVWCIATALACVLVPGGMPVVAWPLAGLVGLAVARAGLQAASDTLAARAGMKGRARLRGGVIEAIM 105
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 106 RGGPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLAAFVQPGSALIMAVCGIAVPFGQALFGIGA 185
Cdd:cd07346 84 RLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 186 AVASRNQFLAMTRLQARFLDRVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLSSASID--CAMVVALVLVA 263
Cdd:cd07346 164 RKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGllTALGTALVLLY 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1154151804 264 lrnGAHLmdlheqgvpaaIMAGQVARGLFVVLV--VPEFFAPFRSLA 308
Cdd:cd07346 244 ---GGYL-----------VLQGSLTIGELVAFLayLGMLFGPIQRLA 276
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
367-559 |
6.05e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTsWIGQ----KPVLfagTLRE 442
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLL-YLGHqpgiKTEL---TALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 NILFARP---DATQEQLGAAVAAAAAGDF----VASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDEPTA 515
Cdd:PRK13538 94 NLRFYQRlhgPGDDEALWEALAQVGLAGFedvpVRQLSAG---------------QQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154151804 516 HLDpDTEADVFESLRRLAARR--TVILATH-SGAVTGFEGQRIDLAQ 559
Cdd:PRK13538 159 AID-KQGVARLEALLAQHAEQggMVILTTHqDLPVASDKVRKLRLGQ 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
365-536 |
6.96e-14 |
|
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: 74.34 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIqPASGRIMFNGVDMTTLAPEALVAMTSWIgQkpVLF-------- 436
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRM-Q--VVFqdpfgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 437 -----AGTLRENILFARPD---ATQEQLgaavaaaaagdfVASLPQ--GLDtfigeggfgLSGG----------QAQRVA 496
Cdd:COG4172 377 prmtvGQIIAEGLRVHGPGlsaAERRAR------------VAEALEevGLD---------PAARhryphefsggQRQRIA 435
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154151804 497 IARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR 536
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREH 475
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
365-543 |
8.54e-14 |
|
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: 71.22 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAlvAMTSWIGQKPVLFAG-TLREN 443
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 ILF--------ARPDATQEQlgaavaaaaagDFVASLPQ--GLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEP 513
Cdd:cd03296 95 VAFglrvkprsERPPEAEIR-----------AKVHELLKlvQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 514 TAHLDpdteADVFESLRRLAAR------RTVILATH 543
Cdd:cd03296 164 FGALD----AKVRKELRRWLRRlhdelhVTTVFVTH 195
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
365-543 |
8.95e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.91 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG---QKPVLFAG-TL 440
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGmifQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFA-----RPDA-----TQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAfLKDAPLVVL 510
Cdd:PRK11153 100 FDNVALPlelagTPKAeikarVTELLELVGLSDKADRYPAQLSGG---------------QKQRVAIARA-LASNPKVLL 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 511 -DEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:PRK11153 164 cDEATSALDPATTRSILELLKDINRELglTIVLITH 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
365-566 |
1.26e-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: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTlapeALVAMTSWIGQKP---VLFAG-TL 440
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPqhnILFHHlTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFarpdatQEQLGAAVAAAAAGDFVASLPQ-GLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDP 519
Cdd:TIGR01257 1021 AEHILF------YAQLKGRSWEEAQLEMEAMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154151804 520 DTEADVFESLRRLAARRTVILATHSGAVTGFEGQRID-LAQGHVVTSG 566
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAiISQGRLYCSG 1142
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
368-544 |
1.51e-13 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 70.02 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLcGASGSGKSTIIELLLGFIQPASGRIMFNGV------DMTTLAPEAlvAMTSWIGQKPVLFAG-TL 440
Cdd:cd03297 16 KIDFDLNEEVTGIF-GASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrKKINLPPQQ--RKIGLVFQQYALFPHlNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFARPDATQEQLGaavaaaaagDFVASLPQ--GLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLD 518
Cdd:cd03297 93 RENLAFGLKRKRNREDR---------ISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180
....*....|....*....|....*...
gi 1154151804 519 PDTEADVFESLRRLAAR--RTVILATHS 544
Cdd:cd03297 164 RALRLQLLPELKQIKKNlnIPVIFVTHD 191
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
366-543 |
1.72e-13 |
|
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: 70.19 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWigqkPVLFAGTLRENIL 445
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNY----SLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 446 FArPDATQEQLGAAVAAAAAGDFVASLpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADV 525
Cdd:TIGR01184 77 LA-VDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180
....*....|....*....|
gi 1154151804 526 FESLRRLA--ARRTVILATH 543
Cdd:TIGR01184 154 QEELMQIWeeHRVTVLMVTH 173
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
369-532 |
1.89e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 369 VSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW-IGQKPVLFAG-TLRENILF 446
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYlVPQEPLLFPNlSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 447 --ARPDATQEQLGaavaaaaagDFVASLPQGLDtfIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEAD 524
Cdd:PRK15439 110 glPKRQASMQKMK---------QLLAALGCQLD--LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETER 178
|
....*...
gi 1154151804 525 VFESLRRL 532
Cdd:PRK15439 179 LFSRIREL 186
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
366-543 |
2.11e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAlvamTSWIGQKPVL------FagT 439
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA----RQRVGVVPQFdnldpdF--T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 LRENIL-----FARPDATQEQLGAAVAaaaagDFvASLPQGLDTFIGEGGFGLSggqaQRVAIARAFLKDAPLVVLDEPT 514
Cdd:PRK13537 97 VRENLLvfgryFGLSAAAARALVPPLL-----EF-AKLENKADAKVGELSGGMK----RRLTLARALVNDPDVLVLDEPT 166
|
170 180 190
....*....|....*....|....*....|
gi 1154151804 515 AHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARgKTILLTTH 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
365-556 |
2.28e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMT-------------------TLAPEALVAM 425
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttaalaagvaiiyqelHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 426 TSWIGQKPVLFaGTLRENILFARpdaTQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDA 505
Cdd:PRK11288 99 NLYLGQLPHKG-GIVNRRLLNYE---AREQLEHLGVDIDPDTPLKYLSIG---------------QRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 506 PLVVLDEPTAHLDPDTEADVFESLRRLAARRTVIL-ATH--------SGAVTGF-EGQRID 556
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILyVSHrmeeifalCDAITVFkDGRYVA 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
367-563 |
5.43e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 71.68 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMT----SWIGQK---------- 432
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRrehfGFIFQRyhllshltaa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 433 -----PVLFAGTLRENILfARPDATQEQLGaavaaaaAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPL 507
Cdd:PRK10535 105 qnvevPAVYAGLERKQRL-LRAQELLQRLG-------LEDRVEYQPSQLS-----------GGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 508 VVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATHSGAVTGFEGQRIDLAQGHVV 563
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
365-519 |
6.77e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 69.10 E-value: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNG--------------VDM------TTLAPEalva 424
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrckhIRMifqdpnTSLNPR---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 425 mtSWIGQ---KPVLFAGTLRENILFARPDATQEQLGAavaaaaagdfvasLPQGLDTFIGEGGFGlsggQAQRVAIARAF 501
Cdd:COG4167 104 --LNIGQileEPLRLNTDLTAEEREERIFATLRLVGL-------------LPEHANFYPHMLSSG----QKQRVALARAL 164
|
170
....*....|....*...
gi 1154151804 502 LKDAPLVVLDEPTAHLDP 519
Cdd:COG4167 165 ILQPKIIIADEALAALDM 182
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
365-543 |
7.70e-13 |
|
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: 69.34 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTlAPEALVAMTSWIGQKPVLFAG-TLREN 443
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQYASVDEDlTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 I-LFAR-----PDATQEQLGAAVAAAAAGDFvASLPQGldTFigeggfglSGGQAQRVAIARAFLKDAPLVVLDEPTAHL 517
Cdd:TIGR01188 87 LeMMGRlyglpKDEAEERAEELLELFELGEA-ADRPVG--TY--------SGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180
....*....|....*....|....*..
gi 1154151804 518 DPDTEADVFESLRRL-AARRTVILATH 543
Cdd:TIGR01188 156 DPRTRRAIWDYIRALkEEGVTILLTTH 182
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
368-567 |
8.48e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 71.73 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRImfngvdmttLAPEALvamtSWIGQKPVLFAGTLRENILFA 447
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERSI----AYVPQQAWIMNATVRGNILFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 448 RPDATQEQLGAAVAAAAAGDfVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFE 527
Cdd:PTZ00243 745 DEEDAARLADAVRVSQLEAD-LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVE 823
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154151804 528 S--LRRLAArRTVILATHSGAVTGFEGQRIDLAQGHVVTSGE 567
Cdd:PTZ00243 824 EcfLGALAG-KTRVLATHQVHVVPRADYVVALGDGRVEFSGS 864
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
360-543 |
1.04e-12 |
|
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: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 360 IARGM--AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMF----NGVDMTTLAPEALVAMTSWIG--- 430
Cdd:TIGR03269 292 VDRGVvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRGRAKRYIGilh 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 431 QKPVLFA-----GTLRENILFARPD--ATQEQLGAAVAAAAAGDFVAS-LPQGLDTFigeggfglSGGQAQRVAIARAFL 502
Cdd:TIGR03269 372 QEYDLYPhrtvlDNLTEAIGLELPDelARMKAVITLKMVGFDEEKAEEiLDKYPDEL--------SEGERHRVALAQVLI 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1154151804 503 KDAPLVVLDEPTAHLDPDTEADVFESLrrLAAR----RTVILATH 543
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSI--LKAReemeQTFIIVSH 486
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
366-542 |
1.27e-12 |
|
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: 67.57 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP--EALVAMtSWIGQKPVLFAG-TLRE 442
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkRARLGI-GYLPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 NILFA---RPDATQEQLgaAVAAAAAGDFvaslpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDP 519
Cdd:cd03218 95 NILAVleiRGLSKKERE--EKLEELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180
....*....|....*....|...
gi 1154151804 520 DTEADVFESLRRLAARRTVILAT 542
Cdd:cd03218 167 IAVQDIQKIIKILKDRGIGVLIT 189
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-418 |
1.88e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 69.83 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 20 RRQAMPVVLLGLAISAIAVGQVWCIATALAcvlvpGGMPVVAWPLAGLVGLAVARAGLQAASDTLAARAGMKGRARLRGG 99
Cdd:COG4615 12 RWLLLLALLLGLLSGLANAGLIALINQALN-----ATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 100 VIEAIMRGGPGLLRQHHTGELTALAVDRIEALDGFFARwLPASVlwVAAPLVIGVLA--AFVQPGSALIMAVC-GIAVPF 176
Cdd:COG4615 87 LSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELL--QSVALVLGCLAylAWLSPPLFLLTLVLlGLGVAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 177 GQALFGIGaavasrNQFLAMTR-----LQARFLDRVRGIATIVLSGRTEDE--TRRLAASAEELRLRTMKVLRVAFLSSA 249
Cdd:COG4615 164 YRLLVRRA------RRHLRRAReaedrLFKHFRALLEGFKELKLNRRRRRAffDEDLQPTAERYRDLRIRADTIFALANN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 250 SIDCAM--VVALVLVALrngahlmdLHEQGVPAAIMAGQVARGLFVVlvvpeffAPFRSLALAYQDRAHASGAASAMRIL 327
Cdd:COG4615 238 WGNLLFfaLIGLILFLL--------PALGWADPAVLSGFVLVLLFLR-------GPLSQLVGALPTLSRANVALRKIEEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 328 PDATPVrvGGQAVCDMTGGVAVA------FEHVSFAW---DIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLG 398
Cdd:COG4615 303 ELALAA--AEPAAADAAAPPAPAdfqtleLRGVTYRYpgeDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTG 380
|
410 420
....*....|....*....|..
gi 1154151804 399 FIQPASGRIMFNG--VDMTTLA 418
Cdd:COG4615 381 LYRPESGEILLDGqpVTADNRE 402
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
369-530 |
1.91e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.54 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 369 VSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENIlfar 448
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---- 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 449 pDATQEQ----LGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEAD 524
Cdd:PLN03130 1334 -DPFNEHndadLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDAL 1412
|
....*.
gi 1154151804 525 VFESLR 530
Cdd:PLN03130 1413 IQKTIR 1418
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
368-544 |
2.13e-12 |
|
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: 68.60 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTT------LAPEAlvAMTSWIGQKPVLFAG-TL 440
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEK--RRIGYVFQEARLFPHlSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFARPDATQEQLGAAVaaaaagDFVASLpQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPD 520
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISF------ERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180
....*....|....*....|....*.
gi 1154151804 521 TEADVFESLRRLAA--RRTVILATHS 544
Cdd:TIGR02142 166 RKYEILPYLERLHAefGIPILYVSHS 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
365-543 |
2.70e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.72 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRimfngVDMTTLAPEALVAMTSWIGQK-PVLFA-----G 438
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT-----VRRAGGARVAYVPQRSEVPDSlPLTVRdlvamG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 439 TLRENILFARPDATQEqlgaavaaAAAGDFVASLpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLD 518
Cdd:NF040873 82 RWARRGLWRRLTRDDR--------AAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180
....*....|....*....|....*.
gi 1154151804 519 PDTEADVFESLRRLAAR-RTVILATH 543
Cdd:NF040873 152 AESRERIIALLAEEHARgATVVVVTH 177
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
366-536 |
3.52e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 66.72 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVL-FAGTLRENI 444
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 445 LFAR----------PDATQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFL------KDAPLV 508
Cdd:PRK13548 98 AMGRaphglsraedDALVAAALAQVDLAHLAGRDYPQLSGG---------------EQQRVQLARVLAqlwepdGPPRWL 162
|
170 180
....*....|....*....|....*...
gi 1154151804 509 VLDEPTAHLDPDTEADVFESLRRLAARR 536
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHER 190
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
345-543 |
3.79e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 345 GGVAVAFEHVSFAWDI-ARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPAsgrimfngvDMTTLAPEALV 423
Cdd:PLN03232 611 GAPAISIKNGYFSWDSkTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA---------ETSSVVIRGSV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 424 AmtsWIGQKPVLFAGTLRENILFARpDATQEQLGAAVAaaaagdfVASLPQGLDTF-------IGEGGFGLSGGQAQRVA 496
Cdd:PLN03232 682 A---YVPQVSWIFNATVRENILFGS-DFESERYWRAID-------VTALQHDLDLLpgrdlteIGERGVNISGGQKQRVS 750
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154151804 497 IARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKgKTRVLVTN 798
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
365-543 |
6.09e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.41 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNG--VDMTTLAPEALVAMTSWIGQKP--VLFAGTL 440
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFArpdATQEQLGAAVAAAAAGDFVASlpQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPD 520
Cdd:PRK13636 101 YQDVSFG---AVNLKLPEDEVRKRVDNALKR--TGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180
....*....|....*....|....*
gi 1154151804 521 TEADVFESLRRLAARR--TVILATH 543
Cdd:PRK13636 176 GVSEIMKLLVEMQKELglTIIIATH 200
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
365-568 |
8.34e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGR--IMFNGVDM-TTLAPEALVAMTSWIG---QK----PV 434
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlnIAGNHFDFsKTPSDKAIRELRRNVGmvfQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 435 LfagTLRENILFArP--------DATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAP 506
Cdd:PRK11124 97 L---TVQQNLIEA-PcrvlglskDQALARAEKLLERLRLKPYADRFPLHLS-----------GGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154151804 507 LVVLDEPTAHLDPDTEADVFESLRRLAARR-TVILATHSGAVTGFEGQR-IDLAQGHVVTSGEK 568
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKTASRvVYMENGHIVEQGDA 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
348-542 |
9.77e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 9.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAWDI-ARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPAS-GRIMFNGVdmttlapEALVAM 425
Cdd:PLN03130 614 AISIKNGYFSWDSkAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-------VAYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 426 TSWIgqkpvlFAGTLRENILFARPDATQEQLGAAVAAAAAGDfVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDA 505
Cdd:PLN03130 687 VSWI------FNATVRDNILFGSPFDPERYERAIDVTALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154151804 506 PLVVLDEPTAHLDPDTEADVFES-LRRLAARRTVILAT 542
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVT 797
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
365-566 |
1.49e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMT------SW---IGQKPVL 435
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVpqseevDWsfpVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 436 FAGTLRENILFARPDATQEQLgaavaaaaagdFVASLPQ-GLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPT 514
Cdd:PRK15056 102 MMGRYGHMGWLRRAKKRDRQI-----------VTAALARvDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154151804 515 AHLDPDTEADVFESLRRLAAR-RTVILATHS-GAVTGFEGQRIdLAQGHVVTSG 566
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEgKTMLVSTHNlGSVTEFCDYTV-MVKGTVLASG 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
352-541 |
2.42e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 64.37 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 352 EHVSFAwdIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQ 431
Cdd:COG4559 5 ENLSVR--LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 432 KPVL-FAGTLRENILFAR----------PDATQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARA 500
Cdd:COG4559 83 HSSLaFPFTVEEVVALGRaphgssaaqdRQIVREALALVGLAHLAGRSYQTLSGG---------------EQQRVQLARV 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154151804 501 FL-----KDAP--LVVLDEPTAHLDPDTEADVFESLRRLAARRTVILA 541
Cdd:COG4559 148 LAqlwepVDGGprWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVA 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
365-543 |
2.87e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.95 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALV-----AMTSWIG-QKPVLF-- 436
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVvfqneGLLPWRNvQDNVAFgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 437 --AGTLREnilfARPDATQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDEPT 514
Cdd:PRK11248 96 qlAGVEKM----QRLEIAHQMLKKVGLEGAEKRYIWQLSGG---------------QRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|.
gi 1154151804 515 AHLDPDTEADVFESLRRLAAR--RTVILATH 543
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
365-544 |
3.25e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.90 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKST-------IIELLLGFIqpASGRIMFNGVDMttLAPEA-LVAMTSWIG---QKP 433
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTllrclnrMNDLIPGAR--VEGEILLDGEDI--YDPDVdVVELRRRVGmvfQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 434 VLFAGTLRENILF----------ARPDATQEQ--------------LgaavaaaaaGDFVASLPQGldtfigeggfglsg 489
Cdd:COG1117 102 NPFPKSIYDNVAYglrlhgikskSELDEIVEEslrkaalwdevkdrL---------KKSALGLSGG-------------- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 490 gQAQRVAIARAF-LKdaPLVVL-DEPTAHLDPDTEADVFESLRRLAARRTVILATHS 544
Cdd:COG1117 159 -QQQRLCIARALaVE--PEVLLmDEPTSALDPISTAKIEELILELKKDYTIVIVTHN 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
365-518 |
3.63e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.97 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEalvamtswigQKPV--------LF 436
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE----------NRHVntvfqsyaLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 437 AG-TLRENILFA-----RPDA-TQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVV 509
Cdd:PRK09452 99 PHmTVFENVAFGlrmqkTPAAeITPRVMEALRMVQLEEFAQRKPHQLS-----------GGQQQRVAIARAVVNKPKVLL 167
|
....*....
gi 1154151804 510 LDEPTAHLD 518
Cdd:PRK09452 168 LDESLSALD 176
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
346-536 |
4.64e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.55 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 346 GVAVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAM 425
Cdd:PRK10419 8 GLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 426 --------------------TSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAaagdfvASLPQGLDtfigeggf 485
Cdd:PRK10419 88 rrdiqmvfqdsisavnprktVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVL------DKRPPQLS-------- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 486 glsGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR 536
Cdd:PRK10419 154 ---GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQF 201
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
364-543 |
6.59e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.88 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 364 MAVDDVSFSVPAGQTLLLCGASGSGKSTII-------ELLLGFiqPASGRIMFNGVDMttLAPEA-LVAMTSWIG---QK 432
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGF--RVEGKVTFHGKNL--YAPDVdPVEVRRRIGmvfQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 433 PVLFAGTLRENILF-ARPDATQEQLGAAVAAAAAGdfvASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLD 511
Cdd:PRK14243 100 PNPFPKSIYDNIAYgARINGYKGDMDELVERSLRQ---AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190
....*....|....*....|....*....|..
gi 1154151804 512 EPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
351-566 |
6.64e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.50 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 351 FEHVSFAWDIA---RGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMfngVDMTTLAPEA----LV 423
Cdd:PRK13634 5 FQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT---IGERVITAGKknkkLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 424 AMTSWIG---QKP--VLFAGTLRENILF-------ARPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQ 491
Cdd:PRK13634 82 PLRKKVGivfQFPehQLFEETVEKDICFgpmnfgvSEEDAKQKAREMIELVGLPEELLARSPFELS-----------GGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154151804 492 AQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATHS-GAVTGFEGQRIDLAQGHVVTSG 566
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSmEDAARYADQIVVMHKGTVFLQG 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
365-566 |
8.09e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 62.34 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDM---TTLAPEALVAMTSWIG---QK----PV 434
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGmvfQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 435 LfagTLRENILFArP--------DATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAP 506
Cdd:COG4161 97 L---TVMENLIEA-PckvlglskEQAREKAMKLLARLRLTDKADRFPLHLS-----------GGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154151804 507 LVVLDEPTAHLDPDTEADVFESLRRLAARR-TVILATHSGAVT-GFEGQRIDLAQGHVVTSG 566
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFArKVASQVVYMEKGRIIEQG 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
347-544 |
8.68e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 62.92 E-value: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 347 VAVAFEHVSFAWDIARGM---AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMT----TLAP 419
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 420 EALVAMTSWIGQKP--VLFAGTLRENILF-----------ARPDATQ--EQLGAAVAAAAAGDFVASlpqgldtfigegg 484
Cdd:PRK13641 81 KKLRKKVSLVFQFPeaQLFENTVLKDVEFgpknfgfsedeAKEKALKwlKKVGLSEDLISKSPFELS------------- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 485 fglsGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRL-AARRTVILATHS 544
Cdd:PRK13641 148 ----GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHN 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
366-543 |
9.75e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.83 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdmttlapEALVAMTSWigqkpvlfagTLRENI- 444
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG--------DLLTEENVW----------DIRHKIg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 445 -LFARPD-----ATQEQ---LGAAVAAAAAGDFVASLPQGLD-----TFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVL 510
Cdd:PRK13650 85 mVFQNPDnqfvgATVEDdvaFGLENKGIPHEEMKERVNEALElvgmqDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 1154151804 511 DEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDYqmTVISITH 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
369-543 |
9.75e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 369 VSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAGTLRENIlfaR 448
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---D 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 449 P--DATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLK-DAPLVVLDEPTAHLDPDTEADV 525
Cdd:PTZ00243 1406 PflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQI 1485
|
170
....*....|....*...
gi 1154151804 526 FESLRRLAARRTVILATH 543
Cdd:PTZ00243 1486 QATVMSAFSAYTVITIAH 1503
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
365-543 |
1.13e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.41 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDmtTLAPEALVAMTSWIG---QKP--VLFAGT 439
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEENLWDIRNKAGmvfQNPdnQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 LRENILFA------RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEP 513
Cdd:PRK13633 103 VEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPHLLS-----------GGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190
....*....|....*....|....*....|..
gi 1154151804 514 TAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKKYgiTIILITH 203
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
365-532 |
1.17e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.19 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTS---WIGQKPV------- 434
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSdiqMIFQDPLaslnprm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 435 ----LFAGTLREnilfARPDATQEQLGAAVAAAAAGdfVASLPQgldtFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVL 510
Cdd:PRK15079 116 tigeIIAEPLRT----YHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180
....*....|....*....|..
gi 1154151804 511 DEPTAHLDPDTEADVFESLRRL 532
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQL 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
368-531 |
1.42e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.18 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTL-APEALVAmtsWIGQKPVLFAG-TLRENIL 445
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLhARDRKVG---FVFQHYALFRHmTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 446 FA--------RPDA------TQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLD 511
Cdd:PRK10851 97 FGltvlprreRPNAaaikakVTQLLEMVQLAHLADRYPAQLSGG---------------QKQRVALARALAVEPQILLLD 161
|
170 180
....*....|....*....|
gi 1154151804 512 EPTAHLDpdteADVFESLRR 531
Cdd:PRK10851 162 EPFGALD----AQVRKELRR 177
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
349-566 |
1.46e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIAR---GMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVA- 424
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 425 ---MTSWIGQKP--VLFAGTLRENILF-------ARPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQA 492
Cdd:PRK13643 82 vrkKVGVVFQFPesQLFEETVLKDVAFgpqnfgiPKEKAEKIAAEKLEMVGLADEFWEKSPFELS-----------GGQM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154151804 493 QRVAIARAFLKDAPLVVLDEPTAHLDPDTEAD---VFESLRRLAarRTVILATH-SGAVTGFEGQRIDLAQGHVVTSG 566
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEmmqLFESIHQSG--QTVVLVTHlMDDVADYADYVYLLEKGHIISCG 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
364-566 |
1.66e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.13 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 364 MAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAM----TSWIGQKPVLFAG- 438
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHm 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 439 TLRENILFArpdatQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLD 518
Cdd:PRK10070 122 TVLDNTAFG-----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 519 PDTEADVFESLRRLAAR--RTVILATHSGAVTGFEGQRIDLAQ-GHVVTSG 566
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhqRTIVFISHDLDEAMRIGDRIAIMQnGEVVQVG 247
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-543 |
1.69e-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: 63.55 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 353 HVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKS----TIIELLLGFIQPASGRIMFNGVDMTTLAPEAL------ 422
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELrrirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 423 -VAMtswIGQKPV-----LF------AGTLRENILFARPDATQ------EQLGAAVAAAAAGDFVASLPQGldtfigegg 484
Cdd:COG4172 93 rIAM---IFQEPMtslnpLHtigkqiAEVLRLHRGLSGAAARAralellERVGIPDPERRLDAYPHQLSGG--------- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 485 fglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:COG4172 161 ------QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITH 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
358-525 |
2.54e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.90 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 358 WDIARGM--------AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWI 429
Cdd:PRK11308 15 YPVKRGLfkperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 430 G---QKPVlfaGTL--RENI--LFARPDATQEQLGAAVAAAAAGDFVASLpqGLDT-FIGEGGFGLSGGQAQRVAIARAF 501
Cdd:PRK11308 95 QivfQNPY---GSLnpRKKVgqILEEPLLINTSLSAAERREKALAMMAKV--GLRPeHYDRYPHMFSGGQRQRIAIARAL 169
|
170 180
....*....|....*....|....
gi 1154151804 502 LKDAPLVVLDEPTAHLDPDTEADV 525
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQV 193
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
365-567 |
2.84e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.16 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDmtTLAPEALVAMTSWIG---QKP-VLFAG-T 439
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGIRKLVGivfQNPeTQFVGrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 LRENILFAR------PDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEP 513
Cdd:PRK13644 95 VEEDLAFGPenlclpPIEIRKRVDRALAEIGLEKYRHRSPKTLS-----------GGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154151804 514 TAHLDPDTEADVFESLRRLAAR-RTVILATHSGAVTGFEGQRIDLAQGHVVTSGE 567
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
365-525 |
3.15e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGfIQPA---SGRIMFNGVDMT-------------------TLAPEAL 422
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQasnirdteragiaiihqelALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 423 VAMTSWIGQKPVLFaGTLRENILFARPDATQEQLGAAVAAAAAgdfVASLPQGldtfigeggfglsggQAQRVAIARAFL 502
Cdd:PRK13549 99 VLENIFLGNEITPG-GIMDYDAMYLRAQKLLAQLKLDINPATP---VGNLGLG---------------QQQLVEIAKALN 159
|
170 180
....*....|....*....|...
gi 1154151804 503 KDAPLVVLDEPTAHLdpdTEADV 525
Cdd:PRK13549 160 KQARLLILDEPTASL---TESET 179
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
366-543 |
4.96e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGV----DMTTLAPEaLVAMTSWIGQKPVLfagTLR 441
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkDLCTYQKQ-LCFVGHRSGINPYL---TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 442 ENILF-ARPDATQEQLGAAVAAAAAGDFVaSLPQGLdtfigeggfgLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDpd 520
Cdd:PRK13540 93 ENCLYdIHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-- 159
|
170 180
....*....|....*....|....*..
gi 1154151804 521 tEADVFESLRRLAARR----TVILATH 543
Cdd:PRK13540 160 -ELSLLTIITKIQEHRakggAVLLTSH 185
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-546 |
5.15e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.49 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 334 RVGGQAVCDMTGGVAVAFEHVSFAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASG-------- 405
Cdd:PRK14271 5 RLGGQSGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 406 ---RIMFNGVDMttLAPEALVAMtswIGQKPVLFAGTLRENIL--------FARPD---ATQEQLGAAVAAAAAGDFVAS 471
Cdd:PRK14271 85 lggRSIFNYRDV--LEFRRRVGM---LFQRPNPFPMSIMDNVLagvrahklVPRKEfrgVAQARLTEVGLWDAVKDRLSD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154151804 472 LPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGA 546
Cdd:PRK14271 160 SPFRLS-----------GGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLA 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
365-543 |
5.61e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.59 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKP--VLFAGTLRE 442
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 NILFArpdATQEQLGAAVAAAAAGDFVASLpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTE 522
Cdd:PRK13652 99 DIAFG---PINLGLDEETVAHRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180
....*....|....*....|...
gi 1154151804 523 ADVFESLRRLAAR--RTVILATH 543
Cdd:PRK13652 174 KELIDFLNDLPETygMTVIFSTH 196
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
365-543 |
7.01e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTL--APEALVAMTSWIGQKPV-------- 434
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkkTKEKEKVLEKLVIQKTRfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 435 ----------------LFAGTLRENILFA-------RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQ 491
Cdd:PRK13651 102 eirrrvgvvfqfaeyqLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGLDESYLQRSPFELS-----------GGQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 492 AQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTH 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
352-567 |
7.58e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 352 EHVSFAWDIARGM---------AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIqPASGRIMFNGVDMTTLAPEAL 422
Cdd:PRK15134 279 EQLQVAFPIRKGIlkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 423 VAMTSWIgqkPVLF-----AGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQ-GLDTFIGEGG-FGLSGGQAQRV 495
Cdd:PRK15134 358 LPVRHRI---QVVFqdpnsSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEvGLDPETRHRYpAEFSGGQRQRI 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154151804 496 AIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTV--ILATHS-GAVTGFEGQRIDLAQGHVVTSGE 567
Cdd:PRK15134 435 AIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDlHVVRALCHQVIVLRQGEVVEQGD 509
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
369-560 |
7.79e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.41 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 369 VSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSW-IG----------------- 430
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhVGfvfqsfmliptlnalen 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 431 -QKPVLFAGtlrENILFARPDATQ--EQLGAavaaaaaGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPL 507
Cdd:PRK10584 109 vELPALLRG---ESSRQSRNGAKAllEQLGL-------GKRLDHLPAQLS-----------GGEQQRVALARAFNGRPDV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154151804 508 VVLDEPTAHLDPDTE---ADVFESLRRLAArRTVILATHSGAVTGFEGQRIDLAQG 560
Cdd:PRK10584 168 LFADEPTGNLDRQTGdkiADLLFSLNREHG-TTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
368-544 |
8.44e-10 |
|
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: 60.50 E-value: 8.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNG---VDMTT---LAPE----ALVAmtswigQKPVLFA 437
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgifLPPHrrriGYVF------QEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 438 G-TLRENILFAR-----------PDATQEQLGAavaaaaaGDFVASLPQGLDTfigeggfglsgGQAQRVAIARAFLKDA 505
Cdd:COG4148 91 HlSVRGNLLYGRkrapraerrisFDEVVELLGI-------GHLLDRRPATLSG-----------GERQRVAIGRALLSSP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1154151804 506 PLVVLDEPTAHLDPDTEADVFESLRRLAARRT--VILATHS 544
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDipILYVSHS 193
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
365-543 |
9.01e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.10 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDmttlaP----EALVAMTSWI-GQK------- 432
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PfkrrKEFARRIGVVfGQRsqlwwdl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 433 PVLfaGTLReniLFAR----PDAT-QEQLGAAVAAAAAGDFVA------SLpqGldtfigeggfglsggQAQRVAIARAF 501
Cdd:COG4586 112 PAI--DSFR---LLKAiyriPDAEyKKRLDELVELLDLGELLDtpvrqlSL--G---------------QRMRCELAAAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154151804 502 LKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSH 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
366-543 |
1.03e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.63 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVL-FAGTLRENI 444
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 445 LFARpdatQEQLGAAVAAAAAGDFV---ASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDT 521
Cdd:PRK09536 99 EMGR----TPHRSRFDTWTETDRAAverAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180
....*....|....*....|...
gi 1154151804 522 EADVFESLRRLAAR-RTVILATH 543
Cdd:PRK09536 175 QVRTLELVRRLVDDgKTAVAAIH 197
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
365-566 |
1.31e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.86 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRI----MFNGVDMTTLAPEA------------LVAMTSW 428
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKP--VLFAGTLRENILFA-------RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIAR 499
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSPFGLS-----------GGQKRRVAIAG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154151804 500 AFLKDAPLVVLDEPTAHLDPDTEADVFE-SLRRLAARRTVILATHS-GAVTGFEGQRIDLAQGHVVTSG 566
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQlILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKILKTG 258
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
366-543 |
1.32e-09 |
|
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: 60.92 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLlGFIQPasgriMFNGVdMTTLAPEALVamtsWIGQKPVLFAGTLRENIL 445
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWP-----VYGGR-LTKPAKGKLF----YVPQRPYMTLGTLRDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 446 FarPDATQEQlgaavAAAAAGDfvASLPQGLD----TFIGEGGFGLSGGQ----------AQRVAIARAFLKDAPLVVLD 511
Cdd:TIGR00954 537 Y--PDSSEDM-----KRRGLSD--KDLEQILDnvqlTHILEREGGWSAVQdwmdvlsggeKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|..
gi 1154151804 512 EPTAHLDPDTEADVFESLRRlaARRTVILATH 543
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLCRE--FGITLFSVSH 637
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
365-544 |
1.68e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.94 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLaPEALVAmtSWIG---QKPVlfAGT-- 439
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRA--KYIGrvfQDPM--MGTap 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 ---LRENILFARPDATQEQLGAAVAAAAAGDF---VASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEP 513
Cdd:COG1101 96 smtIEENLALAYRRGKRRGLRRGLTKKRRELFrelLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190
....*....|....*....|....*....|...
gi 1154151804 514 TAHLDPDTEADVFESLRRLAARR--TVILATHS 544
Cdd:COG1101 176 TAALDPKTAALVLELTEKIVEENnlTTLMVTHN 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
345-521 |
1.72e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.46 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 345 GGVAVAFEHVSFAWD---IargmaVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFnGV--------- 412
Cdd:COG0488 312 GKKVLELEGLSKSYGdktL-----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkigyfdq 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 413 DMTTLAPEALV--AMTSWIGQKPVLFAGTLRENILFARPDATQeqlgaavaaaaagdFVASLPQGldtfigeggfglsgg 490
Cdd:COG0488 386 HQEELDPDKTVldELRDGAPGGTEQEVRGYLGRFLFSGDDAFK--------------PVGVLSGG--------------- 436
|
170 180 190
....*....|....*....|....*....|.
gi 1154151804 491 QAQRVAIARAFLKDAPLVVLDEPTAHLDPDT 521
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDIET 467
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
365-544 |
2.17e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELL--LGFIQP---ASGRIMFNGVDMttLAPEA-LVAMTSWIG---QKPVL 435
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNI--YSPRTdTVDLRKEIGmvfQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 436 FAGTLRENILFA-RPDATQEQ--LGAAVAAAAAGdfvASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDE 512
Cdd:PRK14239 98 FPMSIYENVVYGlRLKGIKDKqvLDEAVEKSLKG---ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190
....*....|....*....|....*....|..
gi 1154151804 513 PTAHLDPDTEADVFESLRRLAARRTVILATHS 544
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRS 206
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
365-566 |
2.70e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.10 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFI---QPASGRIMFNGvdmTTLAPEALVA--------MTSWIGQKP 433
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLG---RTVQREGRLArdirksraNTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 434 VLFAG-TLRENILFARPDAT---QEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVV 509
Cdd:PRK09984 96 NLVNRlSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 510 LDEPTAHLDPDTEADVFESLRRLAARR--TVILATHSGAVTGFEGQRI-DLAQGHVVTSG 566
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIvALRQGHVFYDG 235
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
369-567 |
2.84e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.93 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 369 VSFSVPAGQTLLLCGASGSGKSTIIELLLGFIqPASGRIMFNGVDMTTLAPEALVAMTSWIGQK-PVLFAGTLRENILFA 447
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 448 RPDATQEQLGAAVAAAAAGDFvaslpqGLDTFIGEGGFGLSGGQAQRVAIARAFLK-------DAPLVVLDEPTAHLDPD 520
Cdd:COG4138 94 QPAGASSEAVEQLLAQLAEAL------GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154151804 521 TEADVFESLRRLAAR-RTVILATHSGAVTGFEGQRI-DLAQGHVVTSGE 567
Cdd:COG4138 168 QQAALDRLLRELCQQgITVVMSSHDLNHTLRHADRVwLLKQGKLVASGE 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
367-543 |
2.87e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFI--QPASGRIMFNGVDMTTLAP--EALVAMTSWIGQKPVLFAGTLRE 442
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASliDAIGRKGDFKDAVELLNAVGLSD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 NILFARPdatqeqlgaavaaaaagdfVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTE 522
Cdd:COG2401 127 AVLWLRR-------------------FKELSTG---------------QKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|...
gi 1154151804 523 ADVFESLRRLA--ARRTVILATH 543
Cdd:COG2401 173 KRVARNLQKLArrAGITLVVATH 195
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
367-543 |
4.19e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.41 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdMTTLAPEALVAM----TSWIGQKPVLFAG-TLR 441
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLirqeAGMVFQQFYLFPHlTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 442 ENILF--------ARPDATQ---EQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVL 510
Cdd:PRK09493 96 ENVMFgplrvrgaSKEEAEKqarELLAKVGLAERAHHYPSELSGG---------------QQQRVAIARALAVKPKLMLF 160
|
170 180 190
....*....|....*....|....*....|....
gi 1154151804 511 DEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTH 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
348-567 |
4.97e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.45 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAWDIA---RGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP----E 420
Cdd:PRK13649 2 GINLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 421 ALVAMTSWIGQKP--VLFAGTLRENILF-------ARPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQ 491
Cdd:PRK13649 82 QIRKKVGLVFQFPesQLFEETVLKDVAFgpqnfgvSQEEAEALAREKLALVGISESLFEKNPFELS-----------GGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 492 AQRVAIARAFLKDAPLVVLDEPTAHLDPDTEA---DVFESLRRLAArrTVILATH-SGAVTGFEGQRIDLAQGHVVTSGE 567
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKelmTLFKKLHQSGM--TIVLVTHlMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
367-543 |
5.57e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.54 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMF-NGVDMTTLApealvamtswigQKPVLFAG-TLRENI 444
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGYLP------------QEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 445 L--FARPDATQEQLGAAVAAAAAGDF-----------------------VASLPQGLDtfIGEGGFGLSGG-----QAQR 494
Cdd:COG0488 83 LdgDAELRALEAELEELEAKLAEPDEdlerlaelqeefealggweaearAEEILSGLG--FPEEDLDRPVSelsggWRRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154151804 495 VAIARAFLKDAPLVVLDEPTAHLDpdteadvFESLRRLAA-----RRTVILATH 543
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLD-------LESIEWLEEflknyPGTVLVVSH 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
351-543 |
6.07e-09 |
|
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: 54.76 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 351 FEHVSFAWD---IargmaVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdmttlapealvamts 427
Cdd:cd03221 3 LENLSKTYGgklL-----LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 wiGQKPVLFagtlrenilfarpdatqEQL--GaavaaaaagdfvaslpqgldtfigeggfglsggQAQRVAIARAFLKDA 505
Cdd:cd03221 62 --TVKIGYF-----------------EQLsgG---------------------------------EKMRLALAKLLLENP 89
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154151804 506 PLVVLDEPTAHLDPDTEADVFESLRRLaaRRTVILATH 543
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
365-543 |
6.73e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.01 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMtTLAPEALVAMTSWIG---QKP--VLFAGT 439
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKTVGivfQNPddQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 LRENILFA------RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEP 513
Cdd:PRK13639 96 VEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPHHLS-----------GGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 1154151804 514 TAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEgITIIISTH 195
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
365-567 |
1.02e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.34 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNG--------------VDMTTLAPEALVAMTSWIG 430
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqrIRMIFQDPSTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 431 QkpvLFAGTLRENILFARPDATQEQLGAAVAAAAAGDFVASLPQGLdtfigeggfglSGGQAQRVAIARAFLKDAPLVVL 510
Cdd:PRK15112 108 Q---ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHML-----------APGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 511 DEPTAHLDPDTEADVFESLRRLAARRTV--ILAT-HSGAVTGFEGQRIDLAQGHVVTSGE 567
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKQGIsyIYVTqHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
365-543 |
1.06e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.71 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALV-AMTSWIG---QKP--VLFAG 438
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrPVRKRIGmvfQFPesQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 439 TLRENILF-----------ARPDATQ--EQLGAAVAAAAAGDFVASlpqgldtfigeggfglsGGQAQRVAIARAFLKDA 505
Cdd:PRK13646 102 TVEREIIFgpknfkmnldeVKNYAHRllMDLGFSRDVMSQSPFQMS-----------------GGQMRKIAIVSILAMNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154151804 506 PLVVLDEPTAHLDPDTEADVFESLRRLAAR--RTVILATH 543
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSH 204
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
376-549 |
1.26e-08 |
|
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: 53.92 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 376 GQTLLLCGASGSGKSTIIELLLGFIQPASGRImfngvdmttlapealvamtswigqkpvlfagtlreniLFARPDATQEQ 455
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------------------IYIDGEDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 456 LGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLA-- 533
Cdd:smart00382 45 VLDQLLLIIVGGKKASGSGE---------------LRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180
....*....|....*....|.
gi 1154151804 534 -----ARRTVILATHSGAVTG 549
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLG 130
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
369-567 |
1.60e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.53 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 369 VSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP--------EALVAMTSWIGQKPVLFAG-T 439
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliRQLRQHVGFVFQNFNLFPHrT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 LRENIL--------FARPDATQEQLGAAVAAAAAGDfVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLD 511
Cdd:PRK11264 102 VLENIIegpvivkgEPKEEATARARELLAKVGLAGK-ETSYPRRLS-----------GGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154151804 512 EPTAHLDPDTEADVFESLRRLA-ARRTVILATHSGAVTGFEGQR-IDLAQGHVVTSGE 567
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAqEKRTMVIVTHEMSFARDVADRaIFMDQGRIVEQGP 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
366-568 |
1.74e-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: 54.84 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGF--IQPASGRIMFNGVDMTTLAPE--ALVAMT-SWigQKPVLFAGtl 440
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEerARLGIFlAF--QYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 renilfarpdatqeqlgaavaaAAAGDFVASLPQGLdtfigeggfglSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPD 520
Cdd:cd03217 92 ----------------------VKNADFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 521 TEADVFESLRRLAAR-RTVILATHSGAVtgFEGQRID----LAQGHVVTSGEK 568
Cdd:cd03217 139 ALRLVAEVINKLREEgKSVLIITHYQRL--LDYIKPDrvhvLYDGRIVKSGDK 189
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
376-566 |
2.03e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.98 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 376 GQTLLLCGASGSGKSTIIELLLGFIQPA---SGRIMFNGVDMTTlapEALVAMTSWIGQKPvLFAGTL--RENILF---- 446
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA---KEMRAISAYVQQDD-LFIPTLtvREHLMFqahl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 447 ------------ARPDATQEQLGaavaaaaagdfvasLPQGLDTFIGEGGFGLSGG--QAQRVAIARAFLKDAPLVVLDE 512
Cdd:TIGR00955 127 rmprrvtkkekrERVDEVLQALG--------------LRKCANTRIGVPGRVKGLSggERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 513 PTAHLDPDTEADVFESLRRLAAR-RTVILATHSGAVTGFE--GQRIDLAQGHVVTSG 566
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSSELFElfDKIILMAEGRVAYLG 249
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
366-543 |
2.52e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.88 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAL-VAMtswIGQKPVLFAG-TLREN 443
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRdICM---VFQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 I-----LFARPDA-----TQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAF-LKdaPLVVL-D 511
Cdd:PRK11432 99 VgyglkMLGVPKEerkqrVKEALELVDLAGFEDRYVDQISGG---------------QQQRVALARALiLK--PKVLLfD 161
|
170 180 190
....*....|....*....|....*....|....
gi 1154151804 512 EPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFniTSLYVTH 195
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
365-566 |
2.65e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.40 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFN--GVDMTTLAPEALVAMTSWIG---QKP--VLFA 437
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPANLKKIKEVKRLRKEIGlvfQFPeyQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 438 GTLRENILFARPDATQEQLGAAVAAAAAGDFVaSLPQgldTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHL 517
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPE---DYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 518 DPDTEAD---VFESLRRLAARRtVILATHS-GAVTGFEGQRIDLAQGHVVTSG 566
Cdd:PRK13645 182 DPKGEEDfinLFERLNKEYKKR-IIMVTHNmDQVLRIADEVIVMHEGKVISIG 233
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
365-446 |
2.67e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.09 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdmtTLAPeaLVAMTSwiGQKPVLfagTLRENI 444
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----RVSA--LLELGA--GFHPEL---TGRENI 109
|
..
gi 1154151804 445 LF 446
Cdd:COG1134 110 YL 111
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
371-520 |
3.12e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 371 FSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWI-GQKPVLFAgtlRENILFA-- 447
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLpGLKADLST---LENLHFLcg 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 448 ----RPdatQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPD 520
Cdd:PRK13543 109 lhgrRA---KQMPGSALAIVGLAGYEDTLVRQLS-----------AGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
381-543 |
5.66e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.24 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 381 LCGASGSGKSTIIELLLGFIQPASGRIMFNG--VDMTTLAPEALVAMTSWIGQKP--VLFAGTLRENILFarpdaTQEQL 456
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFYTDIDSDIAF-----SLRNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 457 GAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR- 535
Cdd:PRK13638 107 GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQg 186
|
....*...
gi 1154151804 536 RTVILATH 543
Cdd:PRK13638 187 NHVIISSH 194
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
376-553 |
5.72e-08 |
|
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: 53.95 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 376 GQTLLLCGASGSGKSTIIELLLGFIQPASGRImfnGVDMTTLA--PEALVAMtswigqkpvlFAGTLREnILFARPD--A 451
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSykPQYIKAD----------YEGTVRD-LLSSITKdfY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 452 TQEQLGAAVAAaaagdfvaslPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRR 531
Cdd:cd03237 91 THPYFKTEIAK----------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190
....*....|....*....|....*....|..
gi 1154151804 532 LA--ARRTVILATH--------SGAVTGFEGQ 553
Cdd:cd03237 161 FAenNEKTAFVVEHdiimidylADRLIVFEGE 192
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
361-567 |
8.39e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.55 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 361 ARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPA----SGRIMFNGVdmtTLAPEALVA-MTSWIGQKPVL 435
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGK---PVAPCALRGrKIATIMQNPRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 436 FAGTLRENILFARpdATQEQLGAAVAaaaagdfVASLPQGLDTFIGEGGFGLSGGQA--------QRVAIARAFLKDAPL 507
Cdd:PRK10418 91 AFNPLHTMHTHAR--ETCLALGKPAD-------DATLTAALEAVGLENAARVLKLYPfemsggmlQRMMIALALLCEAPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 508 VVLDEPTAHLDPDTEADVFESLRRLAARRT--VILATHS-GAVTGFEGQRIDLAQGHVVTSGE 567
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDmGVVARLADDVAVMSHGRIVEQGD 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
366-417 |
1.02e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.11 E-value: 1.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTL 417
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL 70
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-543 |
1.03e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.38 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQ-----PASGRIMFNG--------------VDMTTLAPEALVAMT 426
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGqdifkmdvielrrrVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 427 SW----IGQKPVLFAGTLREniLFARPDATQEQlgaavaaaaagdfvASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFL 502
Cdd:PRK14247 99 IFenvaLGLKLNRLVKSKKE--LQERVRWALEK--------------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1154151804 503 KDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
349-531 |
1.22e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.19 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 349 VAFEHVSFAWDIARgmAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAL---VAM 425
Cdd:PRK09544 5 VSLENVSVSFGQRR--VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLyldTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 426 TSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAGdfvaslpqgldtfigeggfglsgGQAQRVAIARAFLKDA 505
Cdd:PRK09544 83 PLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSG-----------------------GETQRVLLARALLNRP 139
|
170 180
....*....|....*....|....*....
gi 1154151804 506 PLVVLDEPTAHLDPDTEA---DVFESLRR 531
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQValyDLIDQLRR 168
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
366-530 |
1.24e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.97 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAM-TSWIGQKPVLFAG-TLREN 443
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 ---ILFARPDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGgfglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPD 520
Cdd:PRK10895 99 lmaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGG-------ERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170
....*....|...
gi 1154151804 521 TEAD---VFESLR 530
Cdd:PRK10895 172 SVIDikrIIEHLR 184
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
365-535 |
1.58e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.06 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGfIQPA---SGRIMFNGVDMT-------------------TLAPEAL 422
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKasnirdteragiviihqelTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 423 VAMTSWIGQKPVLFAGTLRENILFARPDATQEQLgaavaaaaagdfvaSLPQGLDTfigEGGFGLSGGQAQRVAIARAFL 502
Cdd:TIGR02633 95 VAENIFLGNEITLPGGRMAYNAMYLRAKNLLREL--------------QLDADNVT---RPVGDYGGGQQQLVEIAKALN 157
|
170 180 190
....*....|....*....|....*....|...
gi 1154151804 503 KDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR 535
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAH 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
344-425 |
1.66e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 344 TGGVAVAFEHVSfAWDIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALV 423
Cdd:COG3845 253 PGEVVLEVENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR 331
|
..
gi 1154151804 424 AM 425
Cdd:COG3845 332 RL 333
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
365-532 |
1.99e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPeALVAM--TSWIGQK-PVLFAGTLR 441
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDH-KLAAQlgIGIIYQElSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 442 ENILFARpDATQEQLGAAVAAAAAGDFVAS-------LPQGLDTFIgeggFGLSGGQAQRVAIARAFLKDAPLVVLDEPT 514
Cdd:PRK09700 99 ENLYIGR-HLTKKVCGVNIIDWREMRVRAAmmllrvgLKVDLDEKV----ANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170
....*....|....*....
gi 1154151804 515 AHLDpDTEAD-VFESLRRL 532
Cdd:PRK09700 174 SSLT-NKEVDyLFLIMNQL 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
365-535 |
2.83e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNG--VDMTTlAPEAL---VAMTS------------ 427
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKS-SKEALengISMVHqelnlvlqrsvm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 428 ---WIGQKPV--LFagtLRENILFARPDATQEQLGAAVAAAaagDFVASLPqgldtfigeggfglsGGQAQRVAIARAFL 502
Cdd:PRK10982 92 dnmWLGRYPTkgMF---VDQDKMYRDTKAIFDELDIDIDPR---AKVATLS---------------VSQMQMIEIAKAFS 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 503 KDAPLVVLDEPTAHLdpdTEADV---FESLRRLAAR 535
Cdd:PRK10982 151 YNAKIVIMDEPTSSL---TEKEVnhlFTIIRKLKER 183
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
367-521 |
3.43e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.07 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAM---TSWIGQKPVLFAG-TLRE 442
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkrMSMLFQSGALFTDmNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 443 NILFARPDATQeqlgaavaaaaagdfvasLPQ--------------GLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLV 508
Cdd:PRK11831 104 NVAYPLREHTQ------------------LPApllhstvmmkleavGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170
....*....|...
gi 1154151804 509 VLDEPTAHLDPDT 521
Cdd:PRK11831 166 MFDEPFVGQDPIT 178
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
491-543 |
3.99e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 51.73 E-value: 3.99e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1154151804 491 QAQRVAIARAfLKDAPLVVL-DEPTAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:COG4598 159 QQQRAAIARA-LAMEPEVMLfDEPTSALDPELVGEVLKVMRDLAEEgRTMLVVTH 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
365-543 |
5.85e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPaGQTLL--------------LCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG 430
Cdd:PRK10575 13 ALRNVSFRVP-GRTLLhplsltfpagkvtgLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 431 QK-PVLFAGTLRENILFARPdATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVV 509
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGRY-PWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154151804 510 LDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLH 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
366-532 |
6.78e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKS----TIIELLlgfiqPA------SGRIMFNGVDMTTLAPEAL-------VAMtsw 428
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHASEQTLrgvrgnkIAM--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 IGQKPV------------------LFAGTLRENilfARPDATQ--EQLGAAVAAAAAGDFVASLPQGldtfigeggfgls 488
Cdd:PRK15134 97 IFQEPMvslnplhtlekqlyevlsLHRGMRREA---ARGEILNclDRVGIRQAAKRLTDYPHQLSGG------------- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154151804 489 ggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRL 532
Cdd:PRK15134 161 --ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
369-543 |
8.37e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 50.74 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 369 VSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP-------------EALVAMTSWIGQKPVL 435
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqlRLLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 436 FAG-TLRENILfarpDATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGG-FGLSGGQAQRVAIARAFLKDAPLVVLDEP 513
Cdd:PRK10619 104 WSHmTVLENVM----EAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190
....*....|....*....|....*....|.
gi 1154151804 514 TAHLDPDTEADVFESLRRLAAR-RTVILATH 543
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEgKTMVVVTH 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
367-547 |
9.52e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 50.45 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASG----------------RIMFNGvdmTTLAPEALVAMTSWIG 430
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtaplaearedtRLMFQD---ARLLPWKKVIDNVGLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 431 QKpvlfaGTLRenilfarpDATQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVL 510
Cdd:PRK11247 106 LK-----GQWR--------DAALQALAAVGLADRANEWPAALSGG---------------QKQRVALARALIHRPGLLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1154151804 511 DEPTAHLDPDTEADVFESLRRLAARR--TVILATH--SGAV 547
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHdvSEAV 198
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
365-407 |
9.79e-07 |
|
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: 49.84 E-value: 9.79e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRI 407
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV 79
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
365-543 |
1.06e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 50.67 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQP----ASGRIMFNGVDMTTLAPEAL-------VAMtswIGQKP 433
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrkiigreIAM---IFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 434 VLF---AGTLRENILFARPDATQE-------------------QLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQ 491
Cdd:COG4170 99 SSCldpSAKIGDQLIEAIPSWTFKgkwwqrfkwrkkraiellhRVGIKDHKDIMNSYPHELTEG---------------E 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154151804 492 AQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgtSILLISH 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
369-543 |
1.11e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.93 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 369 VSFSVPAGQTLLLCGASGSGKSTIIELLLGfIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQK-PVLFAGTLRENILFA 447
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 448 RPDATQEQlgaaVAAAAAGDFVASLpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAP-------LVVLDEPTAHLDPD 520
Cdd:PRK03695 94 QPDKTRTE----AVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDVA 167
|
170 180
....*....|....*....|....
gi 1154151804 521 TEADVFESLRRLAAR-RTVILATH 543
Cdd:PRK03695 168 QQAALDRLLSELCQQgIAVVMSSH 191
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
491-546 |
1.43e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.84 E-value: 1.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154151804 491 QAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGA 546
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPA 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
366-543 |
1.58e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFnGVDM---------TTLAPEALVAMTSWIGQKPVLF 436
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLevayfdqhrAELDPEKTVMDNLAEGKQEVMV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 437 AGTLR------ENILFARPDATQEqlgaavaaaaagdfVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVL 510
Cdd:PRK11147 414 NGRPRhvlgylQDFLFHPKRAMTP--------------VKALSGG---------------ERNRLLLARLFLKPSNLLIL 464
|
170 180 190
....*....|....*....|....*....|....*
gi 1154151804 511 DEPTAHLDPDTeadvFESLRRLAA--RRTVILATH 543
Cdd:PRK11147 465 DEPTNDLDVET----LELLEELLDsyQGTVLLVSH 495
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
368-540 |
1.69e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.82 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEA-------------------LVAMTSW 428
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarglvylpedrqssglyLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 429 -----IGQKPVLFAGTLRENILFAR---------PDATQEqlgaavaaaaagdfVASLPQGldtfigeggfglsggQAQR 494
Cdd:PRK15439 361 nvcalTHNRRGFWIKPARENAVLERyrralnikfNHAEQA--------------ARTLSGG---------------NQQK 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1154151804 495 VAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVIL 540
Cdd:PRK15439 412 VLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVL 457
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
365-543 |
1.94e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 50.57 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGF--IQPASGRIMFNgvdmTTLAPEAL-VAMTSWIGQKPVLFAGTLR 441
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYH----VALCEKCGyVERPSKVGEPCPVCGGTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 442 -ENILFARPDAT-------------QEQLGAAVAAAAAGDFVASLPQ-------------------GLDTFIGEGGFGLS 488
Cdd:TIGR03269 91 pEEVDFWNLSDKlrrrirkriaimlQRTFALYGDDTVLDNVLEALEEigyegkeavgravdliemvQLSHRITHIARDLS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 489 GGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSH 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
351-519 |
2.50e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 351 FEHVSFAWDiARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIG 430
Cdd:PRK10522 325 LRNVTFAYQ-DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 431 QKPVLFAGTLRENILFARPDATQ---EQLGAAVAAAAAGDFVA--SLPQGldtfigeggfglsggQAQRVAIARAFLKDA 505
Cdd:PRK10522 404 TDFHLFDQLLGPEGKPANPALVEkwlERLKMAHKLELEDGRISnlKLSKG---------------QKKRLALLLALAEER 468
|
170
....*....|....
gi 1154151804 506 PLVVLDEPTAHLDP 519
Cdd:PRK10522 469 DILLLDEWAADQDP 482
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
365-569 |
2.58e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.72 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLaPEALVaMTSWIGQKP----VLFAGTL 440
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW-QTAKI-MREAVAIVPegrrVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENI----LFARPDATQEQLgaavaaaaagDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAH 516
Cdd:PRK11614 98 EENLamggFFAERDQFQERI----------KWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154151804 517 LDPDTEADVFESLRRLAARRTVILATHSGAvtgfeGQRIDLA-QGHVVTSGEKV 569
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQNA-----NQALKLAdRGYVLENGHVV 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
364-543 |
2.71e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.83 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 364 MAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLaPEALVAMTSWIG--QKPVLFAG-TL 440
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMGVVRtfQHVRLFREmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENI---------------LFARPDATQEQLGAAVAAAAAGDFVaslpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDA 505
Cdd:PRK11300 98 IENLlvaqhqqlktglfsgLLKTPAFRRAESEALDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154151804 506 PLVVLDEPTAHLDPDTEADVFESLRRLaaRR----TVILATH 543
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAEL--RNehnvTVLLIEH 212
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
366-543 |
3.64e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.94 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKP--VLFAGTLREN 443
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 444 ILFArpdatQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEA 523
Cdd:PRK13642 103 VAFG-----MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180
....*....|....*....|..
gi 1154151804 524 DVFESLRRLAARR--TVILATH 543
Cdd:PRK13642 178 EIMRVIHEIKEKYqlTVLSITH 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
493-543 |
3.67e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 3.67e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 493 QRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
359-542 |
3.81e-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: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 359 DIARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEAlvAMTSWIG-------Q 431
Cdd:COG1129 261 GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD--AIRAGIAyvpedrkG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 432 KPVLFAGTLRENILFarpdATQEQLGAAVA------AAAAGDFVASL---PQGLDTFIgeggfglsggQA------QRVA 496
Cdd:COG1129 339 EGLVLDLSIRENITL----ASLDRLSRGGLldrrreRALAEEYIKRLrikTPSPEQPV----------GNlsggnqQKVV 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154151804 497 IARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILAT 542
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVIS 451
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
59-262 |
3.82e-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: 48.97 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 59 VVAWPLAGLVGLAVARAGLQAASDTLAARAGMKGRARLRGGVIEAIMRGGPGLLRQHHTGELTALAVDRIEALDGFFARW 138
Cdd:cd18551 34 SSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 139 LPASVLWVAAPLVIGVLAAFVQPGSALIMAVCGIAVPFGQALFGIGAAVASRNQFLAMTRLQARFLDRVRGIATIVLSGR 218
Cdd:cd18551 114 LPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154151804 219 TEDETRRLAASAEELRLRTMKVLRVAFLSSASIDCAMVVALVLV 262
Cdd:cd18551 194 EERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
361-566 |
4.44e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.38 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 361 ARGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTL----APEA---LVAMTSW--IGQ 431
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyaLSEAerrRLLRTEWgfVHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 432 KPvlfAGTLRENI---------LFA---------RPDATQEQLGAAVAAAAAGDFVASLPQGLDtfigeggfglsggqaQ 493
Cdd:PRK11701 97 HP---RDGLRMQVsaggnigerLMAvgarhygdiRATAGDWLERVEIDAARIDDLPTTFSGGMQ---------------Q 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154151804 494 RVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATHSGAVTGFEGQRI-DLAQGHVVTSG 566
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLlVMKQGRVVESG 234
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
493-560 |
4.80e-06 |
|
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: 47.18 E-value: 4.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 493 QRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLA--ARRTVILATHSGAVTGFEGQRIDLAQG 560
Cdd:cd03222 78 QRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
365-543 |
5.68e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGF----IQPASGRIMFNGVDMTTLAPEA---LVAMT-SWIGQKPV-- 434
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRErrkLVGHNvSMIFQEPQsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 435 ------------------LFAGTLRENILFARPDATQ--EQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQR 494
Cdd:PRK15093 102 ldpservgrqlmqnipgwTYKGRWWQRFGWRKRRAIEllHRVGIKDHKDAMRSFPYELTEG---------------ECQK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 495 VAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISH 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
493-543 |
6.02e-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: 49.01 E-value: 6.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 493 QRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATH 543
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDH 514
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
368-544 |
6.53e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPA-GQTLLLcGASGSGKSTIIELLLGFIQPASGRIMFNG---VDMTT---LAPEalvamTSWIG---QKPVLFA 437
Cdd:PRK11144 16 TVNLTLPAqGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPE-----KRRIGyvfQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 438 G-TLRENILFARPDATQEQLgaavaaaaagDFVASLpQGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAH 516
Cdd:PRK11144 90 HyKVRGNLRYGMAKSMVAQF----------DKIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190
....*....|....*....|....*....|
gi 1154151804 517 LDPDTEADVFESLRRLAAR-RTVIL-ATHS 544
Cdd:PRK11144 159 LDLPRKRELLPYLERLAREiNIPILyVSHS 188
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
376-543 |
7.13e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.11 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 376 GQTLLLCGASGSGKSTIIELLLGFIQPAS--GRIMFNGVDMTtlapEALVAMTSWIGQKPVLFAG-TLRENILFARPDAT 452
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFVTQDDILYPHlTVRETLVFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 453 QEQLGAAVAAAAAGDFVASLpqGL---------DTFIGEGGFGlsggQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEA 523
Cdd:PLN03211 170 PKSLTKQEKILVAESVISEL--GLtkcentiigNSFIRGISGG----ERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180
....*....|....*....|.
gi 1154151804 524 DVFESLRRLAAR-RTVILATH 543
Cdd:PLN03211 244 RLVLTLGSLAQKgKTIVTSMH 264
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
366-544 |
7.18e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPeaLVAMTSWIGqkpvLFAGTLRENIL 445
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKKGMA----YITESRRDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 446 F-----ARPDATQEQLGAAVAAAAAGDFVASLPQGLD-----------TFIGEGGFGLSGGQAQRVAIARAFLKDAPLVV 509
Cdd:PRK09700 353 FpnfsiAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAenqrellalkcHSVNQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190
....*....|....*....|....*....|....*
gi 1154151804 510 LDEPTAHLDPDTEADVFESLRRLAARRTVILATHS 544
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSS 467
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
351-551 |
7.26e-06 |
|
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: 46.85 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 351 FEHVSFAWDIARG--MAVDDVSFSVPAGQTLLLCGASGSGKSTIIELL-----LGFIqpaSGRIMFNGVDMttlaPEALV 423
Cdd:cd03232 6 WKNLNYTVPVKGGkrQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILINGRPL----DKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 424 AMTSWIGQKPVLFAG-TLRENILFArpdatqeqlgaavaaaaagdfvASLpQGLDTfigeggfglsgGQAQRVAIARAFL 502
Cdd:cd03232 79 RSTGYVEQQDVHSPNlTVREALRFS----------------------ALL-RGLSV-----------EQRKRLTIGVELA 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154151804 503 KDAPLVVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATHSGAVTGFE 551
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSgQAILCTIHQPSASIFE 174
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
365-567 |
7.34e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.20 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQpASGRIM-----FNGVDMTTLAPE-------ALVAMtswIGQK 432
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaekleFNGQDLQRISEKerrnlvgAEVAM---IFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 433 P-------------------VLFAGTLRENIlfARPDATQEQLGAAVAAAAAGDFVASLPQGLdtfigeggfglsggqAQ 493
Cdd:PRK11022 98 PmtslnpcytvgfqimeaikVHQGGNKKTRR--QRAIDLLNQVGIPDPASRLDVYPHQLSGGM---------------SQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 494 RVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARR--TVILATHSGAVTGFEGQR-IDLAQGHVVTSGE 567
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAEAAHKiIVMYAGQVVETGK 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
365-425 |
7.79e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 7.79e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAM 425
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAL 399
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
348-544 |
8.42e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.72 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAWDIARgmAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPAS-----GRIMFNGVDM--TTLAPE 420
Cdd:PRK14258 7 AIKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 421 ALVAMTSWIGQKPVLFAGTLRENILFA------RPDATQEQLGAAVAAAaagdfvASLPQGLDTFIGEGGFGLSGGQAQR 494
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 495 VAIARAFLKDAPLVVLDEPTAHLDPDTEADVfESL---RRLAARRTVILATHS 544
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKV-ESLiqsLRLRSELTMVIVSHN 210
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
495-544 |
1.71e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 47.00 E-value: 1.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1154151804 495 VAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRT-VILATHS 544
Cdd:pfam13304 248 LAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTHS 298
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
493-547 |
2.23e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 2.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1154151804 493 QRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHSGAV 547
Cdd:PRK13409 219 QRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAV 273
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-326 |
2.57e-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: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 24 MPVVLLGLAISAIAVGQVWCIATALAcVLVPGGMPVVAWPLAGLVGLA-VARAGLQAASDTLAARAGMKGRARLRGGVIE 102
Cdd:cd18565 17 APPLLIGVAIDAVFNGEASFLPLVPA-SLGPADPRGQLWLLGGLTVAAfLLESLFQYLSGVLWRRFAQRVQHDLRTDTYD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 103 AIMRGGPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLAAFVQPGSALIMAVcgiAVPFgqalfg 182
Cdd:cd18565 96 HVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALL---PVPL------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 183 IGAAVasrnqFLAMTRLQARFlDRVR---------------GIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLS 247
Cdd:cd18565 167 IIAGT-----YWFQRRIEPRY-RAVReavgdlnarlennlsGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 248 SASIDCAMVVALVLVALRNGAHLMDlheqGVPAaiMAGQVARGLFVVLVV--PEFFAPFRSLAL---AYQDrahasGAAS 322
Cdd:cd18565 241 FPVIRLVAGAGFVATFVVGGYWVLD----GPPL--FTGTLTVGTLVTFLFytQRLLWPLTRLGDlidQYQR-----AMAS 309
|
....
gi 1154151804 323 AMRI 326
Cdd:cd18565 310 AKRV 313
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
365-549 |
3.58e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 46.26 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIqPASGRI----MFNGVDMTTLAPEAL-------VAMtswIGQKP 433
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGREILNLPEKELnklraeqISM---IFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 434 VLfagTLreNILFARPDATQEQLGAAVAAAAAGDFVASLpQGLDTF--------IGEGGFGLSGGQAQRVAIARAFLKDA 505
Cdd:PRK09473 107 MT---SL--NPYMRVGEQLMEVLMLHKGMSKAEAFEESV-RMLDAVkmpearkrMKMYPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154151804 506 PLVVLDEPTAHLDPDTEADVFESLRRLaaRR----TVILATHS-GAVTG 549
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNEL--KRefntAIIMITHDlGVVAG 227
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
380-544 |
4.02e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 45.73 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 380 LLCGASGSGKSTIIELLLGFIQ------PASgRIMFngvdmtTLAPEALVAMTSWIGQKPVLFAGTLREN----ILFARP 449
Cdd:COG4938 24 LLIGPNGSGKSTLIQALLLLLQsnfiylPAE-RSGP------ARLYPSLVRELSDLGSRGEYTADFLAELenleILDDKS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 450 DATQEQLGAAVAAAAAGDFVASLPQGLDTFIGEGGFGLSGG------QAQR------VAIARAFlKDAPLVVLDEPTAHL 517
Cdd:COG4938 97 KELLEQVEEWLEKIFPGKVEVDASSDLVRLVFRPSGNGKRIplsnvgSGVSellpilLALLSAA-KPGSLLIIEEPEAHL 175
|
170 180
....*....|....*....|....*...
gi 1154151804 518 DPDTEADVFESLRRLAAR-RTVILATHS 544
Cdd:COG4938 176 HPKAQSALAELLAELANSgVQVIIETHS 203
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
27-262 |
4.31e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 45.55 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 27 VLLGLAISAIAVGQVWCIATALACVLVPGGMPVVAWPLAGLVGLAVARAGLQAASDTLAARAGMKGRARLRGGVIEAIMR 106
Cdd:cd18543 5 LLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 107 GGPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLaAFVQPGSALIMAVCGIAVpfgqalfgIGAA 186
Cdd:cd18543 85 LDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVM-LVLSPPLALVALASLPPL--------VLVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 187 VASRNQFLAMTRL-QARFLD-------RVRGIATIVLSGRTEDETRRLAASAEELRLRTMKVLRVAFLSSASIDCAMVVA 258
Cdd:cd18543 156 RRFRRRYFPASRRaQDQAGDlatvveeSVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELG 235
|
....
gi 1154151804 259 LVLV 262
Cdd:cd18543 236 LAAV 239
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
366-543 |
4.96e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 45.07 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAG-TLRENI 444
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHINSRlTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 445 LFAR-P-----------DATQEQLGAAVAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDE 512
Cdd:COG4604 97 AFGRfPyskgrltaedrEIIDEAIAYLDLEDLADRYLDELSGG---------------QRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190
....*....|....*....|....*....|...
gi 1154151804 513 PTAHLDPDTEADVFESLRRLA--ARRTVILATH 543
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLH 194
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
63-312 |
5.18e-05 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 45.16 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 63 PLAGLVGLAVARAGLQAASDTLAARAGMKGRARLRGGVIEAIMRGGPGLLRQHHTGELTALAVDRIEALDGFFARWL-PA 141
Cdd:cd18585 37 PAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLsPP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 142 SVLWVAAPLVIGVLAAFvQPGSALIMAVC----GIAVPfgqALFGIGAAVASRNQFLAMTRLQARFLDRVRGIATIVLSG 217
Cdd:cd18585 117 VVALLVILATILFLAFF-SPALALILLAGlllaGVVIP---LLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 218 RTEDETRRLAAS-----AEELRLRTMKVLRVAfLSSASIDCAMVVALVLVALRNGAHLMDlheqGVPAAIMAgqvarglF 292
Cdd:cd18585 193 ALERQRQQLEQLsdaliKEQRRLARLSGLSQA-LMILLSGLTVWLVLWLGAPLVQNGALD----GALLAMLV-------F 260
|
250 260
....*....|....*....|
gi 1154151804 293 VVLVVPEFFAPfrsLALAYQ 312
Cdd:cd18585 261 AVLASFEAVAP---LPLAFQ 277
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
365-535 |
5.23e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMT-------------------TLAPEALVAM 425
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqeagigiihqelNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 426 TSWIGQKPVLFAGTLRENILFARPDATQEQLGAAVAAAAAgdfVASLPQGldtfigeggfglsggQAQRVAIARAFLKDA 505
Cdd:PRK10762 99 NIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKL---VGELSIG---------------EQQMVEIAKVLSFES 160
|
170 180 190
....*....|....*....|....*....|.
gi 1154151804 506 PLVVLDEPTAHL-DPDTEAdVFESLRRLAAR 535
Cdd:PRK10762 161 KVIIMDEPTDALtDTETES-LFRVIRELKSQ 190
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
345-407 |
6.21e-05 |
|
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: 45.70 E-value: 6.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 345 GGVAVAFEHVSFAWDiaRGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRI 407
Cdd:TIGR03719 319 GDKVIEAENLTKAFG--DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
494-543 |
7.29e-05 |
|
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: 44.14 E-value: 7.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1154151804 494 RVAIARAFLKDAPLVVLDEPTAHLDPDTE----ADVFESLRRLAARRtVILATH 543
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEENIeeslAEIIEERKSQKNFQ-LIVITH 181
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
368-544 |
7.95e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 44.65 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQ------PASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLFAG-TL 440
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHlSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENILFA-RPDATQEQLGAAVAAAAAGDFVASLPQGLDTfIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDP 519
Cdd:PRK14246 108 YDNIAYPlKSHGIKEKREIKKIVEECLRKVGLWKEVYDR-LNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI 186
|
170 180
....*....|....*....|....*
gi 1154151804 520 DTEADVFESLRRLAARRTVILATHS 544
Cdd:PRK14246 187 VNSQAIEKLITELKNEIAIVIVSHN 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
367-541 |
8.08e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.59 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMTSWIGQKPVLfAGTLRENILF 446
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT-PGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 447 ARPDATQEQLgAAVAAAAAGDFVASLPQ--GLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEAD 524
Cdd:PRK10253 103 ARGRYPHQPL-FTRWRKEDEEAVTKAMQatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170
....*....|....*..
gi 1154151804 525 VFESLRRLAARRTVILA 541
Cdd:PRK10253 182 LLELLSELNREKGYTLA 198
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
367-568 |
1.08e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 43.90 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 367 DDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFI--QPASGRIMFNGVDMTTLAPE--AL----VAMtswigQKPVLFAG 438
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDerARagifLAF-----QYPVEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 439 -TLREnilFARpDATQEQLGAAVAAAaagDFVASLPQgldtfigeggfglsggQAQRVAIARAFLK-------------- 503
Cdd:COG0396 92 vSVSN---FLR-TALNARRGEELSAR---EFLKLLKE----------------KMKELGLDEDFLDryvnegfsggekkr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 504 ---------DAPLVVLDEPTAHLDPDTEADVFESLRRLAAR-RTVILATHSgavtgfegQRI------D----LAQGHVV 563
Cdd:COG0396 149 neilqmlllEPKLAILDETDSGLDIDALRIVAEGVNKLRSPdRGILIITHY--------QRIldyikpDfvhvLVDGRIV 220
|
....*
gi 1154151804 564 TSGEK 568
Cdd:COG0396 221 KSGGK 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
344-544 |
1.09e-04 |
|
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: 44.82 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 344 TGGVAVAFEHVSfAWDIA--RGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPA-SGRIMFNGVDMTTLAP- 419
Cdd:TIGR02633 253 IGDVILEARNLT-CWDVInpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPa 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 420 ---EALVAMTSWIGQK----PVLFAGtlrENILFA---------RPDATQEQ--LGAAVAAAAAGDFVASLPQGldtfig 481
Cdd:TIGR02633 332 qaiRAGIAMVPEDRKRhgivPILGVG---KNITLSvlksfcfkmRIDAAAELqiIGSAIQRLKVKTASPFLPIG------ 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 482 eggfGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHS 544
Cdd:TIGR02633 403 ----RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSS 461
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
468-543 |
1.42e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 468 FVASLPQGLDTFigEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTAHLDPDTE---ADVFE-SLRRLAARRTVILATH 543
Cdd:PRK01156 791 SRGGMVEGIDSL--SGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRtnlKDIIEySLKDSSDIPQVIMISH 868
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
365-411 |
2.71e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 2.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGfIQPA---SGRIMFNG 411
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDG 64
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
493-535 |
3.44e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 43.62 E-value: 3.44e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1154151804 493 QRVAIARAFLKDAPLVVLDEPTAHLdpdteaDVFESLRrlAAR 535
Cdd:COG1245 219 QRVAIAAALLRDADFYFFDEPSSYL------DIYQRLN--VAR 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
365-544 |
3.93e-04 |
|
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: 43.46 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAPEALVAMtswiGQKPVLFA----GTL 440
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM----GYCPQFDAiddlLTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 441 RENI-LFAR----PDATQEQLGAAVaaaaagdfVASLpqGLDTFIGEGGFGLSGGQAQRVAIARAFLKDAPLVVLDEPTA 515
Cdd:TIGR01257 2030 REHLyLYARlrgvPAEEIEKVANWS--------IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190
....*....|....*....|....*....|
gi 1154151804 516 HLDPDTEADVFESLRRLAAR-RTVILATHS 544
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSIIREgRAVVLTSHS 2129
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
503-547 |
4.80e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.68 E-value: 4.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1154151804 503 KDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRT-VILATHSGAV 547
Cdd:COG3593 186 PANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNqVIITTHSPHL 231
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
365-421 |
5.85e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.11 E-value: 5.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvDMTTLAPEA 421
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISA 94
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
368-543 |
9.03e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFsvPAGQTLLLCGASGSGKSTIIE---LLLGFIQPASGRIMFNGVDmttlAPEALVAMTswigqkpvlfagtlrenI 444
Cdd:cd03227 15 DVTF--GEGSLTIITGPNGSGKSTILDaigLALGGAQSATRRRSGVKAG----CIVAAVSAE-----------------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 445 LFARPdatqeqlgaavaaaaagdfvaSLPQGldtfigeggfglsggQAQRVAIARAF----LKDAPLVVLDEPTAHLDPD 520
Cdd:cd03227 72 IFTRL---------------------QLSGG---------------EKELSALALILalasLKPRPLYILDEIDRGLDPR 115
|
170 180
....*....|....*....|....
gi 1154151804 521 TEADVFESLRRLAA-RRTVILATH 543
Cdd:cd03227 116 DGQALAEAILEHLVkGAQVIVITH 139
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
345-407 |
1.01e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 1.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 345 GGVAVAFEHVSFAWDiARgMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRI 407
Cdd:PRK11819 321 GDKVIEAENLSKSFG-DR-LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
348-407 |
1.06e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 348 AVAFEHVSFAWDiaRGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRI 407
Cdd:PRK15064 319 ALEVENLTKGFD--NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
365-427 |
1.11e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 1.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154151804 365 AVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGvdmttlaPEALVAMTS 427
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------SAALIAISS 94
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
506-544 |
1.31e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1154151804 506 PLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATHS 544
Cdd:COG4637 280 PLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHS 318
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
366-542 |
1.49e-03 |
|
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: 39.94 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 366 VDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPA---SGRIMFNGVDMTTLA--PEALVAMTSwigQKPVLFAG-T 439
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAekYPGEIIYVS---EEDVHFPTlT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 440 LRENILFArpdatqeqlgaavAAAAAGDFVASLPQGldtfigeggfglsggQAQRVAIARAFLKDAPLVVLDEPTAHLDP 519
Cdd:cd03233 100 VRETLDFA-------------LRCKGNEFVRGISGG---------------ERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180
....*....|....*....|....
gi 1154151804 520 DTEADVFESLRRLA-ARRTVILAT 542
Cdd:cd03233 152 STALEILKCIRTMAdVLKTTTFVS 175
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
28-272 |
2.41e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 40.19 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 28 LLGLAISAIAVGQVWCIATALACVLVPGGMPVVAWPLAGLVGLAVARAGLQAASDTLAARAGMKGRARLRGGVIEAIMRG 107
Cdd:cd18564 21 PLKVVIDDVLGDKPLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 108 GPGLLRQHHTGELTALAVDRIEALDGFFARWLPASVLWVAAPLVIGVLAAFVQPGSALIMAVcgiAVPfgqaLFGIGAAV 187
Cdd:cd18564 101 SLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALA---VAP----LLLLAARR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 188 ASRnQFLAMTRLQARFLDRVRGIATIVLS--------GRTEDETRRLAASAEELRLRTMKVLRVAFLSSASIDCAMVVAL 259
Cdd:cd18564 174 FSR-RIKEASREQRRREGALASVAQESLSairvvqafGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGT 252
|
250
....*....|...
gi 1154151804 260 VLVALRNGAHLMD 272
Cdd:cd18564 253 ALVLWFGAWLVLA 265
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
494-543 |
3.88e-03 |
|
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: 39.92 E-value: 3.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1154151804 494 RVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAArrTVILATH 543
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
492-543 |
4.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1154151804 492 AQRVAIARAFLKDAPLVVLDEPTAHLDPDTEADVFESLRRLAARRTVILATH 543
Cdd:COG4717 570 ALRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTC 621
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
345-518 |
6.09e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.22 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 345 GGVAVAFEHVSfawdiarGMAVDDVSFSVPAGQTLLLCGASGSGKSTIIELLLGFIQPASGRIMFNGVDMTTLAP-EALV 423
Cdd:PRK10762 254 GEVRLKVDNLS-------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqDGLA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 424 AMTSWI-----GQKPVLfAGTLRENI-LFARPDATQE--QLGAAVAAAAAGDFV-------ASLPQ--GLdtfigeggfg 486
Cdd:PRK10762 327 NGIVYIsedrkRDGLVL-GMSVKENMsLTALRYFSRAggSLKHADEQQAVSDFIrlfniktPSMEQaiGL---------- 395
|
170 180 190
....*....|....*....|....*....|..
gi 1154151804 487 LSGGQAQRVAIARAFLKDAPLVVLDEPTAHLD 518
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
368-457 |
6.64e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.47 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLLLCGASGSGKSTIIELLLGfiQPA----SGRIMFNGVDMTTLAPEALVAMTSWIG-QKPVLFAGTLRE 442
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAHLGIFLAfQYPIEIPGVSNA 102
|
90
....*....|....*
gi 1154151804 443 NILFARPDATQEQLG 457
Cdd:CHL00131 103 DFLRLAYNSKRKFQG 117
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
494-521 |
8.78e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.78 E-value: 8.78e-03
10 20
....*....|....*....|....*...
gi 1154151804 494 RVAIARAFLKDAPLVVLDEPTAHLDPDT 521
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
368-520 |
9.89e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 368 DVSFSVPAGQTLL--------------LCGASGSGKSTIIELLLGFIQPASGRIMFNG-VDMTTLAPEALVAMTswIGQK 432
Cdd:PLN03073 513 DASFGYPGGPLLFknlnfgidldsriaMVGPNGIGKSTILKLISGELQPSSGTVFRSAkVRMAVFSQHHVDGLD--LSSN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154151804 433 PVLFagtlrenILFARPDATQEQLgaavaAAAAGDFVASLPQGLDTFIGEGGFglsggQAQRVAIARAFLKDAPLVVLDE 512
Cdd:PLN03073 591 PLLY-------MMRCFPGVPEQKL-----RAHLGSFGVTGNLALQPMYTLSGG-----QKSRVAFAKITFKKPHILLLDE 653
|
....*...
gi 1154151804 513 PTAHLDPD 520
Cdd:PLN03073 654 PSNHLDLD 661
|
|
| |
