|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-557 |
1.24e-116 |
|
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: 371.62 E-value: 1.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 12 RRALVLLGVLAAAKAVGLALVAQGVASGLAALAAGAVRPGVLSAATLVAAAGVLLRAAAEWGTSTVGRWAAVGVKEELRS 91
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 92 QLLEAALEGgaapasaagpvddGAARVASSPAATAV-LAGRGLDGLDALYTQYLPALVQTAVLPLLVGARILGADWVSAL 170
Cdd:TIGR02857 82 RLLEAVAAL-------------GPRWLQGRPSGELAtLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 171 ILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKGRTMATLRVAF 250
Cdd:TIGR02857 149 ILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 251 LSALALELISTISVAVVAVFIGIRLVHGDMTLEAGLLALILAPECFQPLRDLGTAHHASEDG---AEALRRTRARIGAPr 327
Cdd:TIGR02857 229 LSSAVLELFATLSVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGvaaAEALFAVLDAAPRP- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 328 gtvllaaghgrvqDAERPPAGQAAPAGLRVAGLTVWYDGaAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR 407
Cdd:TIGR02857 308 -------------LAGKAPVTAAPASSLEFSGVSVAYPG-RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 408 DGVGASVRGSVDGPD------PRRIAWVPQHPQFSERTVAAELALYAGAAGEGAVPG---EPGALVRELLDQLGLGGLEA 478
Cdd:TIGR02857 374 PTEGSIAVNGVPLADadadswRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREaleRAGLDEFVAALPQGLDTPIG 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 479 ADPAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:TIGR02857 454 EGGAGLSGGQAQRLALARAFLR---DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-557 |
4.63e-110 |
|
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: 355.22 E-value: 4.63e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 7 LGPTSRRALVLLGVLAAAKAVGLALVAQGVASGLAALAAGAVRPGVLSAATLVAAAGVLLRAAAEWGTSTVGRWAAVGVK 86
Cdd:COG4988 11 LARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 87 EELRSQLLEAALEGgaapasaagpvddGAARVASSPAATAV-LAGRGLDGLDALYTQYLPALVQTAVLPLLVGARILGAD 165
Cdd:COG4988 91 RRLRRRLLEKLLAL-------------GPAWLRGKSTGELAtLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 166 WVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKGRTMAT 245
Cdd:COG4988 158 WLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 246 LRVAFLSALALELISTISVAVVAVFIGIRLVHGDMTLEAGLLALILAPECFQPLRDLGTAHHASEDGAEALRRTRAriga 325
Cdd:COG4988 238 LRVAFLSSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFA---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 326 prgtvLLAAGHGRVQDAERPPAGQAAPAgLRVAGLTVWYDGaAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGL 405
Cdd:COG4988 314 -----LLDAPEPAAPAGTAPLPAAGPPS-IELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 406 VRDGVGaSVRgsVDGPDP---------RRIAWVPQHPQFSERTVAAELALYAGAAGEgavpgepgALVRELLDQLGLGGL 476
Cdd:COG4988 387 LPPYSG-SIL--INGVDLsdldpaswrRQIAWVPQNPYLFAGTIRENLRLGRPDASD--------EELEAALEAAGLDEF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 477 EAADP-----------AELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEP 545
Cdd:COG4988 456 VAALPdgldtplgeggRGLSGGQAQRLALARALLR---DAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRL 532
|
570
....*....|..
gi 1001866046 546 RTAALADRTVEL 557
Cdd:COG4988 533 ALLAQADRILVL 544
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
627-1122 |
1.81e-94 |
|
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: 313.24 E-value: 1.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 627 TLSGWLIVRASEQPPILYLLTAITGVRFFGIARAVLRYRERLVLHSAVLSTLTELRERLWALLSVRGLSARRLLVPGAAL 706
Cdd:COG4987 36 ALSGWLIAAAALAPPILNLFVPIVGVRAFAIGRTVFRYLERLVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 707 EALVGDAEAVRDQLPRVLAPITTAVLVAAGALVAVQILLPAQTPVLAAAVVVALVAAPAVARAADRRAAARSQAGRASLL 786
Cdd:COG4987 116 NRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 787 ARMGQALAAGPDLRANGRAGAVLRSIRSADAALTRLERRGAAAEGLAHAIVVAATGAAAALTLGAAQAAGAPAATAAAVL 866
Cdd:COG4987 196 ARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 867 LLQLALAE----PLAAASTAVQQLPALRSALVRVAAEEQAVRDAAEERDDLqdAPGRGPGITLRGVTVGWTGGP-DVLAG 941
Cdd:COG4987 276 ALLVLAALalfeALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPA--PAPGGPSLELEDVSFRYPGAGrPVLDG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 942 LDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS-------------AAVAGPVAWCPQESHLFDSTVRGNLAVAR 1008
Cdd:COG4987 354 LSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSitlggvdlrdldeDDLRRRIAVVPQRPHLFDTTLRENLRLAR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1009 DrdhAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLAL 1088
Cdd:COG4987 434 P---DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL 510
|
490 500 510
....*....|....*....|....*....|....
gi 1001866046 1089 VAALHGALADRTVVMVTHHATELMPGDTLVRLGA 1122
Cdd:COG4987 511 LADLLEALAGRTVLLITHRLAGLERMDRILVLED 544
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
594-1107 |
4.89e-89 |
|
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: 297.35 E-value: 4.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 594 LRTLASLLGPDAGTYARAALAGLGAAAAAVALSTLSGWLIVRASEQPPILYLLTAITGVRFFGIARAVLRYRERLVLHSA 673
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLYLSVAAVAVRAFGIGRAVFRYLERLVGHDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 674 VLSTLTELRERLWALLSVRGLSARRLLVPGAALEALVGDAEAVRDQLPRVLAPITTAVLVAAGALVAVQILLPAQTPVLA 753
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 754 AAVVVALVAAPAVARAADRRAAARSQAGRASLLARMGQALAAGPDLRANGRAGAVLRSIRSADAALTRLERRGAAAEGLA 833
Cdd:TIGR02868 161 AGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 834 HAIVVAATGAAAALTLGAAQAAGAPAATAAAVLLLQLALAEPL----AAASTAVQQLPALRSALVRVAAEEQAVRDAAEE 909
Cdd:TIGR02868 241 AALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAfeafAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 910 RDDLQ-DAPGRGPGITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP--- 985
Cdd:TIGR02868 321 SAPAAgAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvs 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 986 ----------VAWCPQESHLFDSTVRGNLAVARDRdhaPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQR 1055
Cdd:TIGR02868 401 sldqdevrrrVSVCAQDAHLFDTTVRENLRLARPD---ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGER 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 1056 QRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHH 1107
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
16-318 |
1.27e-79 |
|
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: 262.73 E-value: 1.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 16 VLLGVLAAAKAVGLALVAQGVASGLAALAAgavrpgvLSAATLVAAAGVLLRAAAEWGTSTVGRWAAVGVKEELRSQLLE 95
Cdd:cd18584 6 LLAALLIIAQAWLLARIIAGVFLEGAGLAA-------LLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 96 AALEGgaapasaagpvdDGAARVASSPAATAVLAGRGLDGLDALYTQYLPALVQTAVLPLLVGARILGADWVSALILVLT 175
Cdd:cd18584 79 RLLAL------------GPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 176 LPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKGRTMATLRVAFLSALA 255
Cdd:cd18584 147 APLIPLFMILIGKAAQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAV 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 256 LELISTISVAVVAVFIGIRLVHGDMTLEAGLLALILAPECFQPLRDLGTAHHASEDGAEALRR 318
Cdd:cd18584 227 LEFFATLSIALVAVYIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAER 289
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
61-543 |
1.28e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 215.86 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 61 AAGVLLRAAAEWGTSTVGRWAAVGVKEELRSQLLE--AALeggaapasaagpvddGAARVASSPAAT-AVLAGRGLDGLD 137
Cdd:PRK11174 70 ILLFVLRALLAWLRERVGFKAGQHIRQQIRQQVLDklQQL---------------GPAWIQGKPAGSwATLVLEQVEDMH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 138 ALYTQYLPALVQTAVLPLLVGARILGADWVSALILVLTLPLVPVFMILIGrhtlEAVAEAQQ----SLLRLGSHLVELAQ 213
Cdd:PRK11174 135 DFYARYLPQMALAVLVPLLILIAVFPINWAAGLILLGTAPLIPLFMALVG----MGAADANRrnflALARLSGHFLDRLR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 214 GLPVLVGLGRAAEQRRALGELSRAYKGRTMATLRVAFLSALALELISTISVAVVAVFIGI----RLVHGD----MTLEAG 285
Cdd:PRK11174 211 GLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASISIALVAVYFGFsylgELNFGHygtgVTLFAG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 286 LLALILAPECFQPLRDLGTAHHASedgAEAlrrtrarIGAPRGTV-LLAAGHGRVQDAERPPAGQaAPAGLRVAGLTVW- 363
Cdd:PRK11174 291 FFVLILAPEFYQPLRDLGTFYHAK---AQA-------VGAAESLVtFLETPLAHPQQGEKELASN-DPVTIEAEDLEILs 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 364 YDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLvrdgvgASVRGS--VDGP-----DP----RRIAWVPQH 432
Cdd:PRK11174 360 PDGK--TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF------LPYQGSlkINGIelrelDPeswrKHLSWVGQN 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 433 PQFSERTVAAELALYAGAAGEGAVpgePGAL--------VRELLDQLGLGGLEAAdpAELSPGQQRRVAVARGLARVADg 504
Cdd:PRK11174 432 PQLPHGTLRDNVLLGNPDASDEQL---QQALenawvsefLPLLPQGLDTPIGDQA--AGLSVGQAQRLALARALLQPCQ- 505
|
490 500 510
....*....|....*....|....*....|....*....
gi 1001866046 505 agLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSH 543
Cdd:PRK11174 506 --LLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTH 542
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
897-1120 |
9.22e-55 |
|
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: 200.75 E-value: 9.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 897 AAEE-QAVRDAAEE---RDDLQDAPGRGPGITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGF 972
Cdd:COG4988 307 AAEKiFALLDAPEPaapAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 973 LAPRVGSAAVAGP-------------VAWCPQESHLFDSTVRGNLAVARdrdHAPSDAELEAVLARVGLLEHVRSLPGGL 1039
Cdd:COG4988 387 LPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRENLRLGR---PDASDEELEAALEAAGLDEFVAALPDGL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1040 DARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHATELMPGDTLVR 1119
Cdd:COG4988 464 DTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILV 543
|
.
gi 1001866046 1120 L 1120
Cdd:COG4988 544 L 544
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
589-1106 |
8.88e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 171.50 E-value: 8.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 589 RRGAWLRTLASLLGPDAGTYARAALAGLGAAAAAVALSTLSGWLIVRASEQPPILYLLTAITGVRFFGIARAVLRYRERL 668
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 669 VLHSAVLSTLTELRERLWAL---LSVRGLSARRllvPGAALEALVGDAEAVRDQLPRVLAPITTAVLVAAGALVA----- 740
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHllrLPLSFFDRRR---TGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVlfvid 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 741 VQILLPAQTPVLAAAVVVALVAAPAVARAADRRAAARsqagraSLLARMGQALAAGPDLRANGRAGAVLRSIRSADAALT 820
Cdd:COG1132 161 WRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALA------ELNGRLQESLSGIRVVKAFGREERELERFREANEELR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 821 RLERRGAAAEGLAHAIVvaaTGAAAALTLGAAQAAGAPAATAAAVLLLQLALAEPLAAASTAVQQLPALRSALVRVAAEE 900
Cdd:COG1132 235 RANLRAARLSALFFPLM---ELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 901 QAVRDAAEERDDLQDAPGRGP------GITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLA 974
Cdd:COG1132 312 ERIFELLDEPPEIPDPPGAVPlppvrgEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 975 PRVGS-------------AAVAGPVAWCPQESHLFDSTVRGNLAVARDRdhaPSDAELEAVLARVGLLEHVRSLPGGLDA 1041
Cdd:COG1132 392 PTSGRilidgvdirdltlESLRRQIGVVPQDTFLFSGTIRENIRYGRPD---ATDEEVEEAAKAAQAHEFIEALPDGYDT 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 1042 RIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
883-1106 |
7.07e-44 |
|
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: 171.17 E-value: 7.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 883 VQQLPALRSALVRVAAeeqaVRDAAEERDD---LQDAPGRGPGITLRGVTVGWTG-GPDVLAGLDLAARPGDWIVVAGPS 958
Cdd:COG2274 435 LQRFQDAKIALERLDD----ILDLPPEREEgrsKLSLPRLKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRS 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 959 GSGKSTLLALLTGFLAPRVGS-------------AAVAGPVAWCPQESHLFDSTVRGNLAVARDRdhaPSDAELEAVLAR 1025
Cdd:COG2274 511 GSGKSTLLKLLLGLYEPTSGRilidgidlrqidpASLRRQIGVVLQDVFLFSGTIRENITLGDPD---ATDEEIIEAARL 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1026 VGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVT 1105
Cdd:COG2274 588 AGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA 667
|
.
gi 1001866046 1106 H 1106
Cdd:COG2274 668 H 668
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-553 |
9.54e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 156.48 E-value: 9.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 12 RRALVLLGVLAAAKAVGLALVAQGVASGLAALAAGAVRPGVLSAATLVAAAGVLLRAAAEWGTSTVGRWAAVGVKEELRS 91
Cdd:COG1132 19 YRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 92 QLLEAALEGGAAPASaagpvDDGAARVASspaatavLAGRGLDGLDALYTQYLPALVQTAVLPLLVGARILGADWVSALI 171
Cdd:COG1132 99 DLFEHLLRLPLSFFD-----RRRTGDLLS-------RLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 172 LVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKGRTMATLRVAFL 251
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 252 SALALELISTISVAVVAVFIGIRLVHGDMTLEAGLLALILAPECFQPLRDLGTAHHASEDGAEALRRTRARIGAPRgtvl 331
Cdd:COG1132 247 FFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP---- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 332 laaghgRVQDAERPPAGQAAPAGLRVAGLTVWYDGaAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGL--VRDG 409
Cdd:COG1132 323 ------EIPDPPGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFydPTSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 410 vgaSVRgsVDGPDPR---------RIAWVPQHPQFSERTVAAELALYAGAAGEGAVpgepgalvrelldqlglggLEAAD 480
Cdd:COG1132 396 ---RIL--IDGVDIRdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPDATDEEV-------------------EEAAK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 481 PAE----------------------LSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTV 538
Cdd:COG1132 452 AAQahefiealpdgydtvvgergvnLSGGQRQRIAIARALLKDPP---ILILDEATSALDTETEALIQEALERLMKGRTT 528
|
570
....*....|....*
gi 1001866046 539 LLVSHEPRTAALADR 553
Cdd:COG1132 529 IVIAHRLSTIRNADR 543
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
923-1120 |
4.73e-38 |
|
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: 140.21 E-value: 4.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPD-VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS-------------AAVAGPVAW 988
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEilidgvdlrdldlESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 989 CPQESHLFDSTVRGNLavardrdhapsdaeleavlarvgllehvrslpggldarigsrgafLSGGQRQRLAVARTLLAGA 1068
Cdd:cd03228 81 VPQDPFLFSGTIRENI---------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 1069 EVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHATELMPGDTLVRL 1120
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVL 167
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
923-1106 |
2.35e-37 |
|
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: 140.03 E-value: 2.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGP-DVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-------------VAW 988
Cdd:cd03245 3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 989 CPQESHLFDSTVRGNLAVARDrdhAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGA 1068
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAP---LADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1001866046 1069 EVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITH 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
923-1120 |
1.23e-36 |
|
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: 137.22 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPD----VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESHLFDS 998
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 TVRGNLAVARDRDHapsdAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTA 1078
Cdd:cd03250 81 TIRENILFGKPFDE----ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1001866046 1079 HLDPESGLALVA-ALHGALAD-RTVVMVTHHATELMPGDTLVRL 1120
Cdd:cd03250 157 AVDAHVGRHIFEnCILGLLLNnKTRILVTHQLQLLPHADQIVVL 200
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
921-1106 |
1.81e-36 |
|
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: 145.89 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------PVA 987
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 988 WCPQESHLFDSTVRGNLAVARDrdhAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAG 1067
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARP---DASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 1068 AEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
923-1124 |
5.72e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.71 E-value: 5.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPdVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------PVAW------C 989
Cdd:COG4619 1 LELEGLSFRVGGKP-ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampPPEWrrqvayV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 PQESHLFDSTVRGNLA-VARDRDHAPSDAELEAVLARVGLLEHVrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGA 1068
Cdd:COG4619 80 PQEPALWGGTVRDNLPfPFQLRERKFDRERALELLERLGLPPDI------LDKPVER----LSGGERQRLALIRALLLQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 1069 EVVLLDEPTAHLDPESGLALVAALHGALA--DRTVVMVTHHATELM-PGDTLVRLGARE 1124
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIErVADRVLTLEAGR 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
923-1118 |
6.62e-36 |
|
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: 136.21 E-value: 6.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTG-GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------PVAW 988
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 989 CPQESHLFDSTVRGNLAVARDRDhapSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGA 1068
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGA---TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1069 EVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHATELMPGDTLV 1118
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIV 207
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
923-1107 |
1.97e-35 |
|
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: 134.66 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------PVAWC 989
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 PQESHLFDSTVRGNLAVARDRdhaPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAE 1069
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPN---ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1001866046 1070 VVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHH 1107
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHR 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
934-1107 |
2.90e-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: 134.16 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------PVAWCPQESHLFDSTV 1000
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 RGNLavarDRDHAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHL 1080
Cdd:cd03244 95 RSNL----DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180
....*....|....*....|....*..
gi 1001866046 1081 DPESGLALVAALHGALADRTVVMVTHH 1107
Cdd:cd03244 171 DPETDALIQKTIREAFKDCTVLTIAHR 197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
938-1106 |
4.92e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 139.21 E-value: 4.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAG-LDLAARPGDWIVVAGPSGSGKSTLLALLTGFLaPRVGSAAVAG-------------PVAWCPQESHLFDSTVRGN 1003
Cdd:PRK11174 364 TLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1004 LAVArdrDHAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPE 1083
Cdd:PRK11174 443 VLLG---NPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180
....*....|....*....|...
gi 1001866046 1084 SGLALVAALHGALADRTVVMVTH 1106
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVTH 542
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
923-1115 |
2.74e-33 |
|
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: 128.89 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------PVAWC 989
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 PQESHLFDSTVRGNLAVARDrdhAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAE 1069
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRP---DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1001866046 1070 VVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHATELMPGD 1115
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNAD 203
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
146-557 |
2.83e-33 |
|
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: 136.82 E-value: 2.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 146 ALVQTAVLPLLVGARILGADWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQsllRLGSHLVELAQGLPVLVGLGRAA 225
Cdd:COG4987 139 ALLVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARA---ALRARLTDLLQGAAELAAYGALD 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 226 EQRRALGELSRAYKGRTMATLRVAFLSALALELISTISVAVVAVfIGIRLVHGDMTLEAGLLALILAP----ECFQPLRD 301
Cdd:COG4987 216 RALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLW-LAAPLVAAGALSGPLLALLVLAAlalfEALAPLPA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 302 LGTAHHASEDgaeALRRTRARIGAPRgtvllaaghgRVQDAERPPAGQAAPAgLRVAGLTVWYDGAAEPAVGPLDFTAPA 381
Cdd:COG4987 295 AAQHLGRVRA---AARRLNELLDAPP----------AVTEPAEPAPAPGGPS-LELEDVSFRYPGAGRPVLDGLSLTLPP 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 382 GRVTVLAGPSGSGKTTVLAALAGLVR--------DGVGASvrgSVDGPDPRR-IAWVPQHPQFSERTVAAELALYAGAAG 452
Cdd:COG4987 361 GERVAIVGPSGSGKSTLLALLLRFLDpqsgsitlGGVDLR---DLDEDDLRRrIAVVPQRPHLFDTTLRENLRLARPDAT 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 453 EGAVPG-----EPGALVRELLDQLGLGGLEAAdpAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVER 527
Cdd:COG4987 438 DEELWAalervGLGDWLAALPDGLDTWLGEGG--RRLSGGERRRLALARALLR---DAPILLLDEPTEGLDAATEQALLA 512
|
410 420 430
....*....|....*....|....*....|
gi 1001866046 528 AIAALAGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:COG4987 513 DLLEALAGRTVLLITHRLAGLERMDRILVL 542
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
902-1118 |
5.51e-33 |
|
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: 136.00 E-value: 5.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 902 AVRDAAEERDDLQDAPGRGPG-ITLRGVTVGWTG-GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS 979
Cdd:TIGR02203 309 TLLDSPPEKDTGTRAIERARGdVEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 980 AAVAG-------------PVAWCPQESHLFDSTVRGNLAVARDRDHapSDAELEAVLARVGLLEHVRSLPGGLDARIGSR 1046
Cdd:TIGR02203 389 ILLDGhdladytlaslrrQVALVSQDVVLFNDTIANNIAYGRTEQA--DRAEIERALAAAYAQDFVDKLPLGLDTPIGEN 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 1047 GAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHATELMPGDTLV 1118
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIV 538
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
923-1107 |
5.84e-33 |
|
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: 136.92 E-value: 5.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTG-GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS-------------AAVAGPVAW 988
Cdd:TIGR03375 464 IEFRNVSFAYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSvlldgvdirqidpADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 989 CPQESHLFDSTVRGNLAVARDrdhAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGA 1068
Cdd:TIGR03375 544 VPQDPRLFYGTLRDNIALGAP---YADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDP 620
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 1069 EVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHH 1107
Cdd:TIGR03375 621 PILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHR 659
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
923-1106 |
3.99e-32 |
|
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: 125.34 E-value: 3.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPD--VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG------PVAW------ 988
Cdd:cd03249 1 IEFKNVSFRYPSRPDvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlNLRWlrsqig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 989 -CPQESHLFDSTVRGNLAVARDRdhaPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAG 1067
Cdd:cd03249 81 lVSQEPVLFDGTIAENIRYGKPD---ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 1068 AEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
26-317 |
1.17e-31 |
|
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: 125.86 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 26 AVGLALVAQGVASGLAALAAGAVRPGVLSAATLVAAAG-VLLRAAAEWGTSTVGRWAAVGVKEELRSQLLEAALEGGAAp 104
Cdd:cd18561 7 LITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGvIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 105 asaagpvddGAARVASSPAATAVLAGrgLDGLDALYTQYLPALVQTAVLPLLVGARILGADWVSALILVLTLPLVPVFMI 184
Cdd:cd18561 86 ---------YLEGERTGELQTTVVDG--VEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 185 LIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKGRTMATLRVAFLSALALELISTISV 264
Cdd:cd18561 155 LWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGT 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 265 AVVAVFIGIRLVHGDMTLEAGLLALILAPECFQPLRDLGTAHHASEDGAEALR 317
Cdd:cd18561 235 ALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAAD 287
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
921-1106 |
1.90e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 123.23 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWTGGP---DVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVA--------- 987
Cdd:COG1136 3 PLLELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqDISslserelar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 988 -------WCPQESHLFDS-TVRGNLAVA---RDRDHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQ 1056
Cdd:COG1136 83 lrrrhigFVFQFFNLLPElTALENVALPlllAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 1057 RLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHgALAD---RTVVMVTH 1106
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLR-ELNRelgTTIVMVTH 203
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
355-557 |
5.03e-31 |
|
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: 120.18 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVR-GSVDGPD------PRRIA 427
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG-EILiDGVDLRDldleslRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 428 WVPQHPQFSERTVAAELalyagaagegavpgepgalvrelldqlglggleaadpaeLSPGQQRRVAVARGLARvadGAGL 507
Cdd:cd03228 80 YVPQDPFLFSGTIRENI---------------------------------------LSGGQRQRIAIARALLR---DPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 508 LLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVL 167
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
889-1136 |
8.35e-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: 129.10 E-value: 8.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 889 LRSALVRVAAEEQAVRdaaeerddLQDAPGRgpgITLRGVTVGWTGGP-DVLAGLDLAARPGDWIVVAGPSGSGKSTLLA 967
Cdd:COG4618 308 LNELLAAVPAEPERMP--------LPRPKGR---LSVENLTVVPPGSKrPILRGVSFSLEPGEVLGVIGPSGSGKSTLAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 968 LLTGFLAP-----RVGSAAVA-------GP-VAWCPQESHLFDSTVRGNlaVARDRDhaPSDAELEAVLARVGLLEHVRS 1034
Cdd:COG4618 377 LLVGVWPPtagsvRLDGADLSqwdreelGRhIGYLPQDVELFDGTIAEN--IARFGD--ADPEKVVAAAKLAGVHEMILR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1035 LPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALAD-RTVVMVTHHATEL-- 1111
Cdd:COG4618 453 LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLaa 532
|
250 260 270
....*....|....*....|....*....|.
gi 1001866046 1112 ------MPGDTLVRLGARERVLHHAARAAAP 1136
Cdd:COG4618 533 vdkllvLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
917-1106 |
1.31e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 121.74 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 917 PGRGPGITLRGVTVGW---TGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAP-----RVGSAAVAGP--- 985
Cdd:COG1116 2 SAAAPALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtsgevLVDGKPVTGPgpd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 986 VAWCPQESHLFD-STVRGNLAVA---RDRDHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVA 1061
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGlelRGVPKAERRERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1001866046 1062 RTLLAGAEVVLLDEPTAHLDPESGLAL---VAALHGALaDRTVVMVTH 1106
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLqdeLLRLWQET-GKTVLFVTH 197
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
923-1120 |
2.41e-30 |
|
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: 120.28 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTG-GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------PVAW 988
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 989 CPQESHLFDSTVRGNLAVArdrDHAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGA 1068
Cdd:cd03252 81 VLQENVLFNRSIRDNIALA---DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 1069 EVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHATELMPGDTLVRL 1120
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVM 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
921-1135 |
5.87e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 5.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP--------VAWCPQE 992
Cdd:COG1121 5 PAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 993 SHL---FDSTVR-----------GNLAVARDRDHApsdaELEAVLARVGLLEHvrslpggLDARIGSrgafLSGGQRQRL 1058
Cdd:COG1121 84 AEVdwdFPITVRdvvlmgrygrrGLFRRPSRADRE----AVDEALERVGLEDL-------ADRPIGE----LSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1059 AVARTLLAGAEVVLLDEPTAHLDPESG---LALVAALHGalADRTVVMVTHHATELMP--------GDTLVRLGARERVL 1127
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEealYELLRELRR--EGKTILVVTHDLGAVREyfdrvlllNRGLVAHGPPEEVL 226
|
....*...
gi 1001866046 1128 HHAARAAA 1135
Cdd:COG1121 227 TPENLSRA 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
914-1120 |
6.30e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 126.48 E-value: 6.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 914 QDAPGRGPGITLRGVTVGWTGGPD-VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PV-AWC- 989
Cdd:PRK11160 330 STAAADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqPIaDYSe 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 ----------PQESHLFDSTVRGNLAVArdrDHAPSDAELEAVLARVGLLEHVRSlPGGLDARIGSRGAFLSGGQRQRLA 1059
Cdd:PRK11160 410 aalrqaisvvSQRVHLFSATLRDNLLLA---APNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLG 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1060 VARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHATELMPGDTLVRL 1120
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVM 546
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
938-1109 |
7.40e-30 |
|
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: 117.03 E-value: 7.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS------------AAVAGPVAWCPQESHLFDSTVRGNLa 1005
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEitldgvpvsdleKALSSLISVLNQRPYLFDTTLRNNL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1006 vardrdhapsdaeleavlarvgllehvrslpggldarigsrGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESG 1085
Cdd:cd03247 96 -----------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180
....*....|....*....|....
gi 1001866046 1086 LALVAALHGALADRTVVMVTHHAT 1109
Cdd:cd03247 135 RQLLSLIFEVLKDKTLIWITHHLT 158
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
943-1107 |
9.90e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 118.32 E-value: 9.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 943 DLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------PVAWCPQESHLFDS-TVRGNLAVARDR 1010
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalppaerPVSMLFQENNLFPHlTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1011 DHAPSDAE---LEAVLARVGLLEHVRSLPGGldarigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP---ES 1084
Cdd:COG3840 99 GLKLTAEQraqVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrQE 167
|
170 180
....*....|....*....|...
gi 1001866046 1085 GLALVAALHGALaDRTVVMVTHH 1107
Cdd:COG3840 168 MLDLVDELCRER-GLTVLMVTHD 189
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
884-1109 |
3.02e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 124.15 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 884 QQLPALRSALVRVAAEEQAVRDA-AEERDDLQDAPGRGPGITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGK 962
Cdd:COG4178 323 QSLAEWRATVDRLAGFEEALEAAdALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 963 STLLALLTGfLAPRvGSAAVAGP----VAWCPQESHLFDSTVRGNLAVARDRDhAPSDAELEAVLARVGLlEHvrsLPGG 1038
Cdd:COG4178 403 STLLRAIAG-LWPY-GSGRIARPagarVLFLPQRPYLPLGTLREALLYPATAE-AFSDAELREALEAVGL-GH---LAER 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1039 LDARiGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHAT 1109
Cdd:COG4178 476 LDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRST 545
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
934-1124 |
3.29e-29 |
|
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: 116.04 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS------------AAVAGPVAWCPQESHLFDS-TV 1000
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngepirdarEDYRRRLAYLGHADGLKPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 RGNLA-VARDRDHAPSDAELEAVLARVGLLEHvrslpggLDARIGsrgaFLSGGQRQRLAVARTLLAGAEVVLLDEPTAH 1079
Cdd:COG4133 93 RENLRfWAALYGLRADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1001866046 1080 LDPESGLALVAALHGALAD-RTVVMVTHHATELmPGDTLVRLGARE 1124
Cdd:COG4133 162 LDAAGVALLAELIAAHLARgGAVLLTTHQPLEL-AAARVLDLGDFK 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
938-1111 |
3.59e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 117.09 E-value: 3.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG------------PVAWCPQESHLFDS-TVRGNL 1004
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1005 ---AVARDRDHAPSDAELEAVLARVGLLEHvrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:COG1131 95 rffARLYGLPRKEARERIDELLELFGLTDA-------ADRKVGT----LSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190
....*....|....*....|....*....|..
gi 1001866046 1082 PESGLALVAALHgALADR--TVVMVTHHATEL 1111
Cdd:COG1131 164 PEARRELWELLR-ELAAEgkTVLLSTHYLEEA 194
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
923-1123 |
6.17e-29 |
|
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: 115.65 E-value: 6.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGP---DVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAP-----RVGSAAVAGP---VAWCPQ 991
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtsgevLVDGEPVTGPgpdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 992 ESHLFD-STVRGNLAV---ARDRDHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAG 1067
Cdd:cd03293 81 QDALLPwLTVLDNVALgleLQGVPKAEARERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 1068 AEVVLLDEPTAHLDPESGLALVAALHGALADR--TVVMVTHHATE-LMPGDTLVRLGAR 1123
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEaVFLADRVVVLSAR 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
939-1078 |
1.54e-28 |
|
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: 112.36 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 939 LAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-------------VAWCPQESHLF-DSTVRGNL 1004
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 1005 AVAR---DRDHAPSDAELEAVLARVGLlehvrslPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTA 1078
Cdd:pfam00005 81 RLGLllkGLSKREKDARAEEALEKLGL-------GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
925-1113 |
2.34e-28 |
|
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: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 925 LRGVTVGWTGG-PDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------PVAWCP 990
Cdd:cd03225 2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 Q--ESHLFDSTVR-------GNLAVARDRDhapsDAELEAVLARVGLLEHvrslpggLDARIGSrgafLSGGQRQRLAVA 1061
Cdd:cd03225 82 QnpDDQFFGPTVEeevafglENLGLPEEEI----EERVEEALELVGLEGL-------RDRSPFT----LSGGQKQRVAIA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 1062 RTLLAGAEVVLLDEPTAHLDPESGLALVAALHGaLADR--TVVMVTHHATELMP 1113
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLE 199
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
923-1106 |
2.59e-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: 113.74 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGP---DVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCP-------- 990
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtDISKLSekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 --------QESHLFDS-TVRGNLAVA---RDRDHAPSDAELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRL 1058
Cdd:cd03255 81 rrhigfvfQSFNLLPDlTALENVELPlllAGVPKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1059 AVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHG--ALADRTVVMVTH 1106
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTH 199
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
923-1107 |
5.51e-28 |
|
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: 113.99 E-value: 5.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS-------------AAVAGPVAWC 989
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgrdlaslsrRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 PQESHL-FDSTVRGNLAVAR----DRDHAPSDAELEAV---LARVGLLEHVrslpgglDARIGSrgafLSGGQRQRLAVA 1061
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRyphlGLFGRPSAEDREAVeeaLERTGLEHLA-------DRPVDE----LSGGERQRVLIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 1062 RTLLAGAEVVLLDEPTAHLDP---ESGLALVAALHgALADRTVVMVTHH 1107
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLahqLEVLELLRRLA-RERGRTVVMVLHD 197
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
923-1106 |
1.12e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 112.07 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVA------------------- 983
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlsrlkrreipylrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 984 GPVawcPQESHL-FDSTVRGNLA---VARDRDHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLA 1059
Cdd:COG2884 82 GVV---FQDFRLlPDRTVYENVAlplRVTGKSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRVA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 1060 VARTLLAGAEVVLLDEPTAHLDPESGLALVAALHgALADR--TVVMVTH 1106
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLE-EINRRgtTVLIATH 195
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
923-1118 |
2.17e-27 |
|
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: 111.07 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------PVAWCPQ 991
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 992 ESHLFDS-TVRGNLA---VARDRDHAPSDAELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAG 1067
Cdd:cd03259 80 DYALFPHlTVAENIAfglKLRGVPKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALARE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 1068 AEVVLLDEPTAHLDPESGLAL---VAALHGALaDRTVVMVTHHATE-LMPGDTLV 1118
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELreeLKELQREL-GITTIYVTHDQEEaLALADRIA 202
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
923-1107 |
2.35e-27 |
|
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: 111.66 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------PVAWCPQ---- 991
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknLRELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 992 ----ESHLFDSTVRGNLAVA-RDRDHAPSDAE--LEAVLARVGLLEHvrslpggLDARIgsrgAFLSGGQRQRLAVARTL 1064
Cdd:COG1122 81 fqnpDDQLFAPTVEEDVAFGpENLGLPREEIRerVEEALELVGLEHL-------ADRPP----HELSGGQKQRVAIAGVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1001866046 1065 LAGAEVVLLDEPTAHLDPESGLALVAALHG-ALADRTVVMVTHH 1107
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHD 193
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
902-1106 |
8.73e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 116.66 E-value: 8.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 902 AVRDAAEERDDLQDAPGRGPG-ITLRGVTVGWTG--GPdVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVG 978
Cdd:PRK11176 320 AILDLEQEKDEGKRVIERAKGdIEFRNVTFTYPGkeVP-ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 979 SAAVAG-------------PVAWCPQESHLFDSTVRGNLAVARDRDHAPSDAELEAVLARVglLEHVRSLPGGLDARIGS 1045
Cdd:PRK11176 399 EILLDGhdlrdytlaslrnQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYA--MDFINKMDNGLDTVIGE 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1046 RGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
919-1112 |
1.40e-26 |
|
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: 109.68 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 919 RGPGITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCP------- 990
Cdd:COG1127 2 SEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSekelyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 --------QESHLFDS-TVRGNLAVARDRDHAPSDAELEA----VLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQR 1057
Cdd:COG1127 81 rrrigmlfQGGALFDSlTVFENVAFPLREHTDLSEAEIRElvleKLELVGLPGAADKMPSEL-----------SGGMRKR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 1058 LAVARTLLAGAEVVLLDEPTAHLDPESGLA---LVAALHGALaDRTVVMVTHHATELM 1112
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVideLIRELRDEL-GLTSVVVTHDLDSAF 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
356-557 |
2.75e-26 |
|
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: 107.94 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 356 RVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--DGV----GASVRGSVDGPDPRRIAWV 429
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGptSGEvlvdGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 430 PQHP--QFSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagL 507
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAF--GLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD---I 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 508 LLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHEP-RTAALADRTVEL 557
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLdLLLELADRVIVL 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
927-1106 |
2.93e-26 |
|
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: 107.62 E-value: 2.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 927 GVTVGWTGGPdVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP--------VAWCPQeSHLFDS 998
Cdd:cd03235 4 DLTVSYGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQ-RRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 ----TVRGNLAVARDRD----HAPSDAELEAV---LARVGLLEHvrslpggLDARIGSrgafLSGGQRQRLAVARTLLAG 1067
Cdd:cd03235 82 dfpiSVRDVVLMGLYGHkglfRRLSKADKAKVdeaLERVGLSEL-------ADRQIGE----LSGGQQQRVLLARALVQD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1001866046 1068 AEVVLLDEPTAHLDPESG---LALVAALHGalADRTVVMVTH 1106
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQediYELLRELRR--EGMTILVVTH 190
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
937-1129 |
3.20e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 114.75 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 937 DVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-------------VAWCPQESHLFDSTVRGN 1003
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAdlkqwdretfgkhIGYLPQDVELFPGTVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1004 laVARDRDHAPSDAELEA-VLArvGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:TIGR01842 412 --IARFGENADPEKIIEAaKLA--GVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 1083 ESGLALVAAL-HGALADRTVVMVTHHATEL--------MPGDTLVRLGARERVLHH 1129
Cdd:TIGR01842 488 EGEQALANAIkALKARGITVVVITHRPSLLgcvdkilvLQDGRIARFGERDEVLAK 543
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
355-555 |
3.22e-26 |
|
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: 108.04 E-value: 3.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAepAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSV--DGPDP--------- 423
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVllDGKDIydldvdvle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 424 --RRIAWVPQHPQFSERTVAAELALYAGAAGEgAVPGEPGALVRELLDQLGLGGLEA--ADPAELSPGQQRRVAVARGLA 499
Cdd:cd03260 79 lrRRVGMVFQKPNPFPGSIYDNVAYGLRLHGI-KLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 500 RVADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAA-LADRTV 555
Cdd:cd03260 158 NEPE---VLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTA 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
165-557 |
3.98e-26 |
|
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: 115.70 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 165 DWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKGRTMA 244
Cdd:COG2274 294 SPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 245 TLRVAFLSALALELISTISVAVVaVFIGIRLV-HGDMTLeAGLLA-LILAPECFQPLRDLGtahhaseDGAEALRRTRA- 321
Cdd:COG2274 374 LRRLSNLLSTLSGLLQQLATVAL-LWLGAYLViDGQLTL-GQLIAfNILSGRFLAPVAQLI-------GLLQRFQDAKIa 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 322 --RIGAprgtvLLAAGHGRVQDAERPPAGQAAPAgLRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVL 399
Cdd:COG2274 445 leRLDD-----ILDLPPEREEGRSKLSLPRLKGD-IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 400 AALAGLVR--------DGVG------ASVRgsvdgpdpRRIAWVPQHPQFSERTVAAELALYAGAAGEGAVpgepgalvr 465
Cdd:COG2274 519 KLLLGLYEptsgriliDGIDlrqidpASLR--------RQIGVVLQDVFLFSGTIRENITLGDPDATDEEI--------- 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 466 elldqlglggLEAADPAE----------------------LSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAA 523
Cdd:COG2274 582 ----------IEAARLAGlhdfiealpmgydtvvgeggsnLSGGQRQRLAIARALLR---NPRILILDEATSALDAETEA 648
|
410 420 430
....*....|....*....|....*....|....
gi 1001866046 524 LVERAIAALAGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:COG2274 649 IILENLRRLLKGRTVIIIAHRLSTIRLADRIIVL 682
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
355-557 |
4.15e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 107.18 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRG----SVDGPDPRRIAWV 429
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvLWNGepirDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 430 PQHPQF-SERTVAAELALYAGAAGEGAvpgePGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARvadGAGLL 508
Cdd:COG4133 81 GHADGLkPELTVRENLRFWAALYGLRA----DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS---PAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 509 LLDEPTAHLDDASAALVERAIAA-LAGRVTVLLVSHEPRTAAlADRTVEL 557
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELA-AARVLDL 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
924-1120 |
4.88e-26 |
|
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: 105.40 E-value: 4.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 924 TLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGpvawcpqeshlfdstvrgn 1003
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1004 lavardrdHAPSDAELEAVLARVGLLEHvrslpggldarigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPE 1083
Cdd:cd00267 61 --------KDIAKLPLEELRRRIGYVPQ------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 1084 SGLALVAALHGALAD-RTVVMVTHHATELMP-GDTLVRL 1120
Cdd:cd00267 115 SRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVL 153
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
923-1112 |
8.10e-26 |
|
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: 107.20 E-value: 8.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGpVAWCP------------ 990
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG-EDISGlseaelyrlrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 -----QESHLFDS-TVRGNLAVARDRDHAPSDAELEAV----LARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAV 1060
Cdd:cd03261 79 mgmlfQSGALFDSlTVFENVAFPLREHTRLSEEEIREIvlekLEAVGLRGAEDLYP-----------AELSGGMKKRVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 1061 ARTLLAGAEVVLLDEPTAHLDPESGLA---LVAALHGALaDRTVVMVTHHATELM 1112
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGViddLIRSLKKEL-GLTSIMVTHDLDTAF 201
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
886-1120 |
1.84e-25 |
|
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: 114.66 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 886 LPALRSALVRVAAEEQAVR----------DAAEERddlQDAPGRGPGITLRGVTVGWTGG-PDVLAGLDLAARPGDWIVV 954
Cdd:TIGR00957 593 LPMVISSIVQASVSLKRLRiflsheelepDSIERR---TIKPGEGNSITVHNATFTWARDlPPTLNGITFSIPEGALVAV 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 955 AGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESHLFDSTVRGNLAVArdrdHAPSDAELEAVLARVGLLEHVRS 1034
Cdd:TIGR00957 670 VGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFG----KALNEKYYQQVLEACALLPDLEI 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1035 LPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLAL---VAALHGALADRTVVMVTHHATEL 1111
Cdd:TIGR00957 746 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfehVIGPEGVLKNKTRILVTHGISYL 825
|
....*....
gi 1001866046 1112 MPGDTLVRL 1120
Cdd:TIGR00957 826 PQVDVIIVM 834
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
350-557 |
1.95e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.33 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 350 AAPAGLRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVG-ASVRGSVDGPDPRRIAW 428
Cdd:COG1121 2 MMMPAIELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtVRLFGKPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 429 VPQHPQFSER---TVAaELALyAGAAGEGAVPGEPGALVRELLDQLGLGGlEAADPA-----ELSPGQQRRVAVARGLAR 500
Cdd:COG1121 80 VPQRAEVDWDfpiTVR-DVVL-MGRYGRRGLFRRPSRADREAVDEALERV-GLEDLAdrpigELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 501 VADgagLLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHEPRTAA-LADRTVEL 557
Cdd:COG1121 157 DPD---LLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVReYFDRVLLL 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
355-555 |
2.06e-25 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 105.29 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDG-------PDPRRIA 427
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSG---EILIDGrdvtgvpPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 428 WVPQHPQ-FSERTVAAELA--LYAGAAGEGAVPgepgALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARvadG 504
Cdd:cd03259 76 MVFQDYAlFPHLTVAENIAfgLKLRGVPKAEIR----ARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAR---E 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 505 AGLLLLDEPTAHLDDASAALVERAIAAL--AGRVTVLLVSHEPRTA-ALADRTV 555
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEEAlALADRIA 202
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
923-1106 |
2.30e-25 |
|
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: 105.73 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVgWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFL-----APRVGSAAVAGPVAWCP------- 990
Cdd:cd03260 1 IELRDLNV-YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLdvdvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 --------QESHLFDSTVRGNLAVA----RDRDHAPSDAELEAVLARVGLLEHVRSLPGGLDarigsrgafLSGGQRQRL 1058
Cdd:cd03260 80 rrrvgmvfQKPNPFPGSIYDNVAYGlrlhGIKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1001866046 1059 AVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH 198
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
924-1106 |
3.80e-25 |
|
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: 104.26 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 924 TLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP----------VAWCPQES 993
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrksIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 994 --HLFDSTVRGNLAVaRDRDHAPSDAELEAVLARVGLLEHVRSLPggLDarigsrgafLSGGQRQRLAVARTLLAGAEVV 1071
Cdd:cd03226 81 dyQLFTDSVREELLL-GLKELDAGNEQAETVLKDLDLYALKERHP--LS---------LSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 1001866046 1072 LLDEPTAHLDPESgLALVAALHGALA--DRTVVMVTH 1106
Cdd:cd03226 149 IFDEPTSGLDYKN-MERVGELIRELAaqGKAVIVITH 184
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
923-1107 |
4.15e-25 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 105.52 E-value: 4.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG----------------PV 986
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvtalrgralrrlrrRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 987 AWCPQESHLFD-STVRGNLAVAR-----------------DRDHApsdaeLEAvLARVGLLEHvrslpggLDARIGSrga 1048
Cdd:COG3638 83 GMIFQQFNLVPrLSVLTNVLAGRlgrtstwrsllglfppeDRERA-----LEA-LERVGLADK-------AYQRADQ--- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1049 fLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADR--TVVMVTHH 1107
Cdd:COG3638 147 -LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQ 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
938-1110 |
4.34e-25 |
|
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: 104.51 E-value: 4.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG------------PVAWCPQESHLFDS-TVRGNL 1004
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1005 ---AVARDRDHAPSDAELEAVLARVGLLEHvrslpggLDARIGsrgaFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:cd03263 97 rfyARLKGLPKSEIKEEVELLLRVLGLTDK-------ANKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180
....*....|....*....|....*....
gi 1001866046 1082 PESGLALVAALHGALADRTVVMVTHHATE 1110
Cdd:cd03263 166 PASRRAIWDLILEVRKGRSIILTTHSMDE 194
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
923-1106 |
1.04e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 103.92 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVgWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCP------------ 990
Cdd:COG1126 2 IEIENLHK-SFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkkdinklrrkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 ---QESHLFDS-TVRGNLAVA------RDRDHAPSDAelEAVLARVGLLEHVRSLPGGldarigsrgafLSGGQRQRLAV 1060
Cdd:COG1126 81 mvfQQFNLFPHlTVLENVTLApikvkkMSKAEAEERA--MELLERVGLADKADAYPAQ-----------LSGGQQQRVAI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1061 ARTLLAGAEVVLLDEPTAHLDPEsglaLVA---ALHGALADR--TVVMVTH 1106
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPE----LVGevlDVMRDLAKEgmTMVVVTH 194
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
883-1092 |
1.57e-24 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 110.42 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 883 VQQLPALRSALVRV------AAEEQAVRDAAEERDDLQDAPGRGpGITLRGVTVGWTG-GPDVLAGLDLAARPGDWIVVA 955
Cdd:TIGR03796 433 GGTLQELEGDLNRLddvlrnPVDPLLEEPEGSAATSEPPRRLSG-YVELRNITFGYSPlEPPLIENFSLTLQPGQRVALV 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 956 GPSGSGKSTLLALLTGFLAPRVGS-------------AAVAGPVAWCPQESHLFDSTVRGNLAVArdrDHAPSDAELEAV 1022
Cdd:TIGR03796 512 GGSGSGKSTIAKLVAGLYQPWSGEilfdgipreeiprEVLANSVAMVDQDIFLFEGTVRDNLTLW---DPTIPDADLVRA 588
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1023 LARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAAL 1092
Cdd:TIGR03796 589 CKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL 658
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
908-1106 |
1.79e-24 |
|
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: 109.91 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 908 EERDDLQDAPG------RGPGITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS-- 979
Cdd:COG5265 337 DQPPEVADAPDapplvvGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRil 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 980 -----------AAVAGPVAWCPQESHLFDSTVRGNLAVARDrdHApSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGA 1048
Cdd:COG5265 417 idgqdirdvtqASLRAAIGIVPQDTVLFNDTIAYNIAYGRP--DA-SEEEVEAAARAAQIHDFIESLPDGYDTRVGERGL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 1049 FLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:COG5265 494 KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAH 551
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
355-592 |
3.33e-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: 108.07 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGPDP---------RR 425
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLlelsealrgRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 IAWVPQHP--QFSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVAD 503
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDQIAE--ALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 504 gagLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAA-LADRTVELAPSSSAASARfRADVPDAPAADR 580
Cdd:COG1123 163 ---LLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAeIADRVVVMDDGRIVEDGP-PEEILAAPQALA 238
|
250
....*....|..
gi 1001866046 581 GVPAPAAVRRGA 592
Cdd:COG1123 239 AVPRLGAARGRA 250
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
355-557 |
3.44e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.04 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWY-DGAAE-PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVRgsVDGPDP--------- 423
Cdd:COG1136 5 LELRNLTKSYgTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSG-EVL--IDGQDIsslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 424 ----RRIAWVPQHPQ-FSERTVA--AELAL-YAGAAgegavPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVA 495
Cdd:COG1136 82 rlrrRHIGFVFQFFNlLPELTALenVALPLlLAGVS-----RKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 496 RGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAALADRTVEL 557
Cdd:COG1136 157 RALVN---RPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRL 217
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
917-1106 |
6.62e-24 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 108.29 E-value: 6.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 917 PGRGPGITLRGVTVGWT-GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG----------- 984
Cdd:TIGR01846 450 PELRGAITFENIRFRYApDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGvdlaiadpawl 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 985 --PVAWCPQESHLFDSTVRGNLAVARDrdhAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVAR 1062
Cdd:TIGR01846 530 rrQMGVVLQENVLFSRSIRDNIALCNP---GAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIAR 606
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1001866046 1063 TLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:TIGR01846 607 ALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAH 650
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
934-1120 |
6.80e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.39 E-value: 6.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG--PVAWCPQESHLFDS---TVRGNLAVAR 1008
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSEVPDSlplTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1009 DRDHAPS-------DAELEAVLARVGLlehvrslpGGLDARigsRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:NF040873 83 WARRGLWrrltrddRAAVDDALERVGL--------ADLAGR---QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1001866046 1082 PESGLALVAALHGALAD-RTVVMVTHHATELMPGDTLVRL 1120
Cdd:NF040873 152 AESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
906-1106 |
8.71e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 107.35 E-value: 8.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 906 AAEERDDLQDAPGRGPGITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG- 984
Cdd:PRK13657 318 DVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGt 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 985 ------------PVAWCPQESHLFDSTVRGNLAVARDrdhAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSG 1052
Cdd:PRK13657 398 dirtvtraslrrNIAVVFQDAGLFNRSIEDNIRVGRP---DATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 1053 GQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:PRK13657 475 GERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAH 528
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
934-1111 |
9.31e-24 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 101.47 E-value: 9.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDwiVVA--GPSGSGKSTLLALLTGFLAPRVGSAAVAG------------PVAWCPQESHLFDS- 998
Cdd:COG4555 12 GKVPALKDVSFTAKDGE--ITGllGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 TVRGNL---AVARDRDHAPSDAELEAVLARVGLLEHvrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDE 1075
Cdd:COG4555 90 TVRENIryfAELYGLFDEELKKRIEELIELLGLEEF-------LDRRVGE----LSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1001866046 1076 PTAHLDPESGLALVAALHgALAD--RTVVMVTHHATEL 1111
Cdd:COG4555 159 PTNGLDVMARRLLREILR-ALKKegKTVLFSSHIMQEV 195
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
923-1106 |
1.13e-23 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 100.30 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVgWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG---------------PVA 987
Cdd:cd03262 1 IEIKNLHK-SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 988 WCPQESHLFDS-TVRGNLAVA----RDRDHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVAR 1062
Cdd:cd03262 80 MVFQQFNLFPHlTVLENITLApikvKGMSKAEAEERALELLEKVGLADKADAYP-----------AQLSGGQQQRVAIAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 1063 TLLAGAEVVLLDEPTAHLDPEsglaLVAALHGALAD-----RTVVMVTH 1106
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPE----LVGEVLDVMKDlaeegMTMVVVTH 193
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
926-1107 |
1.19e-23 |
|
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: 100.62 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 926 RGVTVGWTGGPD--VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-------------VAWCP 990
Cdd:cd03248 15 QNVTFAYPTRPDtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 QESHLFDSTVRGNLAvardrdHAPSDAELEAVLA---RVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAG 1067
Cdd:cd03248 95 QEPVLFARSLQDNIA------YGLQSCSFECVKEaaqKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1001866046 1068 AEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHH 1107
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHR 208
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
350-555 |
1.82e-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: 100.93 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 350 AAPAGLRVAGLTVWYDGAAE--PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRG-SVDGPDPRR 425
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEvLVDGkPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 iAWVPQHPQ-FSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARvadG 504
Cdd:COG1116 83 -GVVFQEPAlLPWLTVLDNVAL--GLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN---D 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 505 AGLLLLDEPTAHLDDASAALVERAIAAL--AGRVTVLLVSHEPRTA-ALADRTV 555
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAvFLADRVV 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
355-557 |
2.11e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 99.51 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--------DGVgasVRGSVDGPDPRR- 425
Cdd:COG4619 1 LELEGLSFRVGGK--PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPptsgeiylDGK---PLSAMPPPEWRRq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 IAWVPQHPQFSERTVAAELALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAadpAELSPGQQRRVAVARGLARVADga 505
Cdd:COG4619 76 VAYVPQEPALWGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPV---ERLSGGERQRLALIRALLLQPD-- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 506 gLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAA-LADRTVEL 557
Cdd:COG4619 151 -VLLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHDPEQIErVADRVLTL 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
943-1107 |
5.01e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.89 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 943 DLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------PVAWCPQESHLFDS-TVRGNLAVARD- 1009
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttppsrrPVSMLFQENNLFSHlTVAQNIGLGLNp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1010 --RDHAPSDAELEAVLARVGLLEHVRSLPGGldarigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLA 1087
Cdd:PRK10771 99 glKLNAAQREKLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180
....*....|....*....|..
gi 1001866046 1088 LVAALHGALADR--TVVMVTHH 1107
Cdd:PRK10771 168 MLTLVSQVCQERqlTLLMVSHS 189
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
923-1106 |
6.04e-23 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 99.93 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWT-GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRvGSAAVAGpVAW------------- 988
Cdd:cd03289 3 MTVKDLTAKYTeGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDG-VSWnsvplqkwrkafg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 989 -CPQESHLFDSTVRGNLavarDRDHAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAG 1067
Cdd:cd03289 81 vIPQKVFIFSGTFRKNL----DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 1068 AEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEH 195
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
356-557 |
6.14e-23 |
|
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: 96.55 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 356 RVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRdgvgaSVRGSV--DGPDP---------R 424
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEIliDGKDIaklpleelrR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 425 RIAWVPQhpqfsertvaaelalyagaagegavpgepgalvrelldqlglggleaadpaeLSPGQQRRVAVARGLARVADg 504
Cdd:cd00267 74 RIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPD- 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 505 agLLLLDEPTAHLDDASAALVERAIAALA-GRVTVLLVSHEPRTAA-LADRTVEL 557
Cdd:cd00267 101 --LLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAElAADRVIVL 153
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
924-1107 |
6.94e-23 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 97.12 E-value: 6.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 924 TLRGVTVGwTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVA-WCPQEshlfdstvr 1001
Cdd:cd03214 1 EVENLSVG-YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkDLAsLSPKE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 gnlaVARDRdhapsdAELEAVLARVGLLEhvrslpggLDARIGSRgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:cd03214 71 ----LARKI------AYVPQALELLGLAH--------LADRPFNE---LSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180
....*....|....*....|....*....
gi 1001866046 1082 PESGLALVAALHgALAD---RTVVMVTHH 1107
Cdd:cd03214 130 IAHQIELLELLR-RLARergKTVVMVLHD 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
923-1109 |
7.46e-23 |
|
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: 98.28 E-value: 7.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP--------------VAW 988
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 989 CPQESHLFDS-TVRGNLAV-ARDRDHAPSDAELEAVLARVGLLEhvrslpggldARIGSRGAFLSGGQRQRLAVARTLLA 1066
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLgAYARRRAKRKARLERVYELFPRLK----------ERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1001866046 1067 GAEVVLLDEPTAHLDPesglALVAALHGALAD-----RTVVMVTHHAT 1109
Cdd:cd03224 150 RPKLLLLDEPSEGLAP----KIVEEIFEAIRElrdegVTILLVEQNAR 193
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
942-1126 |
7.98e-23 |
|
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: 97.95 E-value: 7.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 942 LDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------PVAWCPQESHLFDS-TVRGNLAVARD 1009
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappadrPVSMLFQENNLFAHlTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1010 ---RDHAPSDAELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP---E 1083
Cdd:cd03298 97 pglKLTAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPalrA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1001866046 1084 SGLALVAALHgALADRTVVMVTHHATELMPGDTLVRLGARERV 1126
Cdd:cd03298 166 EMLDLVLDLH-AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
355-555 |
1.00e-22 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 98.39 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVRgsVDGPDP--------RRI 426
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSG-SIL--IDGEDVrkeprearRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 427 AWVPQHPQFSERTVAAE-LALYAGAAGegaVPGEPGALVRELLDQLGLGGLEAADPA-ELSPGQQRRVAVARGLARVADg 504
Cdd:COG4555 77 GVLPDERGLYDRLTVREnIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPK- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 505 agLLLLDEPTAHLDDASAALVERAIAALA--GRvTVLLVSHEPRT-AALADRTV 555
Cdd:COG4555 153 --VLLLDEPTNGLDVMARRLLREILRALKkeGK-TVLFSSHIMQEvEALCDRVV 203
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
943-1111 |
1.37e-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: 97.24 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 943 DLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------PVAWCPQESHLFDS-TVRGNLAVARD- 1009
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqshtglapyqrPVSMLFQENNLFAHlTVRQNIGLGLHp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1010 --RDHAPSDAELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP---ES 1084
Cdd:TIGR01277 98 glKLNAEQQEKVVDAAQQVGIADYLDRLPEQL-----------SGGQRQRVALARCLVRPNPILLLDEPFSALDPllrEE 166
|
170 180
....*....|....*....|....*..
gi 1001866046 1085 GLALVAALhGALADRTVVMVTHHATEL 1111
Cdd:TIGR01277 167 MLALVKQL-CSERQRTLLMVTHHLSDA 192
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
923-1111 |
1.92e-22 |
|
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: 95.54 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPdVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG------------PVAWCP 990
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 QESHLFDS-TVRGNLAvardrdhapsdaeleavlarvgllehvrslpggldarigsrgafLSGGQRQRLAVARTLLAGAE 1069
Cdd:cd03230 80 EEPSLYENlTVRENLK--------------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1001866046 1070 VVLLDEPTAHLDPESGLALVAALHGaLADR--TVVMVTHHATEL 1111
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRE-LKKEgkTILLSSHILEEA 158
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
355-553 |
2.02e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.44 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--DGvgaSVRgsVDGPDP--------R 424
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRptSG---EVR--VLGEDVardpaevrR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 425 RIAWVPQHPQFSER-TVAAELALYAGAAGEgavpgePGALVRELLDQLGLGG--LEAAD--PAELSPGQQRRVAVARGLA 499
Cdd:COG1131 74 RIGYVPQEPALYPDlTVRENLRFFARLYGL------PRKEARERIDELLELFglTDAADrkVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 500 RVADgagLLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHEPRTA-ALADR 553
Cdd:COG1131 148 HDPE---LLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAeRLCDR 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
895-1106 |
2.94e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 895 RVAAEEQAVRDAAEERD---DLQDAPGRGPG---ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLAL 968
Cdd:COG0488 282 RIKALEKLEREEPPRRDktvEIRFPPPERLGkkvLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 969 LTGFLAP-----RVGSAAVagpVAWCPQESHLFDS--TVRGNLavardRDHAPSDAEleavlarvgllEHVRSLPGGL-- 1039
Cdd:COG0488 361 LAGELEPdsgtvKLGETVK---IGYFDQHQEELDPdkTVLDEL-----RDGAPGGTE-----------QEVRGYLGRFlf 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 1040 -----DARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESglalVAALHGALAD--RTVVMVTH 1106
Cdd:COG0488 422 sgddaFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET----LEALEEALDDfpGTVLLVSH 487
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
923-1106 |
4.11e-22 |
|
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: 96.50 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPD---VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG--------------- 984
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 985 -PVAWCPQESHLFDS-TVRGNLAVARDRDHAPSDAELEAVLArvgLLEHVrslpgGLDARIGSRGAFLSGGQRQRLAVAR 1062
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLE---LLELV-----GLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1001866046 1063 TLLAGAEVVLLDEPTAHLDPE---SGLALVAALHGALaDRTVVMVTH 1106
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPEttqSILALLRDINREL-GLTIVLITH 199
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
923-1107 |
4.37e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.88 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPD--VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------PVA 987
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 988 WCPQESHLFDSTVRGNLAVARDRdhaPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAG 1067
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGLTD---TPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1001866046 1068 AEVVLLDEPTAHLDPESGLALVAALhgALADRTVVMVTHH 1107
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQESR--SRASRTVLLIAHR 673
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
355-553 |
1.12e-21 |
|
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: 95.88 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVRgsVDGPD---------PRR 425
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSG-EVL--LDGRDlaslsrrelARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 IAWVPQHPQFSERTVAAELALYAGAAGEGAVPGEPG---ALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARva 502
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAedrEAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ-- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 503 dGAGLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAA-LADR 553
Cdd:COG1120 155 -EPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAArYADR 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
923-1106 |
1.21e-21 |
|
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: 94.57 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGpDVLAGLDLAARPGDWIVVaGPSGSGKSTLLALLTGFLAPRVGSAAVAGP------------VAWCP 990
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 QESHLFDS-TVRGNL---AVARDRDHAPSDAELEAVLARVGLLEHvrslpggLDARIGSrgafLSGGQRQRLAVARTLLA 1066
Cdd:cd03264 79 QEFGVYPNfTVREFLdyiAWLKGIPSKEVKARVDEVLELVNLGDR-------AKKKIGS----LSGGMRRRVGIAQALVG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1001866046 1067 GAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
356-557 |
1.32e-21 |
|
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: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 356 RVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVG-ASVRGSVDGPDPRRIAWVPQHPQ 434
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGsIRVFGKPLEKERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 435 FS-------ERTVAaeLALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagL 507
Cdd:cd03235 79 IDrdfpisvRDVVL--MGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD---L 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 508 LLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHEPRTA-ALADRTVEL 557
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVlEYFDRVLLL 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
923-1107 |
2.30e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 94.56 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG----------------PV 986
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 987 AWCPQESHLFD-STVRGNLAVARDRDHAP--------SDAELE---AVLARVGLLEHVRSlpggldarigsRGAFLSGGQ 1054
Cdd:cd03256 81 GMIFQQFNLIErLSVLENVLSGRLGRRSTwrslfglfPKEEKQralAALERVGLLDKAYQ-----------RADQLSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 1055 RQRLAVARTLLAGAEVVLLDEPTAHLDPESG---LALVAALHGALaDRTVVMVTHH 1107
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSrqvMDLLKRINREE-GITVIVSLHQ 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
909-1112 |
2.71e-21 |
|
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: 101.14 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 909 ERDDLQDAPGRGPGITLRGVTVGWT-GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLL-ALLTgfLAPRVGSAAVAGpV 986
Cdd:TIGR01271 1204 ENPHAQKCWPSGGQMDVQGLTAKYTeAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsALLR--LLSTEGEIQIDG-V 1280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 987 AW--------------CPQESHLFDSTVRGNLavarDRDHAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSG 1052
Cdd:TIGR01271 1281 SWnsvtlqtwrkafgvIPQKVFIFSGTFRKNL----DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSN 1356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1053 GQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHATELM 1112
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALL 1416
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
355-557 |
2.78e-21 |
|
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: 93.71 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAE--PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRdgvgaSVRGSV--DGPDP------- 423
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR-----PTSGEVrvDGTDIsklseke 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 424 ------RRIAWVPQHPQF-SERTVA--AELALYAGaageGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAV 494
Cdd:cd03255 76 laafrrRHIGFVFQSFNLlPDLTALenVELPLLLA----GVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 495 ARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAG--RVTVLLVSHEPRTAALADRTVEL 557
Cdd:cd03255 152 ARALANDPK---IILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIEL 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
355-555 |
6.10e-21 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 92.53 E-value: 6.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEP--AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRG-SVDGPDPRRiAWVP 430
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEvLVDGePVTGPGPDR-GYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 431 QHPQ-FSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARvadGAGLLL 509
Cdd:cd03293 80 QQDAlLPWLTVLDNVAL--GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAV---DPDVLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 510 LDEPTAHLDDASAALVERAIAAL--AGRVTVLLVSHEPRTA-ALADRTV 555
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAvFLADRVV 203
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
355-555 |
9.01e-21 |
|
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: 92.18 E-value: 9.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWY--DGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLvrdgvGASVRGSV--DGPDP------- 423
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGL-----LKPTSGSIifDGKDLlklsrrl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 424 -----RRIAWVPQHPQFS---ERTVA---AELALYAGaagegavPGEPGALVRELLDQLGLGGLEAAD-----PAELSPG 487
Cdd:cd03257 77 rkirrKEIQMVFQDPMSSlnpRMTIGeqiAEPLRIHG-------KLSKKEARKEAVLLLLVGVGLPEEvlnryPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 488 QQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAA-LADRTV 555
Cdd:cd03257 150 QRQRVAIARALALNPK---LLIADEPTSALDVSVQAQILDLLKKLQEElgLTLLFITHDLGVVAkIADRVA 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
923-1112 |
1.06e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 95.14 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAP-----RVGSAAVAGpVAwcPQE---SH 994
Cdd:COG3839 4 LELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPtsgeiLIGGRDVTD-LP--PKDrniAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 995 LFDS-------TVRGNLAVA---RDRDHAPSDAELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTL 1064
Cdd:COG3839 80 VFQSyalyphmTVYENIAFPlklRKVPKAEIDRRVREAAELLGLEDLLDRKPKQL-----------SGGQRQRVALGRAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1065 LAGAEVVLLDEPTAHLDPESGLAL---VAALHGALaDRTVVMVTHHATELM 1112
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMraeIKRLHRRL-GTTTIYVTHDQVEAM 198
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
934-1106 |
1.18e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP--VAWCPQESHLFDS-TVRGNL------ 1004
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrIGYLPQEPPLDDDlTVLDTVldgdae 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1005 --AVARDRDHAPSD-AELEAVLARVGLLEH-------------VRSLPGGL-------DARIGSrgafLSGGQRQRLAVA 1061
Cdd:COG0488 89 lrALEAELEELEAKlAEPDEDLERLAELQEefealggweaearAEEILSGLgfpeedlDRPVSE----LSGGWRRRVALA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1001866046 1062 RTLLAGAEVVLLDEPTAHLDPESglalVAALHGALADR--TVVMVTH 1106
Cdd:COG0488 165 RALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYpgTVLVVSH 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
919-1110 |
1.37e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 94.78 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 919 RGPGITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------PVA 987
Cdd:COG3842 2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppekrNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 988 WCPQESHLFDS-TVRGNLAVA-RDRDHAPSDAE--LEAVLARVGLlehvrslpGGLDARigsRGAFLSGGQRQRLAVART 1063
Cdd:COG3842 81 MVFQDYALFPHlTVAENVAFGlRMRGVPKAEIRarVAELLELVGL--------EGLADR---YPHQLSGGQQQRVALARA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1064 LLAGAEVVLLDEPTAHLDP---ESGLALVAALHGALaDRTVVMVTHHATE 1110
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAklrEEMREELRRLQREL-GITFIYVTHDQEE 198
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
933-1123 |
1.51e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.70 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 933 TGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-------------VAWCPQESHLFDST 999
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1000 VRGNLAVA-RDRDHAPSDAELEAVLARVGLLEHVrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTA 1078
Cdd:PRK10247 97 VYDNLIFPwQIRNQQPDPAIFLDDLERFALPDTI------LTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1001866046 1079 HLDPESGLALVAALHGALADR--TVVMVTHHATELMPGDTLVRLGAR 1123
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITLQPH 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
932-1112 |
1.82e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 90.30 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 932 WTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLA-PRV-GSAAVAGP----------VAWCPQESHLFDS- 998
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTgLGVsGEVLINGRpldkrsfrkiIGYVPQDDILHPTl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 TVRGNLAVArdrdhapsdAELeavlarvgllehvrslpggldarigsRGafLSGGQRQRLAVARTLLAGAEVVLLDEPTA 1078
Cdd:cd03213 98 TVRETLMFA---------AKL--------------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 1001866046 1079 HLDPESGLALVAALHgALAD--RTVVMVTHHATELM 1112
Cdd:cd03213 141 GLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEI 175
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
355-557 |
1.85e-20 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 89.76 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDGPDP--------RRI 426
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG---EIKVLGKDIkkepeevkRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 427 AWVPQHPQFSERTVAAELAlyagaagegavpgepgalvrelldqlglggleaadpaELSPGQQRRVAVARGLARVADgag 506
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPE--- 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 507 LLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHEPRTA-ALADRTVEL 557
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAeRLCDRVAIL 168
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
935-1106 |
2.46e-20 |
|
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: 97.12 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 935 GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-------------VAWCPQESHLFDSTVR 1001
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 GNLAVArdrdhAPSDAELEAVLARVGLLE---HVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTA 1078
Cdd:TIGR01193 566 ENLLLG-----AKENVSQDEIWAACEIAEikdDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180
....*....|....*....|....*...
gi 1001866046 1079 HLDPESGLALVAALHgALADRTVVMVTH 1106
Cdd:TIGR01193 641 NLDTITEKKIVNNLL-NLQDKTIIFVAH 667
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
355-557 |
2.58e-20 |
|
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: 89.20 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVRgsVDGPDPRRIAWVPQHPQ 434
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSG-RVR--LDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 435 FSerTVAAELALYAGAAGEGAvpgepgalvrelldqlglggleaadpaeLSPGQQRRVAVARGLARvadGAGLLLLDEPT 514
Cdd:cd03246 78 VG--YLPQDDELFSGSIAENI----------------------------LSGGQRQRLGLARALYG---NPRILVLDEPN 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1001866046 515 AHLDDASAALVERAIAAL-AGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:cd03246 125 SHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVL 168
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
923-1106 |
2.60e-20 |
|
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: 89.20 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGG-PDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAP-----RVGSAAVA--------GPVAW 988
Cdd:cd03246 1 LEVENVSFRYPGAePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPtsgrvRLDGADISqwdpnelgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 989 CPQESHLFDSTVRGNLavardrdhapsdaeleavlarvgllehvrslpggldarigsrgafLSGGQRQRLAVARTLLAGA 1068
Cdd:cd03246 81 LPQDDELFSGSIAENI---------------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 1069 EVVLLDEPTAHLDPESGLALVAALHGA-LADRTVVMVTH 1106
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAH 154
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
900-1131 |
3.56e-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: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 900 EQAVRdAAEERDDLQDAPGRGPG----------ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALL 969
Cdd:PRK10790 309 QQAVV-AGERVFELMDGPRQQYGnddrplqsgrIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 970 TGFLAPRVGS-------------AAVAGPVAWCPQESHLFDSTVRGNLAVARDrdhaPSDAELEAVLARVGLLEHVRSLP 1036
Cdd:PRK10790 388 MGYYPLTEGEirldgrplsslshSVLRQGVAMVQQDPVVLADTFLANVTLGRD----ISEEQVWQALETVQLAELARSLP 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1037 GGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHATELMPGDT 1116
Cdd:PRK10790 464 DGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADT 543
|
250
....*....|....*
gi 1001866046 1117 LVrlgarerVLHHAA 1131
Cdd:PRK10790 544 IL-------VLHRGQ 551
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
907-1105 |
3.59e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 97.50 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 907 AEERDDLQDAPGRG--PGITLRGVTVGW--TGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRV-GSAA 981
Cdd:PLN03130 597 AEERVLLPNPPLEPglPAISIKNGYFSWdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVV 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 982 VAGPVAWCPQESHLFDSTVRGNLAVArdrdhAPSDAELEAVLARVGLLEH-VRSLPGGLDARIGSRGAFLSGGQRQRLAV 1060
Cdd:PLN03130 677 IRGTVAYVPQVSWIFNATVRDNILFG-----SPFDPERYERAIDVTALQHdLDLLPGGDLTEIGERGVNISGGQKQRVSM 751
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1001866046 1061 ARTLLAGAEVVLLDEPTAHLDPESGLALV-AALHGALADRTVVMVT 1105
Cdd:PLN03130 752 ARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDELRGKTRVLVT 797
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
355-557 |
4.12e-20 |
|
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: 90.47 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVRgsVDGPDP---------RR 425
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSG-EVL--VDGKDItkknlrelrRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 IAWVPQHP--QFSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLA---R 500
Cdd:COG1122 77 VGLVFQNPddQLFAPTVEEDVAF--GPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAmepE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 501 VadgaglLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHEPRTAA-LADRTVEL 557
Cdd:COG1122 155 V------LVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAeLADRVIVL 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
355-555 |
5.71e-20 |
|
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: 88.40 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--------DGVGASVRGSVDGPDPRRI 426
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpdsgsiliDGEDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 427 AWVPQHPQ-FSERTVAAELALyagaagegavpgepgalvrelldqlglggleaadpaELSPGQQRRVAVARGLARVADga 505
Cdd:cd03229 79 GMVFQDFAlFPHLTVLENIAL------------------------------------GLSGGQQQRVALARALAMDPD-- 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 506 gLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAA-LADRTV 555
Cdd:cd03229 121 -VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAArLADRVV 172
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
923-1131 |
6.36e-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: 90.44 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------PVA------WC 989
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdPVElrrkigYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 PQESHLFDS-TVRGNLAVARDRDHAPSdaelEAVLARVG-LLEHVRSLPGGLDARIGSRgafLSGGQRQRLAVARTLLAG 1067
Cdd:cd03295 81 IQQIGLFPHmTVEENIALVPKLLKWPK----EKIRERADeLLALVGLDPAEFADRYPHE---LSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 1068 AEVVLLDEPTAHLDPESGLAL---VAALHGALAdRTVVMVTHHATE---------LMPGDTLVRLGARERVLHHAA 1131
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLqeeFKRLQQELG-KTIVFVTHDIDEafrladriaIMKNGEIVQVGTPDEILRSPA 228
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
934-1106 |
6.99e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 90.63 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCPQE-------------------- 992
Cdd:COG4598 19 GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeEIRLKPDRdgelvpadrrqlqrirtrlg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 993 ---------SHLfdsTVRGNLAVA------RDRDHAPSDAEleAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQR 1057
Cdd:COG4598 99 mvfqsfnlwSHM---TVLENVIEApvhvlgRPKAEAIERAE--ALLAKVGLADKRDAYP-----------AHLSGGQQQR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 1058 LAVARTLLAGAEVVLLDEPTAHLDPEsglaLVA---ALHGALAD--RTVVMVTH 1106
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPE----LVGevlKVMRDLAEegRTMLVVTH 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
355-555 |
7.73e-20 |
|
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: 89.49 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVG-ASVRGSVDGPDP----RRIAWV 429
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtAYINGYSIRTDRkaarQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 430 PQH-PQFSERTVAAELALYAGAAGegaVPGEPGALVRELLDQLGLGGLEAADPA-ELSPGQQRRVAVArgLARVADGAgL 507
Cdd:cd03263 81 PQFdALFDELTVREHLRFYARLKG---LPKSEIKEEVELLLRVLGLTDKANKRArTLSGGMKRKLSLA--IALIGGPS-V 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 508 LLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTA-ALADRTV 555
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIA 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
923-1106 |
8.01e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 89.39 E-value: 8.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCP----------- 990
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRgraipylrrki 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 ----QESHLF-DSTVRGNLAVA-RDRDHAPSDAE--LEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVAR 1062
Cdd:cd03292 81 gvvfQDFRLLpDRNVYENVAFAlEVTGVPPREIRkrVPAALELVGLSHKHRALPAEL-----------SGGEQQRVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1001866046 1063 TLLAGAEVVLLDEPTAHLDPESGLALVAALHGA-LADRTVVMVTH 1106
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATH 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
923-1114 |
8.38e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 90.14 E-value: 8.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVgWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVG------------------------ 978
Cdd:COG1119 4 LELRNVTV-RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvwelrkrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 979 -SAAVAgpvAWCPQE--------SHLFDSTVRGNLAVARDRDHApsdaelEAVLARVGLlEHVRslpgglDARIGSrgaf 1049
Cdd:COG1119 83 vSPALQ---LRFPRDetvldvvlSGFFDSIGLYREPTDEQRERA------RELLELLGL-AHLA------DRPFGT---- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 1050 LSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALhGALA---DRTVVMVTHHATELMPG 1114
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALL-DKLAaegAPTLVLVTHHVEEIPPG 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
356-555 |
1.04e-19 |
|
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: 87.88 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 356 RVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVRgsVDGPDP---------RRI 426
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG-EIL--LDGKDLaslspkelaRKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 427 AWVPQhpqFSERTVAAELALyagaagegavpgepgalvRELLdqlglggleaadpaELSPGQQRRVAVARGLARVADgag 506
Cdd:cd03214 76 AYVPQ---ALELLGLAHLAD------------------RPFN--------------ELSGGERQRVLLARALAQEPP--- 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 507 LLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAAL-ADRTV 555
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLNLAARyADRVI 169
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
949-1126 |
1.50e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 95.23 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 949 GDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESHLFDSTVRGNLAVardrdHAPSDAELEAVLARVGL 1028
Cdd:PTZ00243 686 GKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILF-----FDEEDAARLADAVRVSQ 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1029 LE-HVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVA-ALHGALADRTVVMVTH 1106
Cdd:PTZ00243 761 LEaDLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEeCFLGALAGKTRVLATH 840
|
170 180
....*....|....*....|
gi 1001866046 1107 HATELMPGDTLVRLGaRERV 1126
Cdd:PTZ00243 841 QVHVVPRADYVVALG-DGRV 859
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
923-1106 |
1.55e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 85.96 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPdVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSaavagpVAWcpqeshlfDSTVRg 1002
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI------VTW--------GSTVK- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1003 nlavardrdhapsdaeleavlarVGLLEHvrslpggldarigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:cd03221 65 -----------------------IGYFEQ------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180
....*....|....*....|....*.
gi 1001866046 1083 ESglalVAALHGALAD--RTVVMVTH 1106
Cdd:cd03221 104 ES----IEALEEALKEypGTVILVSH 125
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
346-554 |
1.67e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 89.33 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 346 PAGQAAPAGLRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSV--DG--- 420
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGD--KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEIllDGedi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 421 --P--DP----RRIAWVPQHPQ---FS-ERTVAAELALYaGAAGegavPGEPGALVRELLDqlglgglEAA--------- 479
Cdd:COG1117 81 ydPdvDVvelrRRVGMVFQKPNpfpKSiYDNVAYGLRLH-GIKS----KSELDEIVEESLR-------KAAlwdevkdrl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 480 -DPA-ELSPGQQRRVAVARGLA---RVadgaglLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAA-LADR 553
Cdd:COG1117 149 kKSAlGLSGGQQQRLCIARALAvepEV------LLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAArVSDY 222
|
.
gi 1001866046 554 T 554
Cdd:COG1117 223 T 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
924-1105 |
1.78e-19 |
|
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: 88.89 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 924 TLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------P-------VAWC 989
Cdd:COG0410 5 EVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglpPhriarlgIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 PQESHLFDS-TVRGNLAVA--RDRDHAPSDAELEAVLARVGLLEhvrslpggldARIGSRGAFLSGGQRQRLAVARTLLA 1066
Cdd:COG0410 84 PEGRRIFPSlTVEENLLLGayARRDRAEVRADLERVYELFPRLK----------ERRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1067 GAEVVLLDEPTAHLDP--------------ESGLALV-------AALhgALADRTVVMVT 1105
Cdd:COG0410 154 RPKLLLLDEPSLGLAPliveeifeiirrlnREGVTILlveqnarFAL--EIADRAYVLER 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
923-1106 |
2.05e-19 |
|
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: 89.09 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPD---VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------PVAWCPQE 992
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 993 SHLF-DS--------TVRGNLA-VARDRDHAPSDAELEAVLARVGLLEHVRSlpggldarigSRGAFLSGGQRQRLAVAR 1062
Cdd:COG1124 82 QMVFqDPyaslhprhTVDRILAePLRIHGLPDREERIAELLEQVGLPPSFLD----------RYPHQLSGGQRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1001866046 1063 TLLAGAEVVLLDEPTAHLDPeSGLALVAALHGALADR---TVVMVTH 1106
Cdd:COG1124 152 ALILEPELLLLDEPTSALDV-SVQAEILNLLKDLREErglTYLFVSH 197
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
923-1106 |
2.26e-19 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 86.86 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVgWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGpvawcpqeshlfdstvrg 1002
Cdd:cd03229 1 LELKNVSK-RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1003 nlavardRDHAPSDAELEAVLARVGLLEHVRSLPGGLDARiGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:cd03229 62 -------EDLTDLEDELPPLRRRIGMVFQDFALFPHLTVL-ENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180
....*....|....*....|....*..
gi 1001866046 1083 ESG---LALVAALHgALADRTVVMVTH 1106
Cdd:cd03229 134 ITRrevRALLKSLQ-AQLGITVVLVTH 159
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
923-1111 |
2.58e-19 |
|
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: 89.03 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPD-VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAwcPQESHLFD---- 997
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEirkk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 998 --------------STVR-----G--NLAVARDrdhapsdaEL----EAVLARVGLLEHVRSLPggldarigsrgAFLSG 1052
Cdd:TIGR04520 79 vgmvfqnpdnqfvgATVEddvafGleNLGVPRE--------EMrkrvDEALKLVGMEDFRDREP-----------HLLSG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 1053 GQRQRLAVARTLLAGAEVVLLDEPTAHLDPESG---LALVAALHgALADRTVVMVTHHATEL 1111
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRkevLETIRKLN-KEEGITVISITHDMEEA 200
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
934-1122 |
2.98e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPrvgsaaVAGPVAWCPQESHLFDS--------------- 998
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP------AAGTIKLDGGDIDDPDVaeachylghrnamkp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 --TVRGNLAVARDRdHAPSDAELEAVLARVGLlEHVRSLPGGldarigsrgaFLSGGQRQRLAVARTLLAGAEVVLLDEP 1076
Cdd:PRK13539 87 alTVAENLEFWAAF-LGGEELDIAAALEAVGL-APLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1001866046 1077 TAHLDPeSGLALVAALHGALADR--TVVMVTHHATELmPGDTLVRLGA 1122
Cdd:PRK13539 155 TAALDA-AAVALFAELIRAHLAQggIVIAATHIPLGL-PGARELDLGP 200
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
370-557 |
3.23e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.90 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 370 PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRdgvgaSVRGSVDGPDPRRIAWVPQHPQFSER---TV--AAEL 444
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR-----PTSGTVRRAGGARVAYVPQRSEVPDSlplTVrdLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 445 ALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAAL 524
Cdd:NF040873 81 GRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEAD---LLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 525 VERAIAALAGR-VTVLLVSHEPRTAALADRTVEL 557
Cdd:NF040873 158 IIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
924-1106 |
3.28e-19 |
|
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: 92.69 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 924 TLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAaVAGP---VAWCPQESHLFDS-T 999
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA-RPQPgikVGYLPQEPQLDPTkT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1000 VRGN--LAVARDRD-----------HAPSDAELEAVLARVGLLE-------------------HVRSLPGGlDARIGSrg 1047
Cdd:TIGR03719 85 VRENveEGVAEIKDaldrfneisakYAEPDADFDKLAAEQAELQeiidaadawdldsqleiamDALRCPPW-DADVTK-- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1048 afLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESglalVAALHGALADR--TVVMVTH 1106
Cdd:TIGR03719 162 --LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYpgTVVAVTH 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
949-1107 |
8.32e-19 |
|
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: 87.89 E-value: 8.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 949 GDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQ------------------ESHLFDSTVR-------GN 1003
Cdd:TIGR04521 31 GEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKkkklkdlrkkvglvfqfpEHQLFEETVYkdiafgpKN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1004 LAVardrdhapSDAELEAvlaRV-GLLEHVrslpgGLDARIGSRGAF-LSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:TIGR04521 111 LGL--------SEEEAEE---RVkEALELV-----GLDEEYLERSPFeLSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180
....*....|....*....|....*....
gi 1001866046 1082 PESG---LALVAALHGAlADRTVVMVTHH 1107
Cdd:TIGR04521 175 PKGRkeiLDLFKRLHKE-KGLTVILVTHS 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
922-1125 |
1.19e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.61 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 922 GITLRGVTVGWTGGPdVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRV---------GSAAVAGP-----VA 987
Cdd:COG4136 1 MLSLENLTITLGGRP-LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasgevllnGRRLTALPaeqrrIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 988 WCPQESHLFDS-TVRGNLAVA--RDRDHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTL 1064
Cdd:COG4136 80 ILFQDDLLFPHlSVGENLAFAlpPTIGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 1065 LAGAEVVLLDEPTAHLDPESGLALVAALHGALADRT--VVMVTHHATELMPGDTLVRLGARER 1125
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGipALLVTHDEEDAPAAGRVLDLGNWQH 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
923-1112 |
1.43e-18 |
|
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: 86.14 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCP----------Q 991
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLPphkrpvntvfQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 992 ESHLFDS-TVRGNLAVA---RDRDHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAG 1067
Cdd:cd03300 80 NYALFPHlTVFENIAFGlrlKKLPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1001866046 1068 AEVVLLDEPTAHLDP---ESGLALVAALHGALAdRTVVMVTHHATELM 1112
Cdd:cd03300 149 PKVLLLDEPLGALDLklrKDMQLELKRLQKELG-ITFVFVTHDQEEAL 195
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
934-1106 |
1.46e-18 |
|
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: 84.78 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCPQ----------------ESHLF 996
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGePLDYSRKgllerrqrvglvfqdpDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 997 DSTVRGNLAVArDRDHAPSDAELEAV----LARVGLLeHVRSLPGGLdarigsrgafLSGGQRQRLAVARTLLAGAEVVL 1072
Cdd:TIGR01166 83 AADVDQDVAFG-PLNLGLSEAEVERRvreaLTAVGAS-GLRERPTHC----------LSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1001866046 1073 LDEPTAHLDPESGLALVAALHGALAD-RTVVMVTH 1106
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTH 185
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
374-515 |
1.89e-18 |
|
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: 83.08 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 374 PLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA------SVRGSVDGPDPRRIAWVPQHPQFSERTVAAE---L 444
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqDLTDDERKSLRKEIGYVFQDPQLFPRLTVREnlrL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 445 ALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARvadGAGLLLLDEPTA 515
Cdd:pfam00005 83 GLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLT---KPKLLLLDEPTA 150
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
934-1106 |
2.25e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.91 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLL------------ALLTGFLAPRVGSAAV------AGPVAwcpQESHL 995
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinkleeitsgDLIVDGLKVNDPKVDErlirqeAGMVF---QQFYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 996 FDS-TVRGNLAVA--RDRDHAPSDAELEA--VLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAEV 1070
Cdd:PRK09493 89 FPHlTALENVMFGplRVRGASKEEAEKQAreLLAKVGLAERAHHYP-----------SELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1001866046 1071 VLLDEPTAHLDPEsglaL---VAALHGALADR--TVVMVTH 1106
Cdd:PRK09493 158 MLFDEPTSALDPE----LrheVLKVMQDLAEEgmTMVIVTH 194
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
938-1107 |
4.45e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCPQE------SHLF---------DSTVR 1001
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkDVTKLPEYkrakyiGRVFqdpmmgtapSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 GNLAVARDRDHAPS---------DAELEAVLARVGL-LEHvRslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVV 1071
Cdd:COG1101 101 ENLALAYRRGKRRGlrrgltkkrRELFRELLATLGLgLEN-R-----LDTKVGL----LSGGQRQALSLLMATLTKPKLL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 1072 LLDEPTAHLDPESGlALVAALHGALADR---TVVMVTHH 1107
Cdd:COG1101 171 LLDEHTAALDPKTA-ALVLELTEKIVEEnnlTTLMVTHN 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
934-1113 |
4.45e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.56 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPrvgsaaVAGPVAWCPQESHLFD-------------STV 1000
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP------DSGEVRWNGTPLAEQRdephenilylghlPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 RGNLAVARD-----RDHAPSDAELEAVLARVGLLeHVRSLPGgldarigsrgAFLSGGQRQRLAVARTLLAGAEVVLLDE 1075
Cdd:TIGR01189 85 KPELSALENlhfwaAIHGGAQRTIEDALAAVGLT-GFEDLPA----------AQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1001866046 1076 PTAHLDPEsGLALVAALHGALADR--TVVMVTHHATELMP 1113
Cdd:TIGR01189 154 PTTALDKA-GVALLAGLLRAHLARggIVLLTTHQDLGLVE 192
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
922-1106 |
4.85e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 84.68 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 922 GITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG----------------- 984
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpsekairll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 985 --PVAWCPQESHLFDS-TVRGNL--AVARDRDHAPSDAELEA--VLARVGLLEHVRSLPggldarigsrgAFLSGGQRQR 1057
Cdd:COG4161 81 rqKVGMVFQQYNLWPHlTVMENLieAPCKVLGLSKEQAREKAmkLLARLRLTDKADRFP-----------LHLSGGQQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1058 LAVARTLLAGAEVVLLDEPTAHLDPESgLALVAALHGALADR--TVVMVTH 1106
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEI-TAQVVEIIRELSQTgiTQVIVTH 199
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
925-1107 |
1.43e-17 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 83.26 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 925 LRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCP------------- 990
Cdd:cd03219 3 VRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeDITGLPpheiarlgigrtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 QESHLFDS-TVRGNLAVARDRDH------APSDAELEAVLARVG-LLEHVrslpgGLDARIGSRGAFLSGGQRQRLAVAR 1062
Cdd:cd03219 82 QIPRLFPElTVLENVMVAAQARTgsglllARARREEREARERAEeLLERV-----GLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1001866046 1063 TLLAGAEVVLLDEPTAHLDPESGLALVAALHG-ALADRTVVMVTHH 1107
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVLLVEHD 202
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
934-1106 |
1.93e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.14 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------------PVAWCPQESH 994
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdkairelrrNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 995 LFDS-TVRGNLAVARDR----DHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAE 1069
Cdd:PRK11124 93 LWPHlTVQQNLIEAPCRvlglSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 1070 VVLLDEPTAHLDPESGLALVAALHGaLADR--TVVMVTH 1106
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRE-LAETgiTQVIVTH 199
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
921-1136 |
2.02e-17 |
|
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: 86.88 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWTGGP-DVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRV---GSAAVAGP----------- 985
Cdd:COG1123 3 PLLEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRdllelsealrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 986 --VAWCPQE--SHLFDSTVRGNLAVARDRDHAPSDAELEAVLArvgLLEHVrslpgGLDARIGSRGAFLSGGQRQRLAVA 1061
Cdd:COG1123 83 rrIGMVFQDpmTQLNPVTVGDQIAEALENLGLSRAEARARVLE---LLEAV-----GLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1062 RTLLAGAEVVLLDEPTAHLDPESG---LALVAALHGALaDRTVVMVTHHATE---------LMPGDTLVRLGARERVLHH 1129
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQaeiLDLLRELQRER-GTTVLLITHDLGVvaeiadrvvVMDDGRIVEDGPPEEILAA 233
|
....*..
gi 1001866046 1130 AARAAAP 1136
Cdd:COG1123 234 PQALAAV 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
938-1130 |
2.48e-17 |
|
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: 82.38 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------P----VAWCPQESHLF-DSTVRGNLA 1005
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlpPekrdISYVPQNYALFpHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1006 VA---RDRDHAPSDAELEAVLARVGLlEHVrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:cd03299 94 YGlkkRKVDKKEIERKVLEIAEMLGI-DHL------LNRKPET----LSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1083 ---ESGLALVAALHgALADRTVVMVTHHATE---------LMPGDTLVRLGARERVLHHA 1130
Cdd:cd03299 163 rtkEKLREELKKIR-KEFGVTVLHVTHDFEEawaladkvaIMLNGKLIQVGKPEEVFKKP 221
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
937-1081 |
2.51e-17 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 82.01 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 937 DVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------------PVAWCPQESHLF-DS 998
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGqslsklssneraklrnkKLGFIYQFHHLLpDF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 TVRGNLAVA-----RDRDHAPSDAEleavlarvGLLEHVrslpgGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLL 1073
Cdd:TIGR02211 99 TALENVAMPlligkKSVKEAKERAY--------EMLEKV-----GLEHRINHRPSELSGGERQRVAIARALVNQPSLVLA 165
|
....*...
gi 1001866046 1074 DEPTAHLD 1081
Cdd:TIGR02211 166 DEPTGNLD 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
923-1103 |
2.54e-17 |
|
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: 82.17 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPD---VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG--------------- 984
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 985 -PVAWCPQEShlFDS-----TVRGNLA-VARDRDHAPSDAELEAVLARvgLLEHVrslpgGLDARIGSRGAF-LSGGQRQ 1056
Cdd:cd03257 82 kEIQMVFQDP--MSSlnprmTIGEQIAePLRIHGKLSKKEARKEAVLL--LLVGV-----GLPEEVLNRYPHeLSGGQRQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 1057 RLAVARTLLAGAEVVLLDEPTAHLDP---------------ESGLALVAALH-----GALADRTVVM 1103
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVsvqaqildllkklqeELGLTLLFITHdlgvvAKIADRVAVM 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
934-1107 |
2.56e-17 |
|
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: 83.16 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCP-------------QESHLFDS- 998
Cdd:COG0411 15 GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrDITGLPphriarlgiartfQNPRLFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 TVRGNLAVARD------------------RDHAPSDAELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAV 1060
Cdd:COG0411 95 TVLENVLVAAHarlgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNL-----------SYGQQRRLEI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 1061 ARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADR--TVVMVTHH 1107
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHD 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
890-1106 |
2.69e-17 |
|
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: 86.50 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 890 RSALVRVAAEEQAVRDAAEERDDLQDAPGRGPGITLRGVTV----GWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTL 965
Cdd:COG1123 228 EEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKrypvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 966 LALLTGFLAPRVGSAAVAG-PVAWCPQES----------------HLFDS--TVRGNLAVARDRDHAPSDAELEAVLARv 1026
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDGkDLTKLSRRSlrelrrrvqmvfqdpySSLNPrmTVGDIIAEPLRLHGLLSRAERRERVAE- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1027 gLLEHVrslpgGLDARIGSRGAF-LSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPeSGLALVAALHGALADR---TVV 1102
Cdd:COG1123 387 -LLERV-----GLPPDLADRYPHeLSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAQILNLLRDLQRElglTYL 459
|
....
gi 1001866046 1103 MVTH 1106
Cdd:COG1123 460 FISH 463
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
923-1106 |
3.39e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.65 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGfLAPRVGSAAVAGPVAWCPQESHLFDS---- 998
Cdd:PRK14247 4 IEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNR-LIELYPEARVSGEVYLDGQDIFKMDVielr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 ----------------TVRGNLAVARDRDH-APSDAELEA----VLARVGLLEHVRSlpggldaRIGSRGAFLSGGQRQR 1057
Cdd:PRK14247 82 rrvqmvfqipnpipnlSIFENVALGLKLNRlVKSKKELQErvrwALEKAQLWDEVKD-------RLDAPAGKLSGGQQQR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 1058 LAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
921-1106 |
3.75e-17 |
|
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: 82.10 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGV--TVGWTGGP-DVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP------------ 985
Cdd:COG4181 7 PIIELRGLtkTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfaldedarar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 986 -----VAWCPQESHLFDS-TVRGNLAV----ARDRDHApsdAELEAVLARVGLLEHVRSLPGGldarigsrgafLSGGQR 1055
Cdd:COG4181 87 lrarhVGFVFQSFQLLPTlTALENVMLplelAGRRDAR---ARARALLERVGLGHRLDHYPAQ-----------LSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 1056 QRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADR--TVVMVTH 1106
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTH 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
338-557 |
4.81e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.01 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 338 RVQDAERPPAGQAAPAGLRVAGLTVW-YDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGvgasvRG 416
Cdd:COG4178 346 DALPEAASRIETSEDGALALEDLTLRtPDG--RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-----SG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 417 SVDGPDPRRIAWVPQHPQFSERTVAAELALyagaagegavPGEPGALVRELLDQL---------GLGGLEAAD-PAELSP 486
Cdd:COG4178 419 RIARPAGARVLFLPQRPYLPLGTLREALLY----------PATAEAFSDAELREAleavglghlAERLDEEADwDQVLSL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 487 GQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:COG4178 489 GEQQRLAFARLLLHKPD---WLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLEL 556
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
375-553 |
5.19e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 81.78 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVG---------ASVRGSVDGPDPRRIAWVPQHPQ-FSERTVAAEL 444
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGevlidgediSGLSEAELYRLRRRMGMLFQSGAlFDSLTVFENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 445 ALYAGAAGEGaVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAAL 524
Cdd:cd03261 99 AFPLREHTRL-SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE---LLLYDEPTAGLDPIASGV 174
|
170 180 190
....*....|....*....|....*....|..
gi 1001866046 525 VERAIAALAGR--VTVLLVSHE-PRTAALADR 553
Cdd:cd03261 175 IDDLIRSLKKElgLTSIMVTHDlDTAFAIADR 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
934-1103 |
5.31e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.13 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVA-W-----------CPQESHL-FDST 999
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrPLAdWspaelarrravLPQHSSLsFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1000 VR-----GNLAVARDRDHApsDAELEAVLARVGL--LEHvRSLPGgldarigsrgafLSGGQRQRLAVARTLL------A 1066
Cdd:PRK13548 93 VEevvamGRAPHGLSRAED--DALVAAALAQVDLahLAG-RDYPQ------------LSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 1067 GAEVVLLDEPTAHLDP---------------ESGLALVAALH-----GALADRTVVM 1103
Cdd:PRK13548 158 PPRWLLLDEPTSALDLahqhhvlrlarqlahERGLAVIVVLHdlnlaARYADRIVLL 214
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
932-1120 |
5.47e-17 |
|
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: 81.22 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 932 WTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFL------------APRVGSAAVA-----GPVAWCPQESH 994
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMqtlegkvhwsnkNESEPSFEATrsrnrYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 995 LFDSTVRGNLAVArdrdhAPSDAE-LEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLL 1073
Cdd:cd03290 90 LLNATVEENITFG-----SPFNKQrYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1074 DEPTAHLDPE-SGLALVAALHGALAD--RTVVMVTHHATELMPGDTLVRL 1120
Cdd:cd03290 165 DDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAM 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
923-1109 |
5.47e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 79.51 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGfLAP----RVGSAAVAGpVAWCPQESHLFDS 998
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwgsgRIGMPEGED-LLFLPQRPYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 TVRGNLAVardrdhaPSDAELeavlarvgllehvrslpggldarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTA 1078
Cdd:cd03223 79 TLREQLIY-------PWDDVL-------------------------------SGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190
....*....|....*....|....*....|.
gi 1001866046 1079 HLDPESGLALVAALHGALAdrTVVMVTHHAT 1109
Cdd:cd03223 121 ALDEESEDRLYQLLKELGI--TVISVGHRPS 149
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
353-555 |
5.53e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 83.97 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 353 AGLRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGL--VRDGvgaSVRgsVDG-------PDP 423
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLedPTSG---EIL--IGGrdvtdlpPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 424 RRIAWVPQHPqfsertvaaelALYagaagegavP---------------GEPGALVRELLDqlglgglEAAD-------- 480
Cdd:COG3839 75 RNIAMVFQSY-----------ALY---------PhmtvyeniafplklrKVPKAEIDRRVR-------EAAEllgledll 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 481 ---PAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDdasAALVERAIAALAG-----RVTVLLVSHEPRTA-ALA 551
Cdd:COG3839 128 drkPKQLSGGQRQRVALGRALVR---EPKVFLLDEPLSNLD---AKLRVEMRAEIKRlhrrlGTTTIYVTHDQVEAmTLA 201
|
....
gi 1001866046 552 DRTV 555
Cdd:COG3839 202 DRIA 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
935-1106 |
6.82e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.72 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 935 GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAP-----RVGSAAVAGPVAWCPQES---------------- 993
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPeagtiRVGDITIDTARSLSQQKGlirqlrqhvgfvfqnf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 994 HLF-DSTVRGNL----AVARDRDHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGA 1068
Cdd:PRK11264 95 NLFpHRTVLENIiegpVIVKGEPKEEATARARELLAKVGLAGKETSYP-----------RRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1001866046 1069 EVVLLDEPTAHLDPE---SGLALVAALhgALADRTVVMVTH 1106
Cdd:PRK11264 164 EVILFDEPTSALDPElvgEVLNTIRQL--AQEKRTMVIVTH 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
377-547 |
7.11e-17 |
|
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: 79.90 E-value: 7.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 377 FTAPAGRVTVLAGPSGSGKTTVLAALAGLVRdgvGASVRGSV--DGPD------PRRIAWVPQHPQFSERTVAAELALYA 448
Cdd:cd03213 30 GKAKPGELTAIMGPSGAGKSTLLNALAGRRT---GLGVSGEVliNGRPldkrsfRKIIGYVPQDDILHPTLTVRETLMFA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 449 gaagegavpgepgALVRElldqlglggleaadpaeLSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERA 528
Cdd:cd03213 107 -------------AKLRG-----------------LSGGERKRVSIALELVS---NPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180
....*....|....*....|.
gi 1001866046 529 IAALA--GRvTVLLVSHEPRT 547
Cdd:cd03213 154 LRRLAdtGR-TIICSIHQPSS 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
937-1106 |
7.55e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.55 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 937 DVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGpvawcpQESHLFDSTvrgNLAVARdRDH---- 1012
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAG------QDVATLDAD---ALAQLR-REHfgfi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1013 -----------APSDAELEAVLARVGL---LEHVRSLPG--GLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEP 1076
Cdd:PRK10535 92 fqryhllshltAAQNVEVPAVYAGLERkqrLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190
....*....|....*....|....*....|..
gi 1001866046 1077 TAHLDPESGLALVAALHgALADR--TVVMVTH 1106
Cdd:PRK10535 172 TGALDSHSGEEVMAILH-QLRDRghTVIIVTH 202
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
128-545 |
7.57e-17 |
|
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: 85.10 E-value: 7.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 128 LAGRGLDGLDALYTQYLPALVQTAVLPLLVGARILGA---DWVSALILVLTLPLVPVFMILIgrhTLEAVAEAQQSLLRL 204
Cdd:TIGR02868 112 LLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIavlSVPAALILAAGLLLAGFVAPLV---SLRAARAAEQALARL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 205 GSHL----VELAQGLPVLVGLGRAAEQRRALGELSRAYKGRTMATLRVAFLSALALELISTISVaVVAVFIGIRLVHGDM 280
Cdd:TIGR02868 189 RGELaaqlTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAV-LGALWAGGPAVADGR 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 281 TLEAGLLALILAP-ECFQPLRDLGTAhhasedgaeALRRTRARIGAPRGTVLLAAGhGRVQDAERPPAGQAAP--AGLRV 357
Cdd:TIGR02868 268 LAPVTLAVLVLLPlAAFEAFAALPAA---------AQQLTRVRAAAERIVEVLDAA-GPVAEGSAPAAGAVGLgkPTLEL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 358 AGLTVWYDGAAePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLV--RDGV----GASVRGSVDGPDPRRIAWVPQ 431
Cdd:TIGR02868 338 RDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLdpLQGEvtldGVPVSSLDQDEVRRRVSVCAQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 432 HPQFSERTVAAELALYAGAAGEGAV-----PGEPGALVRELLDQLGLGGLEAAdpAELSPGQQRRVAVARGLARVADgag 506
Cdd:TIGR02868 417 DAHLFDTTVRENLRLARPDATDEELwaaleRVGLADWLRALPDGLDTVLGEGG--ARLSGGERQRLALARALLADAP--- 491
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1001866046 507 LLLLDEPTAHLD-DASAALVERAIAALAGRvTVLLVSHEP 545
Cdd:TIGR02868 492 ILLLDEPTEHLDaETADELLEDLLAALSGR-TVVLITHHL 530
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
886-1121 |
1.04e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 86.18 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 886 LPALRSALVRVAAEEQAVRDA--AEERDDLQDAPGR--GPGITLRGVTVGW---TGGPdVLAGLDLAARPGDWIVVAGPS 958
Cdd:PLN03232 574 LPNLLSQVVNANVSLQRIEELllSEERILAQNPPLQpgAPAISIKNGYFSWdskTSKP-TLSDINLEIPVGSLVAIVGGT 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 959 GSGKSTLLALLTGFLAP-RVGSAAVAGPVAWCPQESHLFDSTVRGNLAVARDRDhapSDAELEAVlaRVGLLEHVRSLPG 1037
Cdd:PLN03232 653 GEGKTSLISAMLGELSHaETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFE---SERYWRAI--DVTALQHDLDLLP 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1038 GLD-ARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALV-AALHGALADRTVVMVTH--HATELMP 1113
Cdd:PLN03232 728 GRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELKGKTRVLVTNqlHFLPLMD 807
|
....*...
gi 1001866046 1114 GDTLVRLG 1121
Cdd:PLN03232 808 RIILVSEG 815
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
948-1106 |
1.10e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 84.79 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 948 PGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAaVAGP---VAWCPQESHLFDS-TVRGNL--AVARDRD---------- 1011
Cdd:PRK11819 32 PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA-RPAPgikVGYLPQEPQLDPEkTVRENVeeGVAEVKAaldrfneiya 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1012 -HAPSDAELEAVLARVGLLEHV--------------------RSLPGglDARIGSrgafLSGGQRQRLAVARTLLAGAEV 1070
Cdd:PRK11819 111 aYAEPDADFDALAAEQGELQEIidaadawdldsqleiamdalRCPPW--DAKVTK----LSGGERRRVALCRLLLEKPDM 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 1001866046 1071 VLLDEPTAHLDPESglalVAALHGALADR--TVVMVTH 1106
Cdd:PRK11819 185 LLLDEPTNHLDAES----VAWLEQFLHDYpgTVVAVTH 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
921-1081 |
1.27e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.06 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWTGGPD---VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAP-----RVGSAAVAGPVA---WC 989
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPssgeiTLDGVPVTGPGAdrgVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 PQESHLFD-STVRGNLAVA---RDRDHAPSDAELEAVLARVGLLEHVRslpggldARIGSrgafLSGGQRQRLAVARTLL 1065
Cdd:COG4525 82 FQKDALLPwLNVLDNVAFGlrlRGVPKAERRARAEELLALVGLADFAR-------RRIWQ----LSGGMRQRVGIARALA 150
|
170
....*....|....*.
gi 1001866046 1066 AGAEVVLLDEPTAHLD 1081
Cdd:COG4525 151 ADPRFLLMDEPFGALD 166
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
923-1084 |
1.30e-16 |
|
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: 80.81 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP----------------V 986
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkklrklrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 987 AWCPQESHLFD-STVRGNLAVARDRDH----------APSDAELE-AVLARVGLLEHVRSlpggldarigsRGAFLSGGQ 1054
Cdd:TIGR02315 82 GMIFQHYNLIErLTVLENVLHGRLGYKptwrsllgrfSEEDKERAlSALERVGLADKAYQ-----------RADQLSGGQ 150
|
170 180 190
....*....|....*....|....*....|
gi 1001866046 1055 RQRLAVARTLLAGAEVVLLDEPTAHLDPES 1084
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKT 180
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
936-1111 |
1.35e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 84.76 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 936 PDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLT-------------GFLAPRVGSAAVAGPVAWCPQESHLFDSTVRG 1002
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrhfdvsegdirfhDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1003 NLAVARDrDHAPSDAELEAVLARVGllEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:PRK10789 408 NIALGRP-DATQQEIEHVARLASVH--DDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180
....*....|....*....|....*....
gi 1001866046 1083 ESGLALVAALHGALADRTVVMVTHHATEL 1111
Cdd:PRK10789 485 RTEHQILHNLRQWGEGRTVIISAHRLSAL 513
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
355-553 |
1.61e-16 |
|
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: 79.79 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRdgvgaSVRGSV--DGPDPRR------- 425
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-----PRSGSIrfDGRDITGlpphera 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 ---IAWVPQHPQ-FSERTVAAELALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADpaeLSPGQQRRVAVARGLARV 501
Cdd:cd03224 74 ragIGYVPEGRRiFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGT---LSGGEQQMLAIARALMSR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 502 ADgagLLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHEPRTA-ALADR 553
Cdd:cd03224 151 PK---LLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFAlEIADR 201
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
948-1111 |
1.74e-16 |
|
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: 79.65 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 948 PGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-----------------VAWCPQESHLFDS-TVRGNLA-VAR 1008
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQYALFPHlNVRENLAfGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1009 DRDHAPSDAELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLAL 1088
Cdd:cd03297 102 RKRNREDRISVDELLDLLGLDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180
....*....|....*....|....*
gi 1001866046 1089 VAALHGALAD--RTVVMVTHHATEL 1111
Cdd:cd03297 171 LPELKQIKKNlnIPVIFVTHDLSEA 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
947-1107 |
2.23e-16 |
|
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: 80.14 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 947 RPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-VAWCPQE-SHLFDSTVRGNLAvARDRDHApSDAELEAVLA 1024
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtVSYKPQYiKADYEGTVRDLLS-SITKDFY-THPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1025 RvgllehvrslPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAAL-HGALADRTVVM 1103
Cdd:cd03237 101 K----------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIrRFAENNEKTAF 170
|
....
gi 1001866046 1104 VTHH 1107
Cdd:cd03237 171 VVEH 174
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
936-1124 |
2.32e-16 |
|
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: 78.99 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 936 PDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------PVAWCPQESHLFDSTVRG 1002
Cdd:cd03369 21 PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1003 NLavarDRDHAPSDAELEAVLarvgllehvrslpggldaRIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:cd03369 101 NL----DPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1001866046 1083 ESGLALVAALHGALADRTVVMVTHHATELMPGDTLVRLGARE 1124
Cdd:cd03369 159 ATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGE 200
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
914-1106 |
2.46e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.08 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 914 QDAPGRGPGITLRGVTVgWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLL-------ALLTGF-------------L 973
Cdd:COG1117 3 APASTLEPKIEVRNLNV-YYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGArvegeilldgediY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 974 APRVGSAAVAGPVAWCPQESHLFDSTVRGNLA----VARDRDHAPSDAELEAVLARVGLLEHVRslpggldARIGSRGAF 1049
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAyglrLHGIKSKSELDEIVEESLRKAALWDEVK-------DRLKKSALG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1050 LSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLA---LVAALHGalaDRTVVMVTH 1106
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKieeLILELKK---DYTIVIVTH 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
351-555 |
2.49e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.07 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 351 APAGLRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--DGvgaSVRgsVDG-------P 421
Cdd:COG3842 2 AMPALELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETpdSG---RIL--LDGrdvtglpP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 422 DPRRIAWVPQHPQ-FSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLAR 500
Cdd:COG3842 75 EKRNVGMVFQDYAlFPHLTVAENVAF--GLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 501 vadGAGLLLLDEPTAHLDdasAALVERAIAALAG-----RVTVLLVSHEPRTA-ALADRTV 555
Cdd:COG3842 153 ---EPRVLLLDEPLSALD---AKLREEMREELRRlqrelGITFIYVTHDQEEAlALADRIA 207
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
932-1106 |
2.71e-16 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 79.65 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 932 WTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLL-------ALLTGF-------------LAPRVGSAAVAGPVAWCPQ 991
Cdd:TIGR00972 10 FYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLrslnrmnDLVPGVriegkvlfdgqdiYDKKIDVVELRRRVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 992 ESHLFDSTVRGNLA----VARDRDHAPSDAELEAVLARVGLLEHVRSlpggldaRIGSRGAFLSGGQRQRLAVARTLLAG 1067
Cdd:TIGR00972 90 KPNPFPMSIYDNIAygprLHGIKDKKELDEIVEESLKKAALWDEVKD-------RLHDSALGLSGGQQQRLCIARALAVE 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 1068 AEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:TIGR00972 163 PEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTH 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
939-1120 |
2.84e-16 |
|
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: 79.43 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 939 LAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCP--------QESHLFD-STVRGNLAVARD 1009
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdrmvvfQNYSLLPwLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1010 R-DHAPSDAELEAV----LARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDpes 1084
Cdd:TIGR01184 81 RvLPDLSKSERRAIveehIALVGLTEAADKRPGQL-----------SGGMKQRVAIARALSIRPKVLLLDEPFGALD--- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1001866046 1085 glalvAALHGALADR----------TVVMVTHHATE-LMPGDTLVRL 1120
Cdd:TIGR01184 147 -----ALTRGNLQEElmqiweehrvTVLMVTHDVDEaLLLSDRVVML 188
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
943-1135 |
5.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.06 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 943 DLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVA--------------------GPVAWCPqESHLFDSTVRG 1002
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkknkklkplrkkvGIVFQFP-EHQLFEETVEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1003 -------NLAVARDrdhapsDAELEA--VLARVGLLEHVRSlpggldarigsRGAF-LSGGQRQRLAVARTLLAGAEVVL 1072
Cdd:PRK13634 106 dicfgpmNFGVSEE------DAKQKAreMIELVGLPEELLA-----------RSPFeLSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 1073 LDEPTAHLDP---ESGLALVAALHGAlADRTVVMVTH-------HATEL--MPGDTLVRLGARERVLHHAARAAA 1135
Cdd:PRK13634 169 LDEPTAGLDPkgrKEMMEMFYKLHKE-KGLTTVLVTHsmedaarYADQIvvMHKGTVFLQGTPREIFADPDELEA 242
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
938-1120 |
5.69e-16 |
|
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: 79.52 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESHLFDSTVRGNLAVARDRDhapsDA 1017
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYD----EY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1018 ELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD----PESGLALVAALh 1093
Cdd:cd03291 128 RYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfteKEIFESCVCKL- 206
|
170 180
....*....|....*....|....*..
gi 1001866046 1094 gaLADRTVVMVTHHATELMPGDTLVRL 1120
Cdd:cd03291 207 --MANKTRILVTSKMEHLKKADKILIL 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
922-1107 |
6.22e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.08 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 922 GITLRGVTVgwtggpDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESHLFDstvr 1001
Cdd:COG2401 35 GVELRVVER------YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLID---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 gnlAVARDRDhaPSDAelEAVLARVGLLEHVRSLpggldarigSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:COG2401 105 ---AIGRKGD--FKDA--VELLNAVGLSDAVLWL---------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*...
gi 1001866046 1082 PESGLALVAALHGAL--ADRTVVMVTHH 1107
Cdd:COG2401 169 RQTAKRVARNLQKLArrAGITLVVATHH 196
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
354-557 |
6.93e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.52 E-value: 6.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 354 GLRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDG-------PDPRRI 426
Cdd:COG4136 1 MLSLENLTITLGGR--PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGrrltalpAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 427 AWVPQHPQ-FSERTVAAELALyagaagegAVPGEPG-----ALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLAr 500
Cdd:COG4136 79 GILFQDDLlFPHLSVGENLAF--------ALPPTIGraqrrARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 501 vADGAgLLLLDEPTAHLDDASAA----LVERAIAALAgrVTVLLVSHEPRTAALADRTVEL 557
Cdd:COG4136 150 -AEPR-ALLLDEPFSKLDAALRAqfreFVFEQIRQRG--IPALLVTHDEEDAPAAGRVLDL 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
364-555 |
7.12e-16 |
|
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: 78.02 E-value: 7.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 364 YDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGP--DP----RRIAWVPQHPQFSE 437
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPadlrRNIGYVPQDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 438 RTVAAELALYAGAAGEGAVP-----GEPGALVRELLDQLGLGGLEAADpaELSPGQQRRVAVARGLARVADgagLLLLDE 512
Cdd:cd03245 92 GTLRDNITLGAPLADDERILraaelAGVTDFVNKHPNGLDLQIGERGR--GLSGGQRQAVALARALLNDPP---ILLLDE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1001866046 513 PTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALADRTV 555
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRII 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
938-1120 |
8.49e-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: 83.04 E-value: 8.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESHLFDSTVRGNLAVARDRDhapsDA 1017
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYD----EY 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1018 ELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALV-AALHGAL 1096
Cdd:TIGR01271 517 RYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFeSCLCKLM 596
|
170 180
....*....|....*....|....
gi 1001866046 1097 ADRTVVMVTHHATELMPGDTLVRL 1120
Cdd:TIGR01271 597 SNKTRILVTSKLEHLKKADKILLL 620
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-555 |
1.01e-15 |
|
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: 81.49 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 319 TRARIGAPRGtvLLAAGHGRVQDAERPPAGQAAPAGLRVAGLTVWYDGAAE---PAVGPLDFTAPAGRVTVLAGPSGSGK 395
Cdd:COG1123 227 PEEILAAPQA--LAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 396 TTVLAALAGLVR--------DGVG-ASVRGSVDGPDPRRIAWVPQHP--QFSER-TVAAELALYAGAAGEGAvPGEPGAL 463
Cdd:COG1123 305 STLARLLLGLLRptsgsilfDGKDlTKLSRRSLRELRRRVQMVFQDPysSLNPRmTVGDIIAEPLRLHGLLS-RAERRER 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 464 VRElLDQLGLGGLEAAD--PAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGR--VTVL 539
Cdd:COG1123 384 VAE-LLERVGLPPDLADryPHELSGGQRQRVAIARALALEPK---LLILDEPTSALDVSVQAQILNLLRDLQRElgLTYL 459
|
250
....*....|....*..
gi 1001866046 540 LVSHEPRTAA-LADRTV 555
Cdd:COG1123 460 FISHDLAVVRyIADRVA 476
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
375-555 |
1.47e-15 |
|
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: 76.95 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGrVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDG-------------PDPRRIAWVPQHPQ-FSERTV 440
Cdd:cd03297 17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGG---TIVLNGtvlfdsrkkinlpPQQRKIGLVFQQYAlFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 441 AAELALyagaAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDA 520
Cdd:cd03297 93 RENLAF----GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPE---LLLLDEPFSALDRA 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1001866046 521 SAALVERAIAALAGR--VTVLLVSHEPRTA-ALADRTV 555
Cdd:cd03297 166 LRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIV 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
939-1106 |
1.55e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.62 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 939 LAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAP-----RVGSAAVA---------------GPVAWCPqESHLFDS 998
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPtegkvTVGDIVVSstskqkeikpvrkkvGVVFQFP-ESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 TVRGNLAVArDRDHAPSDAELEAVLARVglLEHVrslpgGLDARIGSRGAF-LSGGQRQRLAVARTLLAGAEVVLLDEPT 1077
Cdd:PRK13643 101 TVLKDVAFG-PQNFGIPKEKAEKIAAEK--LEMV-----GLADEFWEKSPFeLSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190
....*....|....*....|....*....|..
gi 1001866046 1078 AHLDPESG---LALVAALHGalADRTVVMVTH 1106
Cdd:PRK13643 173 AGLDPKARiemMQLFESIHQ--SGQTVVLVTH 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
901-1110 |
1.68e-15 |
|
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: 82.37 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 901 QAVRDAAEERDdlqdAPGRGPGITLRG-VTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS 979
Cdd:TIGR01257 911 EGINDSFFERE----LPGLVPGVCVKNlVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGT 986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 980 AAVAG------------PVAWCPQESHLFDS-TVRGNL---AVARDRDHAPSDAELEAVLARVGLlEHVRSlpggldari 1043
Cdd:TIGR01257 987 VLVGGkdietnldavrqSLGMCPQHNILFHHlTVAEHIlfyAQLKGRSWEEAQLEMEAMLEDTGL-HHKRN--------- 1056
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 1044 gSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHATE 1110
Cdd:TIGR01257 1057 -EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE 1122
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
355-557 |
1.70e-15 |
|
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: 77.22 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYdGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--------DGVGASVRGSVDGPDPRR- 425
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEptsgsvliDGTDINKLKGKALRQLRRq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 IAWVPQHPQFSERTVAAELALyAGAAGE--------GAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARG 497
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVL-SGRLGRrstwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 498 LARVADgagLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTA-ALADRTVEL 557
Cdd:cd03256 159 LMQQPK---LILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLArEYADRIVGL 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
889-1129 |
1.94e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 81.95 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 889 LRSALVRVAAEEQAVRDAAEERDDLQDAPGRGPGITLRGVTV-GWTGG----------------PDVLAGLDLAARPGDW 951
Cdd:PLN03232 1185 LLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVsGWPSRgsikfedvhlryrpglPPVLHGLSFFVSPSEK 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 952 IVVAGPSGSGKSTLL-------------ALLTGFLAPRVGSAAVAGPVAWCPQESHLFDSTVRGNLavarDRDHAPSDAE 1018
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLnalfrivelekgrIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI----DPFSEHNDAD 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1019 LEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALAD 1098
Cdd:PLN03232 1341 LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS 1420
|
250 260 270
....*....|....*....|....*....|.
gi 1001866046 1099 RTVVMVTHHATELMPGDTLVRLGARErVLHH 1129
Cdd:PLN03232 1421 CTMLVIAHRLNTIIDCDKILVLSSGQ-VLEY 1450
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
934-1106 |
1.99e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 81.75 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------PVAWCPQESHLFDSTV 1000
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreigayglrelrrQFSMIPQDPVLFDGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 RGNLavarDRDHAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLA-GAEVVLLDEPTAH 1079
Cdd:PTZ00243 1401 RQNV----DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATAN 1476
|
170 180
....*....|....*....|....*..
gi 1001866046 1080 LDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:PTZ00243 1477 IDPALDRQIQATVMSAFSAYTVITIAH 1503
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
375-555 |
2.13e-15 |
|
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: 76.41 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--------DGVgasvrgSVDGPDP------RRIAWVPQHPQ-FSERT 439
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiiiDGL------KLTDDKKninelrQKVGMVFQQFNlFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 440 VAAELALyagaaGEGAVPGEPGALVRELLDQLGLGG--LEAAD--PAELSPGQQRRVAVARGLARVADgagLLLLDEPTA 515
Cdd:cd03262 93 VLENITL-----APIKVKGMSKAEAEERALELLEKVglADKADayPAQLSGGQQQRVAIARALAMNPK---VMLFDEPTS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1001866046 516 HLDDASAALVERAIAALAGR-VTVLLVSHEPRTA-ALADRTV 555
Cdd:cd03262 165 ALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFArEVADRVI 206
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
939-1106 |
2.47e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.12 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 939 LAGLDLAARPGDWIVVAGPSGSGKSTLLALLT--GFLAPRV---GSAAVAGPVAWCP---------------QESHLFDS 998
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVtitGSIVYNGHNIYSPrtdtvdlrkeigmvfQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 TVRGN----LAVARDRDHAPSDAELEAVLARVGLLEHVRSlpggldaRIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLD 1074
Cdd:PRK14239 101 SIYENvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|..
gi 1001866046 1075 EPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
923-1112 |
2.86e-15 |
|
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: 76.14 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVA--WCPQESHL---FD 997
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdLPPKDRDIamvFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 998 S-------TVRGNLAVARDRDHAPSDAELEAVLARVGLLehvrslpgGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEV 1070
Cdd:cd03301 80 NyalyphmTVYDNIAFGLKLRKVPKDEIDERVREVAELL--------QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1001866046 1071 VLLDEPTAHLDPESGLAL---VAALHGALaDRTVVMVTHHATELM 1112
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMraeLKRLQQRL-GTTTIYVTHDQVEAM 195
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
905-1102 |
2.97e-15 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 80.77 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 905 DAAEERDDLQDAPGRGPG-ITLRGVTVGWT-GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS--- 979
Cdd:TIGR03797 433 EALPEVDEAKTDPGKLSGaIEVDRVTFRYRpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSvfy 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 980 ----------AAVAGPVAWCPQESHLFDSTVRGNLAVardrdHAP-SDAELEAVLARVGLLEHVRSLPGGLDARIGSRGA 1048
Cdd:TIGR03797 513 dgqdlagldvQAVRRQLGVVLQNGRLMSGSIFENIAG-----GAPlTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGG 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 1049 FLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVV 1102
Cdd:TIGR03797 588 TLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTRIVI 641
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
922-1106 |
3.90e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 78.26 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 922 GITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG------------PVAWC 989
Cdd:COG1118 2 SIEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnlpprerRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 PQESHLF-DSTVRGNLAVA-RDRdhAPSDAELEAV----LARVGLlehvrslpGGLDARigsRGAFLSGGQRQRLAVART 1063
Cdd:COG1118 81 FQHYALFpHMTVAENIAFGlRVR--PPSKAEIRARveelLELVQL--------EGLADR---YPSQLSGGQRQRVALARA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1064 LLAGAEVVLLDEPTAHLDpesglALVAA--------LHGALaDRTVVMVTH 1106
Cdd:COG1118 148 LAVEPEVLLLDEPFGALD-----AKVRKelrrwlrrLHDEL-GGTTVFVTH 192
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
934-1106 |
4.47e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.55 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGpvawcpQESHLFDSTvRGNLAVARDRDHA 1013
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG------QTINLVRDK-DGQLKVADKNQLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1014 PSDAELEAVLARVGLLEHVRSLPGGLDA---------------------RIG----SRGAF---LSGGQRQRLAVARTLL 1065
Cdd:PRK10619 89 LLRTRLTMVFQHFNLWSHMTVLENVMEApiqvlglskqeareravkylaKVGiderAQGKYpvhLSGGQQQRVSIARALA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1001866046 1066 AGAEVVLLDEPTAHLDPE-SGLALVAALHGALADRTVVMVTH 1106
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPElVGEVLRIMQQLAEEGKTMVVVTH 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
922-1106 |
5.33e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.71 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 922 GITLRGVTVGWTGGPD----VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVA-------------- 983
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstsknkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 984 ------GPVAWCPqESHLFDSTVRGNLAVArDRDHAPSDAELEAV----LARVGLLEHVRSlpggldarigsRGAF-LSG 1052
Cdd:PRK13649 82 qirkkvGLVFQFP-ESQLFEETVLKDVAFG-PQNFGVSQEEAEALarekLALVGISESLFE-----------KNPFeLSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 1053 GQRQRLAVARTLLAGAEVVLLDEPTAHLDPESG---LALVAALHgaLADRTVVMVTH 1106
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRkelMTLFKKLH--QSGMTIVLVTH 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
956-1112 |
6.84e-15 |
|
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: 77.45 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 956 GPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------------PVAWCPQESHLFDS-TVRGNLAVARDR-DHAPSD 1016
Cdd:COG4148 32 GPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFPHlSVRGNLLYGRKRaPRAERR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1017 AELEAVLARVGLlEHVrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALhGAL 1096
Cdd:COG4148 112 ISFDEVVELLGI-GHL------LDRRPAT----LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYL-ERL 179
|
170
....*....|....*....
gi 1001866046 1097 ADRT---VVMVTHHATELM 1112
Cdd:COG4148 180 RDELdipILYVSHSLDEVA 198
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
355-555 |
7.46e-15 |
|
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: 75.34 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAAL-------AGLVR-DGVgaSVRGsVDGPDPRR- 425
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRILiDGH--DVRD-YTLASLRRq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 IAWVPQHPQFSERTVAAELALyagaagegAVPGEPGALVRElldqlglgGLEAADPAE-------------------LSP 486
Cdd:cd03251 78 IGLVSQDVFLFNDTVAENIAY--------GRPGATREEVEE--------AARAANAHEfimelpegydtvigergvkLSG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 487 GQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALADRTV 555
Cdd:cd03251 142 GQRQRIAIARALLKDPP---ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIV 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
923-1106 |
7.70e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 77.04 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVT-VGWTGGPDVLA--GLDLAARPGDwIV-VAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------- 984
Cdd:COG1135 2 IELENLSkTFPTKGGPVTAldDVSLTIEKGE-IFgIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalserelraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 985 --PVAWCPQESHLFDS-TVRGNLA-------VARdrdhapsdaelEAVLARVG-LLEHVrslpgGLDARIGSRGAFLSGG 1053
Cdd:COG1135 81 rrKIGMIFQHFNLLSSrTVAENVAlpleiagVPK-----------AEIRKRVAeLLELV-----GLSDKADAYPSQLSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 1054 QRQRLAVARTLLAGAEVVLLDEPTAHLDPE---SGLALVAALHGALaDRTVVMVTH 1106
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPEttrSILDLLKDINREL-GLTIVLITH 199
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
941-1114 |
9.03e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.07 E-value: 9.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 941 GLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRvgsaavAGPVAWCPQESHLFDSTVRGNL-------AVARD---- 1009
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPD------AGEVLWQGEPIRRQRDEYHQDLlylghqpGIKTEltal 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1010 -------RDHAPSDAE-LEAVLARVGLLehvrslpGGLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:PRK13538 93 enlrfyqRLHGPGDDEaLWEALAQVGLA-------GFEDVPVRQ----LSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1001866046 1082 PEsGLALVAALHGALADR--TVVMVTHHATELMPG 1114
Cdd:PRK13538 162 KQ-GVARLEALLAQHAEQggMVILTTHQDLPVASD 195
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
924-1077 |
1.15e-14 |
|
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: 74.48 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 924 TLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP--------------VAWC 989
Cdd:TIGR03410 2 EVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEditklppheraragIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 PQESHLFDS-TVRGNLAV---ARDRDHAPSDAEleaVLARVGLLEHVRSLPGGLdarigsrgafLSGGQRQRLAVARTLL 1065
Cdd:TIGR03410 81 PQGREIFPRlTVEENLLTglaALPRRSRKIPDE---IYELFPVLKEMLGRRGGD----------LSGGQQQQLAIARALV 147
|
170
....*....|..
gi 1001866046 1066 AGAEVVLLDEPT 1077
Cdd:TIGR03410 148 TRPKLLLLDEPT 159
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
956-1106 |
1.15e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.59 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 956 GPSGSGKSTLLA-------LLTGF-------------LAPRVGSAAVAGPVAWCPQESHLFDSTVRGNLAV-ARDRDHAP 1014
Cdd:PRK14243 43 GPSGCGKSTILRcfnrlndLIPGFrvegkvtfhgknlYAPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYgARINGYKG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1015 SDAEL-EAVLARVGLLEHVRSlpggldaRIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALH 1093
Cdd:PRK14243 123 DMDELvERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMH 195
|
170
....*....|...
gi 1001866046 1094 GALADRTVVMVTH 1106
Cdd:PRK14243 196 ELKEQYTIIIVTH 208
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
923-1118 |
1.29e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.41 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQ----------- 991
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSklqgirklvgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 992 -----ESHLFDSTVRGNLAVARDRDHAPS---DAELEAVLARVGLLEHVRSLPGGldarigsrgafLSGGQRQRLAVART 1063
Cdd:PRK13644 82 vfqnpETQFVGRTVEEDLAFGPENLCLPPieiRKRVDRALAEIGLEKYRHRSPKT-----------LSGGQGQCVALAGI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 1064 LLAGAEVVLLDEPTAHLDPESGLAL---VAALHGalADRTVVMVTHHATELMPGDTLV 1118
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVlerIKKLHE--KGKTIVYITHNLEELHDADRII 206
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
939-1110 |
1.33e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.05 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 939 LAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAprvGSAAVagpvawcpqESH--LFDSTVRGNLAVARD----RDH 1012
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDKSA---------GSHieLLGRTVQREGRLARDirksRAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1013 APSDAELEAVLARVGLLEHVrsLPGGLDA------------------------RIG------SRGAFLSGGQRQRLAVAR 1062
Cdd:PRK09984 88 TGYIFQQFNLVNRLSVLENV--LIGALGStpfwrtcfswftreqkqralqaltRVGmvhfahQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 1063 TLLAGAEVVLLDEPTAHLDPESGLALVAALHGA-LADRTVVMVTHHATE 1110
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVD 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
917-1110 |
1.56e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.61 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 917 PGRGPGITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP----------- 985
Cdd:PRK13537 2 PMSVAPIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 986 -VAWCPQESHLF-DSTVRGNLAVArDRDHAPSDAELEAVLArvGLLEHVRsLPGGLDARIGSrgafLSGGQRQRLAVART 1063
Cdd:PRK13537 81 rVGVVPQFDNLDpDFTVRENLLVF-GRYFGLSAAAARALVP--PLLEFAK-LENKADAKVGE----LSGGMKRRLTLARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1001866046 1064 LLAGAEVVLLDEPTAHLDPESGLALVAALHGALAD-RTVVMVTHHATE 1110
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEE 200
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
375-553 |
1.76e-14 |
|
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: 74.25 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--DGvgaSVRgsVDGPD------------PRRIAWVPQ--------- 431
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpdSG---EIL--VDGQDitglsekelyelRRRIGMLFQggalfdslt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 432 -----------HPQFSERTVA--AELALyagaagegavpgepgALVRelldqlglgGLEAAD--PAELSPGQQRRVAVAR 496
Cdd:COG1127 99 vfenvafplreHTDLSEAEIRelVLEKL---------------ELVG---------LPGAADkmPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 497 GLArvADGAgLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTA-ALADR 553
Cdd:COG1127 155 ALA--LDPE-ILLYDEPTAGLDPITSAVIDELIRELRDElgLTSVVVTHDLDSAfAIADR 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
923-1112 |
1.77e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 72.08 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVgWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGpvawcpqESHLFDStvrg 1002
Cdd:cd03216 1 LELRGITK-RFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-------KEVSFAS---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1003 nlavardrdhaPSDAeleavlarvgllehvrslpggLDARIGSrgAF-LSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:cd03216 69 -----------PRDA---------------------RRAGIAM--VYqLSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 1082 P---ESGLALVAALHGalADRTVVMVTHHATELM 1112
Cdd:cd03216 115 PaevERLFKVIRRLRA--QGVAVIFISHRLDEVF 146
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
355-553 |
1.97e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 72.08 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRGS-VDGPDPRRiawvpqh 432
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEiLVDGKeVSFASPRD------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 433 pqfsertvaaelalyAGAAGEGAVPgepgalvrelldqlglggleaadpaELSPGQQRRVAVARGLARvadGAGLLLLDE 512
Cdd:cd03216 72 ---------------ARRAGIAMVY-------------------------QLSVGERQMVEIARALAR---NARLLILDE 108
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1001866046 513 PTAHLDDASAALVERAIAALAGR-VTVLLVSHEPRTA-ALADR 553
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVfEIADR 151
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
376-555 |
2.14e-14 |
|
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: 75.91 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 376 DFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDG-------------PDPRRIAWVPQHPQ-FSERTVA 441
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSG---RIRLGGevlqdsargiflpPHRRRIGYVFQEARlFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 442 AELaLYagaagegavpgepgALVRELLDQLGLGGLEAAD-----------PAELSPGQQRRVAVARGLARVADgagLLLL 510
Cdd:COG4148 96 GNL-LY--------------GRKRAPRAERRISFDEVVEllgighlldrrPATLSGGERQRVAIGRALLSSPR---LLLM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 511 DEPTAHLDDASAA----LVERAIAALagRVTVLLVSHEPRTAA-LADRTV 555
Cdd:COG4148 158 DEPLAALDLARKAeilpYLERLRDEL--DIPILYVSHSLDEVArLADHVV 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
923-1110 |
2.29e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVawcPQESHL------ 995
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvPV---PARARLararig 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 996 ----FDS-----TVRGNLAVArDRDHAPSDAELEAVLArvGLLEHVRslpggLDARIGSRGAFLSGGQRQRLAVARTLLA 1066
Cdd:PRK13536 118 vvpqFDNldlefTVRENLLVF-GRYFGMSTREIEAVIP--SLLEFAR-----LESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1001866046 1067 GAEVVLLDEPTAHLDPESGLALVAALHGALA-DRTVVMVTHHATE 1110
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEE 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
371-553 |
2.91e-14 |
|
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: 73.17 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 371 AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDGPD--------PRRIAWVPQhpqfsERTVAA 442
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG---RATVAGHDvvreprevRRRIGIVFQ-----DLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 443 ELALYAGAAGEGAVPGEPGALVRELLDQLGLGG--LEAADP--AELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLD 518
Cdd:cd03265 87 ELTGWENLYIHARLYGVPGAERRERIDELLDFVglLEAADRlvKTYSGGMRRRLEIARSLVHRPE---VLFLDEPTIGLD 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1001866046 519 DASAALVERAIAALAGR--VTVLLVSHEPRTA-ALADR 553
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEfgMTILLTTHYMEEAeQLCDR 201
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
354-555 |
3.00e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 75.57 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 354 GLRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR-DgvgasvRGSV--DGPD-------- 422
Cdd:COG1118 2 SIEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpD------SGRIvlNGRDlftnlppr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 423 PRRIAWVPQHPQ-FSERTVAAELAlyAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARv 501
Cdd:COG1118 74 ERRVGFVFQHYAlFPHMTVAENIA--FGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 502 adGAGLLLLDEPTAHLDDASAALVERAIAAL--AGRVTVLLVSHEPRTA-ALADRTV 555
Cdd:COG1118 151 --EPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHDQEEAlELADRVV 205
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
50-318 |
3.08e-14 |
|
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: 74.50 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 50 PGVLSAATLVAAAGVLLRAAAEWGTSTVGRWAAVGVKEELRSQLLEAALEGgaapasaagpvddGAARVASSPAATAV-L 128
Cdd:cd18781 33 TASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRL-------------GPSYQEKVSTAEVVqL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 129 AGRGLDGLDALYTQYLPALVQTAVLPLLVGARILGADWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHL 208
Cdd:cd18781 100 SVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKIAKKLLSKYWGSYTDLGDSF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 209 VELAQGLPVLVGLGRAAEQRRALGELSRAYKGRTMATLRVAFLSALALELISTISVAVVAVFIGIRLVHGDMTLEAGLLA 288
Cdd:cd18781 180 LENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVAYGGAALGIILALLQFANGSISLAGALFI 259
|
250 260 270
....*....|....*....|....*....|
gi 1001866046 289 LILAPECFQPLRDLGTAHHASEDGAEALRR 318
Cdd:cd18781 260 ILLSAEFFLPLRLLGSFFHIAMNGMAASDK 289
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
939-1103 |
3.30e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 74.28 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 939 LAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAwcpQESHLFD------------------STV 1000
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETVWDvrrqvgmvfqnpdnqfvgATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 RGNLAVARDRDHAPSDAELEAV---LARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAEVVLLDEPT 1077
Cdd:PRK13635 100 QDDVAFGLENIGVPREEMVERVdqaLRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1001866046 1078 AHLDP---------------ESGLALVAALH----GALADRTVVM 1103
Cdd:PRK13635 169 SMLDPrgrrevletvrqlkeQKGITVLSITHdldeAAQADRVIVM 213
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
938-1118 |
3.99e-14 |
|
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: 73.79 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTL-LA------------LLTGFLAPRVGSAAVAGPVAWCPQESHLFDSTVRGNL 1004
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLsLAffrmvdifdgkiVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1005 avarDRDHAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPES 1084
Cdd:cd03288 116 ----DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 1085 GLALVAALHGALADRTVVMVTHHATELMPGDTLV 1118
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVL 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
323-553 |
4.41e-14 |
|
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: 76.71 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 323 IGAPRGTVLLAAGHGRVQD--AERPPAGQA----APAG-LRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGK 395
Cdd:COG4618 292 IGGWKQFVSARQAYRRLNEllAAVPAEPERmplpRPKGrLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 396 TTVLAALAGLVRDGVGaSVRgsVDGPDPRR---------IAWVPQHPQFSERTVAAELALYAGAAGEGAVpgepgalvre 466
Cdd:COG4618 372 STLARLLVGVWPPTAG-SVR--LDGADLSQwdreelgrhIGYLPQDVELFDGTIAENIARFGDADPEKVV---------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 467 lldqlglgglEAA----------------------DPAELSPGQQRRVAVARGLARvaDGAgLLLLDEPTAHLDDASAAL 524
Cdd:COG4618 439 ----------AAAklagvhemilrlpdgydtrigeGGARLSGGQRQRIGLARALYG--DPR-LVVLDEPNSNLDDEGEAA 505
|
250 260 270
....*....|....*....|....*....|
gi 1001866046 525 VERAIAAL-AGRVTVLLVSHEPRTAALADR 553
Cdd:COG4618 506 LAAAIRALkARGATVVVITHRPSLLAAVDK 535
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
939-1112 |
5.09e-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: 72.76 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 939 LAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-----------VAWCPQESHLFDS-TVRGNLAV 1006
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYALFRHmTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1007 ---ARDRDHAPSDAELEAvlaRV-GLLEHVRslpggLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:cd03296 98 glrVKPRSERPPEAEIRA---KVhELLKLVQ-----LDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190
....*....|....*....|....*....|...
gi 1001866046 1083 ESGLALVAALHgALADR---TVVMVTHHATELM 1112
Cdd:cd03296 170 KVRKELRRWLR-RLHDElhvTTVFVTHDQEEAL 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
946-1083 |
5.45e-14 |
|
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: 76.36 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 946 ARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQE-SHLFDSTVRGNLavardRDHAPSDAE---LEA 1021
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYiSPDYDGTVEEFL-----RSANTDDFGssyYKT 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 1022 VLARVGLLEHVrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPE 1083
Cdd:COG1245 438 EIIKPLGLEKL------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
376-555 |
5.65e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.48 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 376 DFTAPAGRVTVLAGPSGSGKTTVLAALAGLVrdgvgASVRGSV--DG-------PDPRRIAWVPQ-HPQFSERTVAAELA 445
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFL-----PPDSGRIlwNGqdltalpPAERPVSMLFQeNNLFPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 446 LyagaageGAVPG-----EPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDA 520
Cdd:COG3840 94 L-------GLRPGlkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR---KRPILLLDEPFSALDPA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1001866046 521 ----SAALVeRAIAALAGRvTVLLVSHEPRTAA-LADRTV 555
Cdd:COG3840 164 lrqeMLDLV-DELCRERGL-TVLMVTHDPEDAArIADRVL 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
934-1107 |
5.94e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 71.76 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPrvgsaaVAGPVAWCPQESHLFDSTVRGNLAVArdrDHA 1013
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP------LAGRVLLNGGPLDFQRDSIARGLLYL---GHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1014 P-------------------SDAELEAVLARVGLlehvrslpGGLDARIgsrGAFLSGGQRQRLAVARTLLAGAEVVLLD 1074
Cdd:cd03231 82 PgikttlsvlenlrfwhadhSDEQVEEALARVGL--------NGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 1001866046 1075 EPTAHLDPESglalVAALHGALADRT-----VVMVTHH 1107
Cdd:cd03231 151 EPTTALDKAG----VARFAEAMAGHCarggmVVLTTHQ 184
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
921-1112 |
6.03e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.87 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWTGGPDVlAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------PVAWC 989
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlshvppyqrPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 PQESHLFDS-TVRGNLAVARDRDHAPSD---AELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLL 1065
Cdd:PRK11607 97 FQSYALFPHmTVEQNIAFGLKQDKLPKAeiaSRVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1066 AGAEVVLLDEPTAHLDPE----SGLALVAALHGALAdrTVVMVTHHATELM 1112
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKlrdrMQLEVVDILERVGV--TCVMVTHDQEEAM 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
943-1123 |
6.95e-14 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 73.06 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 943 DLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCPQE----------SHLFDS-------TVRGNL 1004
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqDIAAMSRKelrelrrkkiSMVFQSfallphrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1005 AVARDRDHAPSDAELEA---VLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:cd03294 124 AFGLEVQGVPRAEREERaaeALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 1082 P-------ESGLALVAALHgaladRTVVMVTHHATELMpgdtlvRLGAR 1123
Cdd:cd03294 193 PlirremqDELLRLQAELQ-----KTIVFITHDLDEAL------RLGDR 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
945-1112 |
8.19e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 8.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 945 AARPGDWIVVAGPSGSGKSTLLALLTGFLAPRV---GSAAVAG-PV-AWC-------PQESHLF--DSTVRGNL---AVA 1007
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGmPIdAKEmraisayVQQDDLFipTLTVREHLmfqAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1008 RDRDHAPSD---AELEAVLARVGLLEhvrslpgGLDARIGSRGAF--LSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:TIGR00955 127 RMPRRVTKKekrERVDEVLQALGLRK-------CANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190
....*....|....*....|....*....|...
gi 1001866046 1083 ESGLALVAALHGaLAD--RTVVMVTHHAT-ELM 1112
Cdd:TIGR00955 200 FMAYSVVQVLKG-LAQkgKTIICTIHQPSsELF 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
375-546 |
8.90e-14 |
|
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: 71.92 E-value: 8.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDG----PD--PRRIAWVPQHPQF-SERTVAAELALY 447
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGqprkPDqfQKCVAYVRQDDILlPGLTVRETLTYT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 448 AGAAGEGAVPGEPGALVRELLDQLGLGGLEAADP--AELSPGQQRRVAVARGLARVadgAGLLLLDEPTAHLDDASAALV 525
Cdd:cd03234 106 AILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNlvKGISGGERRRVSIAVQLLWD---PKVLILDEPTSGLDSFTALNL 182
|
170 180
....*....|....*....|..
gi 1001866046 526 ERAIAALAGR-VTVLLVSHEPR 546
Cdd:cd03234 183 VSTLSQLARRnRIVILTIHQPR 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
923-1081 |
9.46e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.83 E-value: 9.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG----------------PV 986
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflrrQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 987 AWCPQESHLF-DSTVRGNLAVARDRDHAPSD---AELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVAR 1062
Cdd:PRK10908 82 GMIFQDHHLLmDRTVYDNVAIPLIIAGASGDdirRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
|
170
....*....|....*....
gi 1001866046 1063 TLLAGAEVVLLDEPTAHLD 1081
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLD 169
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
936-1081 |
9.79e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.32 E-value: 9.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 936 PDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------PVAWCPQESHLFDSTVRG 1002
Cdd:PLN03130 1252 PPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVRF 1331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 1003 NLavarDRDHAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:PLN03130 1332 NL----DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
949-1120 |
1.10e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.48 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 949 GDWIVVAGPSGSGKSTLLALLTGFLAPRVG-----SAAVA-----------GPVAWCPqESHLFDSTVRGNLAVARDRDH 1012
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynNQAITddnfeklrkhiGIVFQNP-DNQFVGSIVKYDVAFGLENHA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1013 APSD---AELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALV 1089
Cdd:PRK13648 114 VPYDemhRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190
....*....|....*....|....*....|...
gi 1001866046 1090 AALHGALADR--TVVMVTHHATELMPGDTLVRL 1120
Cdd:PRK13648 183 DLVRKVKSEHniTIISITHDLSEAMEADHVIVM 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
919-1081 |
1.25e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.83 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 919 RGPGITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-VAWCPQESH--- 994
Cdd:PRK09452 11 LSPLVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdITHVPAENRhvn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 995 -LFDS-------TVRGNLAVARDRDHAPSdAELEavlARV-GLLEHVRslpggLDARIGSRGAFLSGGQRQRLAVARTLL 1065
Cdd:PRK09452 90 tVFQSyalfphmTVFENVAFGLRMQKTPA-AEIT---PRVmEALRMVQ-----LEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170
....*....|....*.
gi 1001866046 1066 AGAEVVLLDEPTAHLD 1081
Cdd:PRK09452 161 NKPKVLLLDESLSALD 176
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
366-555 |
1.30e-13 |
|
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: 71.95 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 366 GAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRG-SVDGPDP----RRIAWVPQHPQ-FSER 438
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEiFIDGeDIREQDPvelrRKIGYVIQQIGlFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 439 TVAAELALyagaagegaVP---GEPGA----LVRELLDQLGLGGLEAAD--PAELSPGQQRRVAVARGLArvADgAGLLL 509
Cdd:cd03295 91 TVEENIAL---------VPkllKWPKEkireRADELLALVGLDPAEFADryPHELSGGQQQRVGVARALA--AD-PPLLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 510 LDEPTAHLDDASAALVERAIAALAGRV--TVLLVSHEPRTA-ALADRTV 555
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAfRLADRIA 207
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
934-1111 |
1.91e-13 |
|
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: 70.32 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESH-----LFDS-------TVR 1001
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALrrigaLIEApgfypnlTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 GNLAVArDRDHAPSDAELEAVLARVGLLEHVrslpgglDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:cd03268 91 ENLRLL-ARLLGIRKKRIDEVLDVVGLKDSA-------KKKVKG----FSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190
....*....|....*....|....*....|..
gi 1001866046 1082 PEsGLALVAALHGALAD--RTVVMVTHHATEL 1111
Cdd:cd03268 159 PD-GIKELRELILSLRDqgITVLISSHLLSEI 189
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
930-1106 |
2.03e-13 |
|
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: 70.76 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 930 VGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGflapRVGSAAVAGPVAW---CPQESHLFDS-------- 998
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG----RVEGGGTTSGQILfngQPRKPDQFQKcvayvrqd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 -------TVRGNLA-VARDRDHAPSDAELEAVLARVGLLEHVRslpgglDARIGS---RGafLSGGQRQRLAVARTLLAG 1067
Cdd:cd03234 90 dillpglTVRETLTyTAILRLPRKSSDAIRKKRVEDVLLRDLA------LTRIGGnlvKG--ISGGERRRVSIAVQLLWD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1001866046 1068 AEVVLLDEPTAHLDPESGLALVAAL-HGALADRTVVMVTH 1106
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLsQLARRNRIVILTIH 201
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
375-557 |
2.19e-13 |
|
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: 70.96 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVrgsVDG-PDP--------RRIAWVPQHPQFSERTVAAELA 445
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVL---LDGkPISqyehkylhSKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 446 LYAGAAG-----EGAVPGEPGALVRELLDQLGLGGLEAAdpAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDA 520
Cdd:cd03248 110 YGLQSCSfecvkEAAQKAHAHSFISELASGYDTEVGEKG--SQLSGGQKQRVAIARALIR---NPQVLILDEATSALDAE 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 1001866046 521 SAALVERAIAALAGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:cd03248 185 SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVL 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
938-1111 |
2.46e-13 |
|
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: 70.65 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG------PV--------AWCPQESHLF-DSTVRG 1002
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklPMhkrarlgiGYLPQEASIFrKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1003 NLAVA---RDRDHAPSDAELEAVLARVGLlEHVRSlpggldarigSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAH 1079
Cdd:cd03218 95 NILAVleiRGLSKKEREEKLEELLEEFHI-THLRK----------SKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 1080 LDPESgLALVAALHGALADRTV-VMVT-HHATEL 1111
Cdd:cd03218 164 VDPIA-VQDIQKIIKILKDRGIgVLITdHNVRET 196
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
355-557 |
2.68e-13 |
|
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: 69.10 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVwYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGvgasvRGSVDGPDPRRIAWVPQHPQ 434
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-----SGRIGMPEGEDLLFLPQRPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 435 FSERTVAAELALyagaagegavpgepgalvrelldqlglggleaadP--AELSPGQQRRVAVARGLARVADgagLLLLDE 512
Cdd:cd03223 75 LPLGTLREQLIY----------------------------------PwdDVLSGGEQQRLAFARLLLHKPK---FVFLDE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1001866046 513 PTAHLDDASAALVERAIAALagRVTVLLVSHEPRTAALADRTVEL 557
Cdd:cd03223 118 ATSALDEESEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLDL 160
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
365-557 |
3.19e-13 |
|
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: 70.16 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 365 DGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAG---------LVRDGVGAsvrgsVD--GPDPRR-------- 425
Cdd:COG4778 20 GGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsiLVRHDGGW-----VDlaQASPREilalrrrt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 IAWVPQH----PQFSERTVAAELALYAGAAGEGAvpgepgalvrelldqlglgGLEAAD---------------PAELSP 486
Cdd:COG4778 95 IGYVSQFlrviPRVSALDVVAEPLLERGVDREEA-------------------RARAREllarlnlperlwdlpPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 487 GQQRRVAVARGLARVADgagLLLLDEPTAHLDDAS-AALVERAIAALAGRVTVLLVSHEPRT-AALADRTVEL 557
Cdd:COG4778 156 GEQQRVNIARGFIADPP---LLLLDEPTASLDAANrAVVVELIEEAKARGTAIIGIFHDEEVrEAVADRVVDV 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
934-1110 |
3.51e-13 |
|
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: 70.09 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG------------PVAWCPQESHLFDS-TV 1000
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 RGNLAVaRDRDHAPSDAEL----EAVLARVGLLEHVrslpgglDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEP 1076
Cdd:cd03265 91 WENLYI-HARLYGVPGAERreriDELLDFVGLLEAA-------DRLVKT----YSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1001866046 1077 TAHLDPESGLAL---VAALHGALaDRTVVMVTHHATE 1110
Cdd:cd03265 159 TIGLDPQTRAHVweyIEKLKEEF-GMTILLTTHYMEE 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
389-557 |
3.55e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 389 GPSGSGKTTVLAALAGLVR-DGvgasvrGSVDGPDPRRIAWVPQHPQF-SERTVAAE-----------LALYAGAAGEGA 455
Cdd:COG0488 31 GRNGAGKSTLLKILAGELEpDS------GEVSIPKGLRIGYLPQEPPLdDDLTVLDTvldgdaelralEAELEELEAKLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 456 VPGEPGALVRELLDQLGLGGLEAADP--------------------AELSPGQQRRVAVARGLARVADgagLLLLDEPTA 515
Cdd:COG0488 105 EPDEDLERLAELQEEFEALGGWEAEAraeeilsglgfpeedldrpvSELSGGWRRRVALARALLSEPD---LLLLDEPTN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1001866046 516 HLDDASAALVERAIAALAGrvTVLLVSHEpRT--AALADRTVEL 557
Cdd:COG0488 182 HLDLESIEWLEEFLKNYPG--TVLVVSHD-RYflDRVATRILEL 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
354-555 |
3.57e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 70.45 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 354 GLRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVD----GPDPRRIAWV 429
Cdd:cd03296 2 SIEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDatdvPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 430 PQH-PQFSERTVAAELA--LYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLA---RVad 503
Cdd:cd03296 80 FQHyALFRHMTVFDNVAfgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAvepKV-- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 504 gaglLLLDEPTAHLDdasaALVERAIAALAGR------VTVLLVSHEPRTA-ALADRTV 555
Cdd:cd03296 158 ----LLLDEPFGALD----AKVRKELRRWLRRlhdelhVTTVFVTHDQEEAlEVADRVV 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
355-543 |
3.58e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 69.91 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAepAVGPLDFTAPAGrVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGPDP-----RRIAWV 429
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQpqklrRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 430 PQHPQFSERTVAAELALYAGAAGeGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLarVADgAGLLL 509
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQAL--VGD-PSILI 153
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 510 LDEPTAHLDDASAALVERAIAALAGRVTVLLVSH 543
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
938-1120 |
3.72e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 71.37 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAP--------RVGSAAVAGPVAWCPQE----------SHLFDST 999
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskiTVDGITLTAKTVWDIREkvgivfqnpdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1000 VRGNLAVARDRDHAPSDAELEAV---LARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAEVVLLDEP 1076
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVrdvLADVGMLDYIDSEP-----------ANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1001866046 1077 TAHLDPESGLALVAALHGALADR--TVVMVTHHATELMPGDTLVRL 1120
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVL 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
355-543 |
4.21e-13 |
|
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: 67.86 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDgpdprRIAWVPQhpq 434
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----KIGYFEQ--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 435 fsertvaaelalyagaagegavpgepgalvrelldqlglggleaadpaeLSPGQQRRVAVARGLARvadGAGLLLLDEPT 514
Cdd:cd03221 71 -------------------------------------------------LSGGEKMRLALAKLLLE---NPNLLLLDEPT 98
|
170 180
....*....|....*....|....*....
gi 1001866046 515 AHLDDASAALVERAIAALAGrvTVLLVSH 543
Cdd:cd03221 99 NHLDLESIEALEEALKEYPG--TVILVSH 125
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
355-543 |
4.26e-13 |
|
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: 70.50 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASV------RGSVDGPDPR-RIA 427
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWELRkRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 428 WVPQ--HPQFSERTVAAELALYAGAAGEGaVPGEPGA----LVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLarV 501
Cdd:COG1119 82 LVSPalQLRFPRDETVLDVVLSGFFDSIG-LYREPTDeqreRARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL--V 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1001866046 502 ADGAgLLLLDEPTAHLDDASAALVERAIAALA--GRVTVLLVSH 543
Cdd:COG1119 159 KDPE-LLILDEPTAGLDLGARELLLALLDKLAaeGAPTLVLVTH 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
355-553 |
5.09e-13 |
|
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: 69.77 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAepAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRG-SVDGPDPRRIA----- 427
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSvLFDGeDITGLPPHEIArlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 428 WVPQHPQ-FSERTVAAELALyagaageGAVPGEPGALVRELLDQLGLGGLEAAD---------------PAELSPGQQRR 491
Cdd:cd03219 79 RTFQIPRlFPELTVLENVMV-------AAQARTGSGLLLARARREEREARERAEellervgladladrpAGELSYGQQRR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 492 VAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHE-PRTAALADR 553
Cdd:cd03219 152 LEIARALAT---DPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDmDVVMSLADR 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
355-555 |
5.15e-13 |
|
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: 69.96 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVD----GPDPRRIAWVP 430
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 431 QH-PQFSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLarvADGAGLLL 509
Cdd:cd03300 79 QNyALFPHLTVFENIAF--GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARAL---VNEPKVLL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 510 LDEPTAHLDDASAALVERAIAALAGRV--TVLLVSHEPRTA-ALADRTV 555
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEAlTMSDRIA 202
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-549 |
6.02e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 360 LTVWYdGAAEPAVGpLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSV---------DGPDP----RRI 426
Cdd:PRK14267 10 LRVYY-GSNHVIKG-VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVrlfgrniysPDVDPievrREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 427 AWVPQHPQ-FSERTVAAELALYAGAAGEGAVPGEPGALVrELLDQLGLGGLEAAD-----PAELSPGQQRRVAVARGLAR 500
Cdd:PRK14267 88 GMVFQYPNpFPHLTIYDNVAIGVKLNGLVKSKKELDERV-EWALKKAALWDEVKDrlndyPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 501 VADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAA 549
Cdd:PRK14267 167 KPK---ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAA 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
922-1122 |
7.64e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.60 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 922 GITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGflaprvgsaavagpvawcpqeshLFDSTvR 1001
Cdd:PRK11000 3 SVTLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-----------------------LEDIT-S 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 GNLAVARDR--DHAPSDAELEAVLARVGLLEHVR---------SLPGGLDARIGSR----------GAFL-------SGG 1053
Cdd:PRK11000 58 GDLFIGEKRmnDVPPAERGVGMVFQSYALYPHLSvaenmsfglKLAGAKKEEINQRvnqvaevlqlAHLLdrkpkalSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 1054 QRQRLAVARTLLAGAEVVLLDEPTAHLDPesglAL-------VAALHGALAdRTVVMVTHHATELMP-GDTLVRLGA 1122
Cdd:PRK11000 138 QRQRVAIGRTLVAEPSVFLLDEPLSNLDA----ALrvqmrieISRLHKRLG-RTMIYVTHDQVEAMTlADKIVVLDA 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
934-1081 |
7.96e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 69.73 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS-----AAVAGPVA----WCPQESHLFDSTVRGNL 1004
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSitldgKPVEGPGAergvVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1005 AVARDRDHAPSDAELE---AVLARVGLlehvrslpGGLDARigsRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:PRK11248 92 AFGLQLAGVEKMQRLEiahQMLKKVGL--------EGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
946-1083 |
8.14e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 946 ARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQE-SHLFDSTVRGNLA-VARDRDHAPSDAELEAVL 1023
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYiKPDYDGTVEDLLRsITDDLGSSYYKSEIIKPL 441
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1024 ArvglLEHVrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPE 1083
Cdd:PRK13409 442 Q----LERL------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
941-1110 |
8.20e-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: 70.50 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 941 GLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG------------PVAWCPQESHLFDS-TVRGNLAVA 1007
Cdd:TIGR01188 11 GVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvreprkvrrSIGIVPQYASVDEDlTGRENLEMM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1008 RD-----RDHApsDAELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:TIGR01188 91 GRlyglpKDEA--EERAEELLELFELGEAADRPVGTY-----------SGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190
....*....|....*....|....*....|.
gi 1001866046 1083 ESGLA---LVAALHGalADRTVVMVTHHATE 1110
Cdd:TIGR01188 158 RTRRAiwdYIRALKE--EGVTILLTTHYMEE 186
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
956-1106 |
9.05e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 69.34 E-value: 9.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 956 GPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCP------------QESHlFDS--TVR------------GNLAvAR 1008
Cdd:COG4604 34 GPNGAGKSTLLSMISRLLPPDSGEVLVDGlDVATTPsrelakrlailrQENH-INSrlTVRelvafgrfpyskGRLT-AE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1009 DRDHapsdaeLEAVLARVGL--LEHVRslpggLDArigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGL 1086
Cdd:COG4604 112 DREI------IDEAIAYLDLedLADRY-----LDE--------LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSV 172
|
170 180
....*....|....*....|...
gi 1001866046 1087 ALVAALHGaLAD---RTVVMVTH 1106
Cdd:COG4604 173 QMMKLLRR-LADelgKTVVIVLH 194
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
925-1107 |
1.03e-12 |
|
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: 69.46 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 925 LRGVTVGWT-GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGpvawcpQESHLFDSTVRGN 1003
Cdd:TIGR03873 2 LRLSRVSWSaGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAG------VDLHGLSRRARAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1004 LA--VARDRDHAPSDAELEAVLarVGLLEHvRSLPGG--------LDARIGSRGA---------FLSGGQRQRLAVARTL 1064
Cdd:TIGR03873 76 RValVEQDSDTAVPLTVRDVVA--LGRIPH-RSLWAGdsphdaavVDRALARTELshladrdmsTLSGGERQRVHVARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1001866046 1065 LAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHH 1107
Cdd:TIGR03873 153 AQEPKLLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAALH 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
375-545 |
1.11e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGPDPRRIAWVPQHPQFSERTVAAELalyAGAAGEG 454
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAVEL---LNAVGLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 455 AVPgepgaLVRelldqlglggleaADPAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALA- 533
Cdd:COG2401 126 DAV-----LWL-------------RRFKELSTGQKFRFRLALLLAE---RPKLLVIDEFCSHLDRQTAKRVARNLQKLAr 184
|
170
....*....|...
gi 1001866046 534 -GRVTVLLVSHEP 545
Cdd:COG2401 185 rAGITLVVATHHY 197
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
941-1107 |
1.19e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.86 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 941 GLD---LAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------------PVAWCPQ--ESHLFDS 998
Cdd:PRK13641 22 GLDnisFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQfpEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 TVrgnlavARDRDHAPSD---AELEAVLARVGLLEHVrslpgGLDARIGSRGAF-LSGGQRQRLAVARTLLAGAEVVLLD 1074
Cdd:PRK13641 102 TV------LKDVEFGPKNfgfSEDEAKEKALKWLKKV-----GLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 1075 EPTAHLDPESGLALVAA-LHGALADRTVVMVTHH 1107
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHN 204
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
375-544 |
1.30e-12 |
|
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: 67.83 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGPDPR--------RIAWVPQHP--QFSERTVAAEL 444
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkgllerrqRVGLVFQDPddQLFAADVDQDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 445 ALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAAL 524
Cdd:TIGR01166 91 AF--GPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPD---VLLLDEPTAGLDPAGREQ 165
|
170 180
....*....|....*....|.
gi 1001866046 525 VERAIAAL-AGRVTVLLVSHE 544
Cdd:TIGR01166 166 MLAILRRLrAEGMTVVISTHD 186
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
355-555 |
1.36e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.66 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRGSVDGPDP-----RRIAW 428
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTiTVGGMVLSEETvwdvrRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 429 VPQHP--QFSERTVAAELALyaGAAGEGaVPGEpgALVRELLDQLGLGGLEA---ADPAELSPGQQRRVAVARGLARVAD 503
Cdd:PRK13635 86 VFQNPdnQFVGATVQDDVAF--GLENIG-VPRE--EMVERVDQALRQVGMEDflnREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 504 gagLLLLDEPTAHLDDASAALVERAIAAL--AGRVTVLLVSHEPRTAALADRTV 555
Cdd:PRK13635 161 ---IIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVI 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
956-1112 |
1.49e-12 |
|
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: 70.22 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 956 GPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------PVAWCPQESHLFDS-TVRGNLAVARDRDHAPSDAELEAVL 1023
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGedvtnvpphlrHINMVFQSYALFPHmTVEENVAFGLKMRKVPRAEIKPRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1024 ARVGLLEhvrslpggLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD----PESGLALVAALHGalADR 1099
Cdd:TIGR01187 83 EALRLVQ--------LEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQ--LGI 152
|
170
....*....|...
gi 1001866046 1100 TVVMVTHHATELM 1112
Cdd:TIGR01187 153 TFVFVTHDQEEAM 165
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
355-555 |
1.66e-12 |
|
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: 68.16 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEP--AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDGPD--------PR 424
Cdd:cd03266 2 ITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG---FATVDGFDvvkepaeaRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 425 RIAWVPQHPQFSERTVAAELALYAGAAgEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLarVADg 504
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGL-YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL--VHD- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 505 AGLLLLDEPTAHLDDASAALVERAIAAL-AGRVTVLLVSHE-PRTAALADRTV 555
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHImQEVERLCDRVV 207
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
354-549 |
2.08e-12 |
|
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: 68.69 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 354 GLRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR------DGVGASVRGSVDGPDPRRIA 427
Cdd:TIGR03873 1 GLRLSRVSWSAGG--RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRpdagtvDLAGVDLHGLSRRARARRVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 428 WVPQH----PQFSERTVAAeLALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARvad 503
Cdd:TIGR03873 79 LVEQDsdtaVPLTVRDVVA-LGRIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQ--- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1001866046 504 GAGLLLLDEPTAHLDDASAALVERAIAALAG-RVTVLLVSHEPRTAA 549
Cdd:TIGR03873 155 EPKLLLLDEPTNHLDVRAQLETLALVRELAAtGVTVVAALHDLNLAA 201
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-549 |
2.12e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.40 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSV--DGPD---------PRRIAWVPQHPQ-FSERTVAA 442
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVylDGQDifkmdvielRRRVQMVFQIPNpIPNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 443 ELALYAGAAGEGAVPGEPGALVRELLDQLG----LGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLD 518
Cdd:PRK14247 102 NVALGLKLNRLVKSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPE---VLLADEPTANLD 178
|
170 180 190
....*....|....*....|....*....|.
gi 1001866046 519 DASAALVERAIAALAGRVTVLLVSHEPRTAA 549
Cdd:PRK14247 179 PENTAKIESLFLELKKDMTIVLVTHFPQQAA 209
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
932-1106 |
2.12e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 932 WTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFL--------------------APRVGSAAVAGPVAWCPQ 991
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneearvegevrlfgrniySPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 992 ESHLFDS-TVRGNLAVARD-----RDHAPSDAELEAVLARVGLLEHVRSlpggldaRIGSRGAFLSGGQRQRLAVARTLL 1065
Cdd:PRK14267 93 YPNPFPHlTIYDNVAIGVKlnglvKSKKELDERVEWALKKAALWDEVKD-------RLNDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1001866046 1066 AGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
370-544 |
2.32e-12 |
|
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: 67.99 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 370 PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVRgsVDGPD------------PRRIAWVPQHPQ-FS 436
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSG-SVL--VDGTDltllsgkelrkaRRRIGMIFQHFNlLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 437 ERTVAAELALYAGAAGEGAVpgEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAH 516
Cdd:cd03258 96 SRTVFENVALPLEIAGVPKA--EIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK---VLLCDEATSA 170
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 517 LDDASAalveRAIAALAGRV------TVLLVSHE 544
Cdd:cd03258 171 LDPETT----QSILALLRDInrelglTIVLITHE 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
355-553 |
3.03e-12 |
|
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: 67.70 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRdgvgaSVRGSV--DGPD---------P 423
Cdd:COG0410 4 LEVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-----PRSGSIrfDGEDitglpphriA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 424 RR-IAWVPQHPQ-FSERTVAA--ELALYAGAAGEGAvpgepgalvrelldqlglggleAADPAE---------------- 483
Cdd:COG0410 77 RLgIGYVPEGRRiFPSLTVEEnlLLGAYARRDRAEV----------------------RADLERvyelfprlkerrrqra 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 484 --LSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLddaSAALVE---RAIAALAGR-VTVLLVSHEPRTA-ALADR 553
Cdd:COG0410 135 gtLSGGEQQMLAIGRALMS---RPKLLLLDEPSLGL---APLIVEeifEIIRRLNREgVTILLVEQNARFAlEIADR 205
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
937-1081 |
3.74e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.15 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 937 DVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVG-------------SAAVAG----PVAWCPQESHLF-DS 998
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdvifngqpmsklsSAAKAElrnqKLGFIYQFHHLLpDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 TVRGNLAVARDRDH-APSDAELEA--VLARVGLlehvrslpgglDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDE 1075
Cdd:PRK11629 103 TALENVAMPLLIGKkKPAEINSRAleMLAAVGL-----------EHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
....*.
gi 1001866046 1076 PTAHLD 1081
Cdd:PRK11629 172 PTGNLD 177
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
375-545 |
4.49e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGPDPRRIAWV----PQHPQFSERTVAAELALYAga 450
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAChylgHRNAMKPALTVAENLEFWA-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 451 agegAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIA 530
Cdd:PRK13539 99 ----AFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS---NRPIWILDEPTAALDAAAVALFAELIR 171
|
170
....*....|....*.
gi 1001866046 531 A-LAGRVTVLLVSHEP 545
Cdd:PRK13539 172 AhLAQGGIVIAATHIP 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
360-557 |
4.63e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.90 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 360 LTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGP--------DPR-RIAWVP 430
Cdd:PRK13640 11 VSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGItltaktvwDIReKVGIVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 431 QHP--QFSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARvadGAGLL 508
Cdd:PRK13640 91 QNPdnQFVGATVGDDVAF--GLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV---EPKII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 509 LLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAALADRTVEL 557
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVL 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
355-543 |
4.69e-12 |
|
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: 67.37 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAepAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--------DGVgasvrgSVDGPDPRRI 426
Cdd:COG0411 5 LEVRGLTKRFGGLV--AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgrilfDGR------DITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 427 AWVP-----QHPQ-FSERTVA--AELALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAAD-----------PAELSPG 487
Cdd:COG0411 77 ARLGiartfQNPRlFPELTVLenVLVAAHARLGRGLLAALLRLPRARREEREARERAEELLErvgladradepAGNLSYG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 488 QQRRVAVARGLARvadGAGLLLLDEPTAHLDDA-SAALVE--RAIAALAGrVTVLLVSH 543
Cdd:COG0411 157 QQRRLEIARALAT---EPKLLLLDEPAAGLNPEeTEELAEliRRLRDERG-ITILLIEH 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
915-1106 |
4.91e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 70.27 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 915 DAPGrGPGITLRGVTVGWTGGPDVLA----GLDLAARpgdwIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCP 990
Cdd:PLN03073 502 DRPG-PPIISFSDASFGYPGGPLLFKnlnfGIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 QESHLFDSTvrgnlavarDRDHAPsdaeleavlarvgLLEHVRSLPG----GLDARIGSRGA----------FLSGGQRQ 1056
Cdd:PLN03073 577 FSQHHVDGL---------DLSSNP-------------LLYMMRCFPGvpeqKLRAHLGSFGVtgnlalqpmyTLSGGQKS 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1057 RLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALhgALADRTVVMVTH 1106
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSH 682
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
375-545 |
5.24e-12 |
|
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: 66.36 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRdgvgasvrgsvdgPDPRRIAWvPQHPQFSERTVAAELALYAGAAgeg 454
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP-------------PLAGRVLL-NGGPLDFQRDSIARGLLYLGHA--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 455 avPGEPGAL-----------------VRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLarvADGAGLLLLDEPTAHL 517
Cdd:cd03231 82 --PGIKTTLsvlenlrfwhadhsdeqVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLL---LSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*....
gi 1001866046 518 DDASAALVERAIAALAGR-VTVLLVSHEP 545
Cdd:cd03231 157 DKAGVARFAEAMAGHCARgGMVVLTTHQD 185
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
920-1106 |
5.31e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.10 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 920 GPGITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-------------V 986
Cdd:PRK09536 1 MPMIDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 987 AWCPQESHL-FDSTVRGNLAVAR-------DRDHAPSDAELEAVLARVGLLEHVrslpgglDARIGSrgafLSGGQRQRL 1058
Cdd:PRK09536 80 ASVPQDTSLsFEFDVRQVVEMGRtphrsrfDTWTETDRAAVERAMERTGVAQFA-------DRPVTS----LSGGERQRV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1059 AVARTLLAGAEVVLLDEPTAHLDPESG---LALVAALhgALADRTVVMVTH 1106
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQvrtLELVRRL--VDDGKTAVAAIH 197
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
935-1113 |
5.86e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.41 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 935 GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAW-------CPQ---------ESHLFD 997
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYdkkslleVRKtvgivfqnpDDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 998 STVRGNLAVARDRDHAPSDAELEAV---LARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAEVVLLD 1074
Cdd:PRK13639 94 PTVEEDVAFGPLNLGLSKEEVEKRVkeaLKAVGMEGFENKPP-----------HHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 1075 EPTAHLDPESGLALVAALHGALADRTVVMVTHHATELMP 1113
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVP 201
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
923-1106 |
7.41e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.96 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-------------VAWC 989
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 990 PQEsHLF--DSTVRGNLAVAR-----------DRDHAPSDAELEAVlarvglleHVRSLPgglDARIGSrgafLSGGQRQ 1056
Cdd:PRK11231 82 PQH-HLTpeGITVRELVAYGRspwlslwgrlsAEDNARVNQAMEQT--------RINHLA---DRRLTD----LSGGQRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 1057 RLAVARTLLAGAEVVLLDEPTAHLDPESGLALVaALHGALAD--RTVVMVTH 1106
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELM-RLMRELNTqgKTVVTVLH 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
991-1125 |
8.20e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 QESHLFDSTVRGNLAVARDrdhapsDAELEAVlARV----GLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLA 1066
Cdd:PTZ00265 1303 QEPMLFNMSIYENIKFGKE------DATREDV-KRAckfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLR 1375
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1067 GAEVVLLDEPTAHLDPESGLALVAALHGA--LADRTVVMVTHHATELMPGDTLVRLGARER 1125
Cdd:PTZ00265 1376 EPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNPDR 1436
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
355-557 |
8.38e-12 |
|
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: 66.30 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEP--AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVRgsVDGPD---------- 422
Cdd:COG4181 9 IELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSG-TVR--LAGQDlfaldedara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 423 ---PRRIAWVPQhpqfSERTVAAELALyagaagEG-AVP----GEPGALVRELLDQLGLGGLEAAD--PAELSPGQQRRV 492
Cdd:COG4181 86 rlrARHVGFVFQ----SFQLLPTLTAL------ENvMLPlelaGRRDARARARALLERVGLGHRLDhyPAQLSGGEQQRV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 493 AVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAALADRTVEL 557
Cdd:COG4181 156 ALARAFATEPA---ILFADEPTGNLDAATGEQIIDLLFELNRErgTTLVLVTHDPALAARCDRVLRL 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
939-1105 |
8.74e-12 |
|
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: 65.36 E-value: 8.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 939 LAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGsaaVAGPVAWCPQESHLFDSTVRGNLA-VARDRDHAPsda 1017
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS---VEGDIHYNGIPYKEFAEKYPGEIIyVSEEDVHFP--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1018 eleaVLARVGLLEHVRSLPGglDARIgsRGafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHgALA 1097
Cdd:cd03233 97 ----TLTVRETLDFALRCKG--NEFV--RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIR-TMA 165
|
170
....*....|
gi 1001866046 1098 D--RTVVMVT 1105
Cdd:cd03233 166 DvlKTTTFVS 175
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
923-1113 |
9.00e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.14 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP---------------VA 987
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 988 WCPQESHLFDSTVRGNLA---VARDRDHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTL 1064
Cdd:PRK13652 84 FQNPDDQIFSPTVEQDIAfgpINLGLDEETVAHRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 1065 LAGAEVVLLDEPTAHLDPEsGLALVAALHGALADR---TVVMVTHHaTELMP 1113
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQ-GVKELIDFLNDLPETygmTVIFSTHQ-LDLVP 202
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
376-555 |
9.47e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 66.17 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 376 DFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--------DGVgasvrgSVDGPDP------RRIAWVPQHPQ-FSERTV 440
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtitvDGE------DLTDSKKdinklrRKVGMVFQQFNlFPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 441 AAELALyagaagegavpgepgALVRELLDQLGLGGLEA------------AD--PAELSPGQQRRVAVARGLA---RVad 503
Cdd:COG1126 95 LENVTL---------------APIKVKKMSKAEAEERAmellervgladkADayPAQLSGGQQQRVAIARALAmepKV-- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 504 gaglLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHEPRTA-ALADRTV 555
Cdd:COG1126 158 ----MLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFArEVADRVV 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
376-555 |
1.02e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 66.33 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 376 DFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVRgsVDGPD---------PRRIAWVPQHPQ----FSERTVAA 442
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSG-EVR--LNGRPladwspaelARRRAVLPQHSSlsfpFTVEEVVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 443 elalyAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLA---RVADGAGLLLLDEPTAHLDD 519
Cdd:PRK13548 99 -----MGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwEPDGPPRWLLLDEPTSALDL 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 520 ASAALVERAIAALAGR--VTVLLVSHEPRTAAL-ADRTV 555
Cdd:PRK13548 174 AHQHHVLRLARQLAHErgLAVIVVLHDLNLAARyADRIV 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
344-548 |
1.08e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.94 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 344 RPPA--GQAAPAGLRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVD-- 419
Cdd:PRK11607 7 RPQAktRKALTPLLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDls 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 420 --GPDPRRIAWVPQ-HPQFSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVAR 496
Cdd:PRK11607 85 hvPPYQRPINMMFQsYALFPHMTVEQNIAF--GLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALAR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 497 GLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGRV--TVLLVSHEPRTA 548
Cdd:PRK11607 163 SLAKRPK---LLLLDEPMGALDKKLRDRMQLEVVDILERVgvTCVMVTHDQEEA 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
938-1112 |
1.13e-11 |
|
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: 69.59 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTL-LAL------------LTGFLAPRVGSAAVAGPVAWCPQESHLFDSTVRGNL 1004
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLfrinesaegeiiIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1005 avarDRDHAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPES 1084
Cdd:TIGR00957 1381 ----DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
170 180
....*....|....*....|....*...
gi 1001866046 1085 GLALVAALHGALADRTVVMVTHHATELM 1112
Cdd:TIGR00957 1457 DNLIQSTIRTQFEDCTVLTIAHRLNTIM 1484
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
375-557 |
1.40e-11 |
|
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: 65.21 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVD----GPDPRRIAWVPQHPQ-FSERTVAAELALyag 449
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDvtaaPPADRPVSMLFQENNlFAHLTVEQNVGL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 450 aageGAVPG-----EPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAAL 524
Cdd:cd03298 94 ----GLSPGlkltaEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVR---DKPVLLLDEPFAALDPALRAE 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1001866046 525 VERAIAALAG--RVTVLLVSHEPRTA-ALADRTVEL 557
Cdd:cd03298 167 MLDLVLDLHAetKMTVLMVTHQPEDAkRLAQRVVFL 202
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
938-1107 |
1.73e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 65.43 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESHL--------------FDSTVRGN 1003
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLrrigvvfgqktqlwWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1004 LAVARDRDHAPsDAELEAVLARVGLLEHVRSLpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPE 1083
Cdd:cd03267 116 FYLLAAIYDLP-PARFKKRLDELSELLDLEEL---LDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180
....*....|....*....|....*
gi 1001866046 1084 SGLALVAALHGALADR-TVVMVTHH 1107
Cdd:cd03267 188 AQENIRNFLKEYNRERgTTVLLTSH 212
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
370-546 |
1.85e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 64.30 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 370 PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRdgvgasvrgsvdgPDPRRIAWvPQHPQFSERTVAAELALYAG 449
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR-------------PDSGEVRW-NGTPLAEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 450 AAgegavPGEPGAL-------------------VRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLarvADGAGLLLL 510
Cdd:TIGR01189 80 HL-----PGLKPELsalenlhfwaaihggaqrtIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLW---LSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1001866046 511 DEPTAHLDDASAALVERAIAALAGRV-TVLLVSHEPR 546
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGgIVLLTTHQDL 188
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
938-1082 |
2.20e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.05 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDwiVVA--GPSGSGKSTLLALLTGFLAPRVGSAAVAG------P--------VAWCPQESHLF-DSTV 1000
Cdd:COG1137 18 VVKDVSLEVNQGE--IVGllGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlPmhkrarlgIGYLPQEASIFrKLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 RGN-LAVA--RDRDHAPSDAELEAVLARVGLlEHVRSlpggldarigSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPT 1077
Cdd:COG1137 96 EDNiLAVLelRKLSKKEREERLEELLEEFGI-THLRK----------SKAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
....*
gi 1001866046 1078 AHLDP 1082
Cdd:COG1137 165 AGVDP 169
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
375-553 |
2.56e-11 |
|
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: 65.05 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDG-------PDPRRIAWVPQ-HPQFSERTVAAELAL 446
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSG---KILLNGkditnlpPEKRDISYVPQnYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 447 yaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLarVADgAGLLLLDEPTAHLDdasAALVE 526
Cdd:cd03299 95 --GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARAL--VVN-PKILLLDEPFSALD---VRTKE 166
|
170 180 190
....*....|....*....|....*....|...
gi 1001866046 527 RAIAALA-----GRVTVLLVSHE-PRTAALADR 553
Cdd:cd03299 167 KLREELKkirkeFGVTVLHVTHDfEEAWALADK 199
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
375-543 |
2.66e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 64.69 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDGPD---------P---RRIAWVPQ-HPQFSERTVA 441
Cdd:COG2884 21 VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSG---QVLVNGQDlsrlkrreiPylrRRIGVVFQdFRLLPDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 442 AELALYAGAAGEGavPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDAS 521
Cdd:COG2884 98 ENVALPLRVTGKS--RKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE---LLLADEPTGNLDPET 172
|
170 180
....*....|....*....|...
gi 1001866046 522 AALVERAIAALAGR-VTVLLVSH 543
Cdd:COG2884 173 SWEIMELLEEINRRgTTVLIATH 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
938-1118 |
2.66e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.49 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAV-----------------AGPVAWCPqESHLFDSTV 1000
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldtsdeenlwdirnkAGMVFQNP-DNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 RGNLAVARDRDHAPSD---AELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAEVVLLDEPT 1077
Cdd:PRK13633 104 EEDVAFGPENLGIPPEeirERVDESLKKVGMYEYRRHAP-----------HLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1001866046 1078 AHLDPeSGLALVAALHGALADR---TVVMVTHHATELMPGDTLV 1118
Cdd:PRK13633 173 AMLDP-SGRREVVNTIKELNKKygiTIILITHYMEEAVEADRII 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
375-555 |
2.87e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.16 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRG--SVDGPDP-----RRIAWVPQHPQF--------SERT 439
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGdiTIDTARSlsqqkGLIRQLRQHVGFvfqnfnlfPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 440 VAAELAlyagaAGEGAVPGEPG----ALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTA 515
Cdd:PRK11264 102 VLENII-----EGPVIVKGEPKeeatARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPE---VILFDEPTS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1001866046 516 HLDDASAALVERAIAALAG-RVTVLLVSHEPRTAA-LADRTV 555
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARdVADRAI 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
375-544 |
2.99e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 64.73 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAAL--------AGLVRDGVgaSVRG-SVDGPDPRRIA-WVPQH----PQFSertv 440
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitsGDLIVDGL--KVNDpKVDERLIRQEAgMVFQQfylfPHLT---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 441 AAELALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDA 520
Cdd:PRK09493 94 ALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK---LMLFDEPTSALDPE 170
|
170 180
....*....|....*....|....*
gi 1001866046 521 SAALVERAIAALAGR-VTVLLVSHE 544
Cdd:PRK09493 171 LRHEVLKVMQDLAEEgMTMVIVTHE 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
938-1106 |
3.24e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.42 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFlaprvgSAAVAGPVAWCPQESHLFDSTVRGNL------------- 1004
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGL------DDGSSGEVSLVGQPLHQMDEEARAKLrakhvgfvfqsfm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1005 --------------AVARDRDHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAEV 1070
Cdd:PRK10584 99 liptlnalenvelpALLRGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1001866046 1071 VLLDEPTAHLDPESGLALVAALHGALADR--TVVMVTH 1106
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
944-1112 |
3.33e-11 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 64.49 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 944 LAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG--------PVAWCPQESHL---FDSTVRGNLAVARDR-- 1010
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGaspgkgwrHIGYVPQRHEFawdFPISVAHTVMSGRTGhi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1011 ---------DHAPSDAELEavlaRVGLlEHVRSLPGGLdarigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:TIGR03771 81 gwlrrpcvaDFAAVRDALR----RVGL-TELADRPVGE----------LSGGQRQRVLVARALATRPSVLLLDEPFTGLD 145
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 1082 ---PESGLALVAALHGalADRTVVMVTHHATELM 1112
Cdd:TIGR03771 146 mptQELLTELFIELAG--AGTAILMTTHDLAQAM 177
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
355-557 |
3.93e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.01 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGaaEPAVGPLDFTAPAG-RVTVLaGPSGSGKTT-------VLAALAGLVRdgVGASVRgsvdgpdprrI 426
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGdRIGLI-GPNGAGKSTllkllagELEPDSGTVK--LGETVK----------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 427 AWVPQHPQF--SERTVAAELALYAGAAGEGAV---------PGEpgalvrelldqlglgglEAADPAE-LSPGQQRRVAv 494
Cdd:COG0488 381 GYFDQHQEEldPDKTVLDELRDGAPGGTEQEVrgylgrflfSGD-----------------DAFKPVGvLSGGEKARLA- 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 495 argLARV-ADGAGLLLLDEPTAHLDDASAALVERAIAALAGrvTVLLVSHEPR-TAALADRTVEL 557
Cdd:COG0488 443 ---LAKLlLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG--TVLLVSHDRYfLDRVATRILEF 502
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
371-555 |
4.52e-11 |
|
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: 63.81 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 371 AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVD----GPDPRRIAWVPQ-HPQFSERTVAAELA 445
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdlPPKDRDIAMVFQnYALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 446 LyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDdasAALV 525
Cdd:cd03301 95 F--GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK---VFLMDEPLSNLD---AKLR 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1001866046 526 ERAIAALAG-----RVTVLLVSHEPRTA-ALADRTV 555
Cdd:cd03301 167 VQMRAELKRlqqrlGTTTIYVTHDQVEAmTMADRIA 202
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
939-1136 |
4.65e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.73 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 939 LAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP---------------VAWCPQESHLFDSTVRGN 1003
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrrkigMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1004 LAVARDRDHAPSDAEL----EAVLArVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAH 1079
Cdd:PRK13642 103 VAFGMENQGIPREEMIkrvdEALLA-VNMLDFKTREP-----------ARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1080 LDPESGLALVAALHgALADR---TVVMVTHHATELMPGDTLVRLGARERVlhhaaRAAAP 1136
Cdd:PRK13642 171 LDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEII-----KEAAP 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
355-518 |
4.80e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.26 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYdgAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLV--RDGV----GASVRGSVDGPDPRRIAW 428
Cdd:PRK11231 3 LRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtpQSGTvflgDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 429 VPQHPQFSERTVAAELALYagaaGE-------GAVPGEPGALVREllDQLGLGGLEAADP--AELSPGQQRRVAVARGLA 499
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAY----GRspwlslwGRLSAEDNARVNQ--AMEQTRINHLADRrlTDLSGGQRQRAFLAMVLA 154
|
170
....*....|....*....
gi 1001866046 500 RVADgagLLLLDEPTAHLD 518
Cdd:PRK11231 155 QDTP---VVLLDEPTTYLD 170
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
921-1107 |
5.87e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.52 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP----------VAWCP 990
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 QESH-------LFDSTV-------RGNLAVARDRDHapsdAELEAVLARVGLLEHVRSlpggldaRIGSrgafLSGGQRQ 1056
Cdd:PRK15056 85 QSEEvdwsfpvLVEDVVmmgryghMGWLRRAKKRDR----QIVTAALARVDMVEFRHR-------QIGE----LSGGQKK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 1057 RLAVARTLLAGAEVVLLDEPTAHLDPESGlALVAALHGALAD--RTVVMVTHH 1107
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTE-ARIISLLRELRDegKTMLVSTHN 201
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
351-553 |
5.89e-11 |
|
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: 62.45 E-value: 5.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 351 APAGLRVAGLTVWydgaaePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLvRDGVGASVRgsVDGPDPRRiawvp 430
Cdd:cd03215 1 GEPVLEVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGL-RPPASGEIT--LDGKPVTR----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 431 qhpqfseRTVAAelALYAGAA-------GEGAVPGEPgalVRElldqlglgglEAADPAELSPGQQRRVAVARGLARVAD 503
Cdd:cd03215 67 -------RSPRD--AIRAGIAyvpedrkREGLVLDLS---VAE----------NIALSSLLSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 504 gagLLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHE-PRTAALADR 553
Cdd:cd03215 125 ---VLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSElDELLGLCDR 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
949-1106 |
6.71e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.68 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 949 GDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAV------------------AGPVAWCPqESHLFDSTVRGNLAVArDR 1010
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditdkkvklsdirkkVGLVFQYP-EYQLFEETIEKDIAFG-PI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1011 DHAPSDAELEAVLARVglLEHVrslpgGLD-ARIGSRGAF-LSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP---ESG 1085
Cdd:PRK13637 111 NLGLSEEEIENRVKRA--MNIV-----GLDyEDYKDKSPFeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrDEI 183
|
170 180
....*....|....*....|.
gi 1001866046 1086 LALVAALHGALaDRTVVMVTH 1106
Cdd:PRK13637 184 LNKIKELHKEY-NMTIILVSH 203
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
905-1110 |
1.02e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 905 DAAEERDDLQDAPGRGPGITLRGVTVGWTGGPD-VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVA 983
Cdd:TIGR01257 1920 DVAEERQRIISGGNKTDILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVA 1999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 984 GP------------VAWCPQeshlFDS-----TVRGNLAV-ARDRDhAPSDaELEAV----LARVGLLEHVRSLPGGLda 1041
Cdd:TIGR01257 2000 GKsiltnisdvhqnMGYCPQ----FDAiddllTGREHLYLyARLRG-VPAE-EIEKVanwsIQSLGLSLYADRLAGTY-- 2071
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 1042 rigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVTHHATE 1110
Cdd:TIGR01257 2072 ---------SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2131
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
956-1081 |
1.03e-10 |
|
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: 64.75 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 956 GPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------------PVAWCPQESHLFDS-TVRGNLAVARDRDHAPS-D 1016
Cdd:TIGR02142 30 GRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLFPHlSVRGNLRYGMKRARPSErR 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 1017 AELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:TIGR02142 110 ISFERVIELLGIGHLLGRLPGRL-----------SGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
355-554 |
1.38e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 63.26 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYdgAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSV---------DGPDP-- 423
Cdd:PRK14243 11 LRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVtfhgknlyaPDVDPve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 424 --RRIAWVPQHPQFSERTVAAELALYAGAAGegaVPGEPGALVrELLDQLGLGGLEAADPAE-----LSPGQQRRVAVAR 496
Cdd:PRK14243 89 vrRRIGMVFQKPNPFPKSIYDNIAYGARING---YKGDMDELV-ERSLRQAALWDEVKDKLKqsglsLSGGQQQRLCIAR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 497 GLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAA-LADRT 554
Cdd:PRK14243 165 AIAVQPE---VILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAArVSDMT 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
131-283 |
1.42e-10 |
|
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: 63.43 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 131 RGLDGLDALYTQYLPALVQTAVLPLLVGARILGADWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVE 210
Cdd:pfam00664 106 NDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEE 185
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 211 LAQGLPVLVGLGR-AAEQRRALGELSRAYKgrtmATLRVAFLSAL---ALELISTISVAVVAvFIGIRLVH-GDMTLE 283
Cdd:pfam00664 186 SLSGIRTVKAFGReEYELEKYDKALEEALK----AGIKKAVANGLsfgITQFIGYLSYALAL-WFGAYLVIsGELSVG 258
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
938-1112 |
1.51e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.33 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-----------VAWCPQESHLFDS-TVRGNLA 1005
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHYALFRHmTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1006 VA------RDRdhaPSDAELEAVLARvgLLEHVRSlpGGLDARIGSRgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAH 1079
Cdd:PRK10851 97 FGltvlprRER---PNAAAIKAKVTQ--LLEMVQL--AHLADRYPAQ---LSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1001866046 1080 LDPESGLAL---VAALHGALaDRTVVMVTHHATELM 1112
Cdd:PRK10851 167 LDAQVRKELrrwLRQLHEEL-KFTSVFVTHDQEEAM 201
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
370-557 |
1.70e-10 |
|
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: 62.04 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 370 PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVRgsVDGPD-----PRRIAWVPQH--PQFSERTVAA 442
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSG-TIR--VNGQDvsdlrGRAIPYLRRKigVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 443 ELALYAGAAGEGAVPGEPGALVRELLDQLGLGG----LEAADPAELSPGQQRRVAVARGlarVADGAGLLLLDEPTAHLD 518
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKRVPAALELVglshKHRALPAELSGGEQQRVAIARA---IVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1001866046 519 DASAALVERAIAALAGR-VTVLLVSHEPR-TAALADRTVEL 557
Cdd:cd03292 169 PDTTWEIMNLLKKINKAgTTVVVATHAKElVDTTRHRVIAL 209
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
134-318 |
1.76e-10 |
|
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: 63.34 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 134 DGLDALYTQYLPALVQTAVLPLLVGARILGADWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQ 213
Cdd:cd07346 107 DAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 214 GLPVLVGLGRAAEQRRALGELSRAYKGRTMATLRVAFLSALALELISTISVAVVAVFIGIRLVHGDMTLEAGLLALILAP 293
Cdd:cd07346 187 GIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLG 266
|
170 180
....*....|....*....|....*
gi 1001866046 294 ECFQPLRDLGTAHHASEDGAEALRR 318
Cdd:cd07346 267 MLFGPIQRLANLYNQLQQALASLER 291
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
938-1103 |
1.94e-10 |
|
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: 62.07 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTG-----------------------------------------FL--A 974
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsilvrhdggwvdlaqaspreilalrrrtigyvsqFLrvI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 975 PRVGS-AAVAGPvawcpqeshlfdstvrgnlAVARDRDHAPSDAELEAVLARVGLLEHVRSLPGgldarigsrgAFLSGG 1053
Cdd:COG4778 106 PRVSAlDVVAEP-------------------LLERGVDREEARARARELLARLNLPERLWDLPP----------ATFSGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 1054 QRQRLAVARTLLAGAEVVLLDEPTAHLDPES--------------GLALVAALH-----GALADRTVVM 1103
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANravvvelieeakarGTAIIGIFHdeevrEAVADRVVDV 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
895-1092 |
2.00e-10 |
|
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: 64.96 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 895 RVAAEEQAVRDAAEERDDLQD---APGRGPG---ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLAL 968
Cdd:TIGR03719 289 RLARYEELLSQEFQKRNETAEiyiPPGPRLGdkvIEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRM 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 969 LTGFLAPRVGSAAVAgpvawcpqeshlfdSTVRgnLA-VARDRDH-APSDAELEAVlarvgllehvrslPGGLD------ 1040
Cdd:TIGR03719 368 ITGQEQPDSGTIEIG--------------ETVK--LAyVDQSRDAlDPNKTVWEEI-------------SGGLDiiklgk 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 1041 ARIGSR---GAF-------------LSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAAL 1092
Cdd:TIGR03719 419 REIPSRayvGRFnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL 486
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
361-552 |
2.07e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 64.65 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 361 TVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVlAALAGLVRDGVGASVrgSVDGPDPR---------RIAWVPQ 431
Cdd:PRK11176 348 TFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI-ANLLTRFYDIDEGEI--LLDGHDLRdytlaslrnQVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 432 HPQFSERTVAAELAlYAG----------AAGEGA---------------VPGEPGALvrelldqlglggleaadpaeLSP 486
Cdd:PRK11176 425 NVHLFNDTIANNIA-YARteqysreqieEAARMAyamdfinkmdngldtVIGENGVL--------------------LSG 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 487 GQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALAD 552
Cdd:PRK11176 484 GQRQRIAIARALLR---DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKAD 546
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
934-1082 |
2.11e-10 |
|
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: 62.03 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPvAWCPQESH----LFDS-------TVRG 1002
Cdd:TIGR03740 11 GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH-PWTRKDLHkigsLIESpplyenlTARE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1003 NLAVARDRDHAPsDAELEAVLARVGLlEHVRSLPGGLdarigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:TIGR03740 90 NLKVHTTLLGLP-DSRIDEVLNIVDL-TNTGKKKAKQ----------FSLGMKQRLGIAIALLNHPKLLILDEPTNGLDP 157
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
375-552 |
2.21e-10 |
|
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: 62.25 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALaglVR--DGVGASVRgsVDGPDPR---------RIAWVPQH-PQFSErTVAA 442
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLL---FRfyDVSSGSIL--IDGQDIRevtldslrrAIGVVPQDtVLFND-TIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 443 ELAlYagaagegavpGEPGALVRELLdqlglgglEAADPAE----------------------LSPGQQRRVAVARGLAR 500
Cdd:cd03253 94 NIR-Y----------GRPDATDEEVI--------EAAKAAQihdkimrfpdgydtivgerglkLSGGEKQRVAIARAILK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 501 VADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALAD 552
Cdd:cd03253 155 NPP---ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNAD 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
923-1106 |
2.24e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP--VAWCPQESHLfDSTV 1000
Cdd:PRK09544 5 VSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYL-DTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 rgNLAVARDRDHAPS--DAELEAVLARVGLlEHVrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTA 1078
Cdd:PRK09544 83 --PLTVNRFLRLRPGtkKEDILPALKRVQA-GHL------IDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190
....*....|....*....|....*....|.
gi 1001866046 1079 HLDPESGLA---LVAALHGALaDRTVVMVTH 1106
Cdd:PRK09544 150 GVDVNGQVAlydLIDQLRREL-DCAVLMVSH 179
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
923-1106 |
2.28e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.53 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPdVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRvgsaavAGPVAW--------CPQE-S 993
Cdd:PRK15064 320 LEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPD------SGTVKWsenanigyYAQDhA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 994 HLFDSTVrgNLAVARDRDHAPSDAELeAVLARVGllehvRSLPGGLDarIGSRGAFLSGGQRQRLAVARTLLAGAEVVLL 1073
Cdd:PRK15064 393 YDFENDL--TLFDWMSQWRQEGDDEQ-AVRGTLG-----RLLFSQDD--IKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190
....*....|....*....|....*....|...
gi 1001866046 1074 DEPTAHLDPESGLALVAALHgaLADRTVVMVTH 1106
Cdd:PRK15064 463 DEPTNHMDMESIESLNMALE--KYEGTLIFVSH 493
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
375-543 |
2.35e-10 |
|
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: 62.17 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAglvR--DGVGASVrgSVDGPDPRR---------IAWVPQHPQFSERTVAAE 443
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLE---RfyDPTSGEI--LLDGVDIRDlnlrwlrsqIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 444 LALyagaagegavpGEPGALVRELLdqlglgglEAADPAE----------------------LSPGQQRRVAVARGLARV 501
Cdd:cd03249 97 IRY-----------GKPDATDEEVE--------EAAKKANihdfimslpdgydtlvgergsqLSGGQKQRIAIARALLRN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1001866046 502 ADgagLLLLDEPTAHLDDASAALVERAI-AALAGRvTVLLVSH 543
Cdd:cd03249 158 PK---ILLLDEATSALDAESEKLVQEALdRAMKGR-TTIVIAH 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
375-557 |
2.57e-10 |
|
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: 61.33 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRdgvgaSVRGSVDGpdPRRIAWVPQHP-------------------QF 435
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELE-----KLSGSVSV--PGSIAYVSQEPwiqngtirenilfgkpfdeER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 436 SERTVAA-----ELALYAGaaGEGAVPGEPGALvrelldqlglggleaadpaeLSPGQQRRVAVARGLARVADgagLLLL 510
Cdd:cd03250 97 YEKVIKAcalepDLEILPD--GDLTEIGEKGIN--------------------LSGGQKQRISLARAVYSDAD---IYLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 511 DEPTAHLD-DASAALVERAI-AALAGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:cd03250 152 DDPLSAVDaHVGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVL 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
344-548 |
2.60e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.40 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 344 RPPagQAAPAGLRVAGLTvwYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA---SVRGSVDG 420
Cdd:PRK13543 3 EPL--HTAPPLLAAHALA--FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQiqiDGKTATRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 421 PDPRRIAWVPQHPQFSERTVAAE-LALYAGAAGEGA--VPGEPGALVrelldqlGLGGLEAADPAELSPGQQRRVAVARg 497
Cdd:PRK13543 79 DRSRFMAYLGHLPGLKADLSTLEnLHFLCGLHGRRAkqMPGSALAIV-------GLAGYEDTLVRQLSAGQKKRLALAR- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 498 laRVADGAGLLLLDEPTAHLDDASAALVERAIAA-LAGRVTVLLVSHEPRTA 548
Cdd:PRK13543 151 --LWLSPAPLWLLDEPYANLDLEGITLVNRMISAhLRGGGAALVTTHGAYAA 200
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
880-1083 |
2.69e-10 |
|
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: 64.43 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 880 STAVQQLPALRSALV---RVAAEEQAVRDAAEERDDLQDAPGRGP--GITLRGVT---------VGWTGGPdvlagLDLA 945
Cdd:COG4615 280 SQLVGALPTLSRANValrKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTyrypgedgdEGFTLGP-----IDLT 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 946 ARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCPQES------------HLFDSTVrgnlavarDRDH 1012
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqPVTADNREAyrqlfsavfsdfHLFDRLL--------GLDG 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1013 APSDAELEAVLARVGlLEHVRSLPGGldaRIGSRGafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPE 1083
Cdd:COG4615 427 EADPARARELLERLE-LDHKVSVEDG---RFSTTD--LSQGQRKRLALLVALLEDRPILVFDEWAADQDPE 491
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
938-1107 |
3.15e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS---------------AAVAGpVAWCPQESHLFDS-TVR 1001
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEilldgepvrfrsprdAQAAG-IAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 GNLAVARDR------DHAPSDAELEAVLARVGLleHVRslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDE 1075
Cdd:COG1129 98 ENIFLGREPrrggliDWRAMRRRARELLARLGL--DID-----PDTPVGD----LSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1001866046 1076 PTAHLDPESglalVAALHG---ALADR--TVVMVTHH 1107
Cdd:COG1129 167 PTASLTERE----VERLFRiirRLKAQgvAIIYISHR 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
921-1106 |
3.19e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.89 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWtggPDVLA--GLDLAARPGDwiVVA--GPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVA-WCPQESH 994
Cdd:COG3845 4 PALELRGITKRF---GGVVAndDVSLTVRPGE--IHAllGENGAGKSTLMKILYGLYQPDSGEILIDGkPVRiRSPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 995 ------------LFDS-TVRGNLAVARDR------DHAPSDAELEAVLARVGLleHVRslpggLDARIGSrgafLSGGQR 1055
Cdd:COG3845 79 algigmvhqhfmLVPNlTVAENIVLGLEPtkggrlDRKAARARIRELSERYGL--DVD-----PDAKVED----LSVGEQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 1056 QRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHgALAD--RTVVMVTH 1106
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILR-RLAAegKSIIFITH 199
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
362-557 |
3.50e-10 |
|
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: 61.47 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 362 VW--YDGAaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--------DGVG------ASVRgsvdgpdpRR 425
Cdd:cd03254 8 VNfsYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDpqkgqiliDGIDirdisrKSLR--------SM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 IAWVPQHPQFSERTVAAELAL---YAGAAGEGAVPGEPGA--LVRELLDQLGLGGLEAADpaELSPGQQRRVAVARGLAR 500
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLgrpNATDEEVIEAAKEAGAhdFIMKLPNGYDTVLGENGG--NLSQGERQLLAIARAMLR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 501 VADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:cd03254 157 DPK---ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVL 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
350-553 |
3.90e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.04 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 350 AAPAgLRVAGLTVWYdgAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSV--------DGP 421
Cdd:PRK14271 18 AAPA-MAAVNLTLGF--AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllggrsifNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 422 D----PRRIAWVPQHPQFSERTVAAELalYAGAAGEGAVP-----GEPGALVRELLDQLGLGGLEAADPAELSPGQQRRV 492
Cdd:PRK14271 95 DvlefRRRVGMLFQRPNPFPMSIMDNV--LAGVRAHKLVPrkefrGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 493 AVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAA-LADR 553
Cdd:PRK14271 173 CLARTLAVNPE---VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAArISDR 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
919-1110 |
3.91e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.62 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 919 RGPGITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSA-AVAGPVAWCPQESHLF- 996
Cdd:PRK11247 9 QGTPLLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlAGTAPLAEAREDTRLMf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 997 -DS------TVRGNLAVARDRDHAPsdAELEAvLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAE 1069
Cdd:PRK11247 88 qDArllpwkKVIDNVGLGLKGQWRD--AALQA-LAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1001866046 1070 VVLLDEPTAHLDPESGL---ALVAAL---HGAladrTVVMVTHHATE 1110
Cdd:PRK11247 154 LLLLDEPLGALDALTRIemqDLIESLwqqHGF----TVLLVTHDVSE 196
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
938-1106 |
4.15e-10 |
|
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: 60.84 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCPQESH-----LFDS-------TVRGNL 1004
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrlgfVSDStglydrlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1005 AVArDRDHAPSDAELEAVLARVGLLEHVRSLpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPES 1084
Cdd:cd03266 100 EYF-AGLYGLKGDELTARLEELADRLGMEEL---LDRRVGG----FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180
....*....|....*....|...
gi 1001866046 1085 GLALVAAL-HGALADRTVVMVTH 1106
Cdd:cd03266 172 TRALREFIrQLRALGKCILFSTH 194
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
922-1112 |
4.43e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.94 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 922 GITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPV--------------- 986
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelepadrdiamvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 987 ---AWCPqesHLfdsTVRGNLA------------VARDRDHAPSDAELEAVLARvgllehvrslpggldarigsRGAFLS 1051
Cdd:PRK11650 83 qnyALYP---HM---SVRENMAyglkirgmpkaeIEERVAEAARILELEPLLDR--------------------KPRELS 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 1052 GGQRQRLAVARTLLAGAEVVLLDEPTAHLDPesglALVAA-------LHGALAdRTVVMVTHHATELM 1112
Cdd:PRK11650 137 GGQRQRVAMGRAIVREPAVFLFDEPLSNLDA----KLRVQmrleiqrLHRRLK-TTSLYVTHDQVEAM 199
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
139-302 |
4.52e-10 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 62.02 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 139 LYTQYLPALVQTAVLplLVGarILGA----DWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQG 214
Cdd:cd18544 114 LFTSGLVTLIGDLLL--LIG--ILIAmfllNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 215 LPVLVGLGRAAEQRRALGELSRAYKGRTMATLRVAFLSALALELISTISVAVVAVFIGIRLVHGDMTLeaGLL-ALI-LA 292
Cdd:cd18544 190 MSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTL--GVLyAFIqYI 267
|
170
....*....|
gi 1001866046 293 PECFQPLRDL 302
Cdd:cd18544 268 QRFFRPIRDL 277
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
938-1106 |
5.13e-10 |
|
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: 60.37 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVG---------SAAVAGPVAWCPQESHLF-DSTVRGNLA-V 1006
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGevlfdgkplDIAARNRIGYLPEERGLYpKMKVIDQLVyL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1007 ARDRDHAPSDA--ELEAVLARVGLLEHvrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPES 1084
Cdd:cd03269 95 AQLKGLKKEEArrRIDEWLERLELSEY-------ANKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180
....*....|....*....|....
gi 1001866046 1085 GLALVAALHgALAD--RTVVMVTH 1106
Cdd:cd03269 164 VELLKDVIR-ELARagKTVILSTH 186
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
355-554 |
5.15e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.33 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEPAVGPLDFTaPAGrVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVD--GPD---PR----- 424
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFY-PNE-ITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVynGHNiysPRtdtvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 425 ---RIAWVPQHPQ---FS--ERTVaaeLALYAGAAGEGAVPGEpgalVRELLDQLGLGGLEAAD-----PAELSPGQQRR 491
Cdd:PRK14239 84 lrkEIGMVFQQPNpfpMSiyENVV---YGLRLKGIKDKQVLDE----AVEKSLKGASIWDEVKDrlhdsALGLSGGQQQR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 492 VAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAA-LADRT 554
Cdd:PRK14239 157 VCIARVLATSPK---IILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASrISDRT 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
954-1110 |
5.52e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.22 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 954 VAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESHLFDS--------------------TVRGNLAVARdRDHA 1013
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnpfphlSIYDNIAYPL-KSHG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1014 PSDAE-----LEAVLARVGLLEHVRSlpggldaRIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLAL 1088
Cdd:PRK14246 120 IKEKReikkiVEECLRKVGLWKEVYD-------RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAI 192
|
170 180
....*....|....*....|..
gi 1001866046 1089 VAALHGALADRTVVMVTHHATE 1110
Cdd:PRK14246 193 EKLITELKNEIAIVIVSHNPQQ 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
993-1125 |
6.13e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 993 SHLFDSTVRGNLAVARDRDHAPSDAELEAVLARVGLLEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVL 1072
Cdd:PTZ00265 523 NDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILI 602
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 1073 LDEPTAHLDPESGLAL---VAALHGAlADRTVVMVTHHATELMPGDTLVRLGARER 1125
Cdd:PTZ00265 603 LDEATSSLDNKSEYLVqktINNLKGN-ENRITIIIAHRLSTIRYANTIFVLSNRER 657
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
923-1106 |
6.51e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.40 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCPQ---------- 991
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkPIDYSRKglmklresvg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 992 ------ESHLFDSTVRGNLAVARDRDHAPSDA---ELEAVLARVGLlEHVRSLPGgldarigsrgAFLSGGQRQRLAVAR 1062
Cdd:PRK13636 86 mvfqdpDNQLFSASVYQDVSFGAVNLKLPEDEvrkRVDNALKRTGI-EHLKDKPT----------HCLSFGQKKRVAIAG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1001866046 1063 TLLAGAEVVLLDEPTAHLDPEsGLALVAALHGALA---DRTVVMVTH 1106
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPM-GVSEIMKLLVEMQkelGLTIIIATH 200
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
2-534 |
6.58e-10 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 63.74 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 2 KPDIPLGPTSRRALVLLGVLAAAKAVGLALVAQGVasglaaLAAGAVRPGVLSAATLVAAAGVLLRAAAEWGTSTVGRWA 81
Cdd:COG3321 860 RVPLPTYPFQREDAAAALLAAALAAALAAAAALGA------LLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 82 AVGVKEELRSQLLEAALEGGAAPASAAGPVDDGAARVASSPAATAVLAGRGLDGLDALYTQYLPALVQTAVLPLLVGARI 161
Cdd:COG3321 934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 162 LGADWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKGR 241
Cdd:COG3321 1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 242 TMATLRVAFLSALALELISTISVAVVAVFIGIRLVHGDMTLEAGLLALILAPECFQPLRDLGTAHHASEDGAEALRRTRA 321
Cdd:COG3321 1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 322 RIGAPRGTVLLAAGHGRVQDAERPPAGQAAPAGLRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAA 401
Cdd:COG3321 1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 402 LAGLVRDGVGASVRGSVDGPDPRRIAWVPQHPQFSERTVAAELALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADP 481
Cdd:COG3321 1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 482 AELSPGQQRRVAVARGLARVADGAGLLLLDEPTAHLDDASAALVERAIAALAG 534
Cdd:COG3321 1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
935-1106 |
6.88e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 61.29 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 935 GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQE---------------SHLFDST 999
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkwvrskvglvfqdpdDQVFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1000 VRGNLA---VARDRDHAPSDAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAEVVLLDEP 1076
Cdd:PRK13647 97 VWDDVAfgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190
....*....|....*....|....*....|...
gi 1001866046 1077 TAHLDP---ESGLALVAALHGalADRTVVMVTH 1106
Cdd:PRK13647 166 MAYLDPrgqETLMEILDRLHN--QGKTVIVATH 196
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
938-1105 |
8.28e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.97 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGflapRVGSAAVAGPV---------------AWCPQESHLFDS-TVR 1001
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG----RIQGNNFTGTIlannrkptkqilkrtGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 GNL---AVARDRDHAPSDAEL---EAVLARVGLLEHVRSLPGglDARIgsRGafLSGGQRQRLAVARTLLAGAEVVLLDE 1075
Cdd:PLN03211 159 ETLvfcSLLRLPKSLTKQEKIlvaESVISELGLTKCENTIIG--NSFI--RG--ISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|
gi 1001866046 1076 PTAHLDPESGLALVAALhGALADRTVVMVT 1105
Cdd:PLN03211 233 PTSGLDATAAYRLVLTL-GSLAQKGKTIVT 261
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
382-555 |
8.57e-10 |
|
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: 60.50 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 382 GRVTVLAGPSGSGKTTVLAALAGLVRDGVGASvrgSVDGPDprrIAWVPQHPQfSERTVAAELALYAGAAGEGAVPgepg 461
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDT---VSYKPQYIK-ADYEGTVRDLLSSITKDFYTHP---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 462 alvrelldqlgLGGLEAADP-----------AELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIA 530
Cdd:cd03237 94 -----------YFKTEIAKPlqieqildrevPELSGGELQRVAIAACLSKDAD---IYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180
....*....|....*....|....*...
gi 1001866046 531 --ALAGRVTVLLVSHEPRTAA-LADRTV 555
Cdd:cd03237 160 rfAENNEKTAFVVEHDIIMIDyLADRLI 187
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
325-543 |
9.60e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.77 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 325 APRGTVLLAA--GHGRVQDAERPPAGQAAPAGLRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAAL 402
Cdd:PRK13536 10 APRRLELSPIerKHQGISEAKASIPGSMSTVAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 403 AGLVRDGVGA-SVRGSvdgPDP-------RRIAWVPQHPQFS-ERTVAAELALYAGAAGEGAVPGEpgALVRELLDQLGL 473
Cdd:PRK13536 88 LGMTSPDAGKiTVLGV---PVPararlarARIGVVPQFDNLDlEFTVRENLLVFGRYFGMSTREIE--AVIPSLLEFARL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 474 GGLEAADPAELSPGQQRRVAVARGLarvADGAGLLLLDEPTAHLDDASAALV-ERAIAALAGRVTVLLVSH 543
Cdd:PRK13536 163 ESKADARVSDLSGGMKRRLTLARAL---INDPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTH 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
954-1106 |
9.83e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.40 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 954 VAGPSGSGKSTLLALLTGFLAPRVGSAAV-----------AGPVAWCPQ--------------------ESHLFDSTVRG 1002
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnHELITNPYSkkiknfkelrrrvsmvfqfpEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1003 -------NLAVARDRDHAPSDAELEAVlarvgllehvrslpgGLDARIGSRGAF-LSGGQRQRLAVARTLLAGAEVVLLD 1074
Cdd:PRK13631 137 dimfgpvALGVKKSEAKKLAKFYLNKM---------------GLDDSYLERSPFgLSGGQKRRVAIAGILAIQPEILIFD 201
|
170 180 190
....*....|....*....|....*....|...
gi 1001866046 1075 EPTAHLDPESGLALVAALHGALAD-RTVVMVTH 1106
Cdd:PRK13631 202 EPTAGLDPKGEHEMMQLILDAKANnKTVFVITH 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
354-553 |
1.32e-09 |
|
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: 62.72 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 354 GLRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVD---GPDPRR--IAW 428
Cdd:TIGR01257 928 GVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDietNLDAVRqsLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 429 VPQHP-QFSERTVAAELALYAGAAGEGAvpgEPGALVRELLDQLGLGGLEAADPA-ELSPGQQRRVAVArgLARVADgAG 506
Cdd:TIGR01257 1008 CPQHNiLFHHLTVAEHILFYAQLKGRSW---EEAQLEMEAMLEDTGLHHKRNEEAqDLSGGMQRKLSVA--IAFVGD-AK 1081
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 507 LLLLDEPTAHLDDASaalvERAIAAL-----AGRVTVLLVSHEPRTAALADR 553
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYS----RRSIWDLllkyrSGRTIIMSTHHMDEADLLGDR 1129
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
923-1106 |
1.43e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.97 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVT-VGWTGGPDVLA--GLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG--------------- 984
Cdd:PRK11153 2 IELKNISkVFPQGGRTIHAlnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalsekelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 985 -PVAWCPQESHLFDS-TVRGNLAVARDRDHAPS---DAELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLA 1059
Cdd:PRK11153 82 rQIGMIFQHFNLLSSrTVFDNVALPLELAGTPKaeiKARVTELLELVGLSDKADRYP-----------AQLSGGQKQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1060 VARTLLAGAEVVLLDEPTAHLDPE---SGLALVAALHGALaDRTVVMVTH 1106
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPAttrSILELLKDINREL-GLTIVLITH 199
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
942-1106 |
1.54e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 942 LDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAV--------------------AGPVAWCPqESHLFDSTVR 1001
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditithktkdkyirpvrkrIGMVFQFP-ESQLFEDTVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 gnlavaRDRDHAPSD--AELEAVLARV-GLLehvrsLPGGLDARIGSRGAF-LSGGQRQRLAVARTLLAGAEVVLLDEPT 1077
Cdd:PRK13646 105 ------REIIFGPKNfkMNLDEVKNYAhRLL-----MDLGFSRDVMSQSPFqMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190
....*....|....*....|....*....|.
gi 1001866046 1078 AHLDPESGLALVAALHGALAD--RTVVMVTH 1106
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDenKTIILVSH 204
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
24-592 |
1.64e-09 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 62.58 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 24 AKAVGLALVAQGVASGLAALAAGAVRPGVLSAATLVAA------AGVLLRAAAEWGTSTVGR------------WAAVGV 85
Cdd:COG3321 799 PGPVLTGLVRQCLAAAGDAVVLPSLRRGEDELAQLLTAlaqlwvAGVPVDWSALYPGRGRRRvplptypfqredAAAALL 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 86 KEELRSQLLEAALEGGAAPASAAGPVDDGAARVASSPAATAVLAGRGLDGLDALYTQYLPALVQTAVLPLLVGARILGAD 165
Cdd:COG3321 879 AAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAA 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 166 WVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKGRTMAT 245
Cdd:COG3321 959 AEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAA 1038
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 246 LRVAFLSALALELISTISVAVVAVFIGIRLVHGDMTLEAGLLALILAPECFQPLRDLGTAHHASEDGAEALRRTRARIGA 325
Cdd:COG3321 1039 AAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALA 1118
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 326 PRGTVLLAAGHGRVQDAERPPAGQAAPAGLRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGL 405
Cdd:COG3321 1119 AAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLA 1198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 406 VRDGVGASVRGSVDGPDPRRIAWVPQHPQFSERTVAAELALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELS 485
Cdd:COG3321 1199 ALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAA 1278
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 486 PGQQRRVAVARGLARVADGAGLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALADRTVELAPSSSAAS 565
Cdd:COG3321 1279 AAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAA 1358
|
570 580
....*....|....*....|....*..
gi 1001866046 566 ARFRADVPDAPAADRGVPAPAAVRRGA 592
Cdd:COG3321 1359 AAAALAAAAGAAAAAAALALAALAAAV 1385
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
938-1112 |
1.64e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.02 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSaavagpVAWcpqESHLFDSTVRGNLA-------VARDR 1010
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGA------VLW---QGKPLDYSKRGLLAlrqqvatVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1011 D----HAPSDAELEAVLARVGLLEH--VRSLPGGL---DARIGSRGAF--LSGGQRQRLAVARTLLAGAEVVLLDEPTAH 1079
Cdd:PRK13638 87 EqqifYTDIDSDIAFSLRNLGVPEAeiTRRVDEALtlvDAQHFRHQPIqcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190
....*....|....*....|....*....|...
gi 1001866046 1080 LDPESGLALVAALHGALADRTVVMVTHHATELM 1112
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLI 199
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
949-1115 |
1.83e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.13 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 949 GDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAwcpQESHLFD------------------STVRGNLAVARDR 1010
Cdd:PRK13650 33 GEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDirhkigmvfqnpdnqfvgATVEDDVAFGLEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1011 DHAPSDAELEAV---LARVGLLEHVRSLPggldARigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLA 1087
Cdd:PRK13650 110 KGIPHEEMKERVneaLELVGMQDFKEREP----AR-------LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190
....*....|....*....|....*....|
gi 1001866046 1088 LVAALHGALADR--TVVMVTHHATELMPGD 1115
Cdd:PRK13650 179 LIKTIKGIRDDYqmTVISITHDLDEVALSD 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
380-544 |
1.89e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 380 PAGRVTVLaGPSGSGKTTVLAALAGLVRDGVGASVrgsvdgPDP-RRIAWVPQHPQFSE-RTV-------AAEL------ 444
Cdd:TIGR03719 30 PGAKIGVL-GLNGAGKSTLLRIMAGVDKDFNGEAR------PQPgIKVGYLPQEPQLDPtKTVrenveegVAEIkdaldr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 445 --ALYAGAAGEGAvpgEPGALVRELLDQLGL--------------GGLEA-------ADPAELSPGQQRRVAVARGLARV 501
Cdd:TIGR03719 103 fnEISAKYAEPDA---DFDKLAAEQAELQEIidaadawdldsqleIAMDAlrcppwdADVTKLSGGERRRVALCRLLLSK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1001866046 502 ADgagLLLLDEPTAHLDDASAALVERAIAALAGrvTVLLVSHE 544
Cdd:TIGR03719 180 PD---MLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTHD 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
355-544 |
3.01e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.09 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEP--AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--DGvgaSVRgsVDGPD-------- 422
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERptSG---SVL--VDGVDltalsere 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 423 ----PRRIAWVPQHPQ-FSERTVAAELAL---YAGAAGEgavpgEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAV 494
Cdd:COG1135 77 lraaRRKIGMIFQHFNlLSSRTVAENVALpleIAGVPKA-----EIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 495 ARGLarvADGAGLLLLDEPTAHLDDASAalveRAIAALAGRV------TVLLVSHE 544
Cdd:COG1135 152 ARAL---ANNPKVLLCDEATSALDPETT----RSILDLLKDInrelglTIVLITHE 200
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
371-555 |
3.03e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 59.68 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 371 AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGPDP--------RRIAWVPQHP--QFSERTV 440
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvklsdirKKVGLVFQYPeyQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 441 AAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAAD--PAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLD 518
Cdd:PRK13637 102 EKDIAF--GPINLGLSEEEIENRVKRAMNIVGLDYEDYKDksPFELSGGQKRRVAIAGVVAMEPK---ILILDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1001866046 519 DASAALVERAIAALAGR--VTVLLVSHEPR-TAALADRTV 555
Cdd:PRK13637 177 PKGRDEILNKIKELHKEynMTIILVSHSMEdVAKLADRII 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
355-518 |
3.03e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.94 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGS--VDGPDPRRIAWVPQH 432
Cdd:PRK11248 2 LQISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpVEGPGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 433 PQFSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLArvADgAGLLLLDE 512
Cdd:PRK11248 80 GLLPWRNVQDNVAF--GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALA--AN-PQLLLLDE 154
|
....*.
gi 1001866046 513 PTAHLD 518
Cdd:PRK11248 155 PFGALD 160
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-549 |
3.27e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 347 AGQAAPAGLRVAGLTVWYDGAAepAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR-DGVGASVRGSV--DGPDP 423
Cdd:PRK14246 3 AGKSAEDVFNISRLYLYINDKA--ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVlyFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 424 RRIAWVPQHPQ----FSERTVAAELALYAGAA----GEGAVPGEPGALVRELLDQLGLGGLEAAD----PA-ELSPGQQR 490
Cdd:PRK14246 81 FQIDAIKLRKEvgmvFQQPNPFPHLSIYDNIAyplkSHGIKEKREIKKIVEECLRKVGLWKEVYDrlnsPAsQLSGGQQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 491 RVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAA 549
Cdd:PRK14246 161 RLTIARALALKPK---VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVA 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
941-1082 |
3.35e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.85 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 941 GLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCP-------------QESHLFDS-TVRGNLA 1005
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGqHIEGLPghqiarmgvvrtfQHVRLFREmTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1006 VARDRdHAPSD-------------AELEAV------LARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLA 1066
Cdd:PRK11300 103 VAQHQ-QLKTGlfsgllktpafrrAESEALdraatwLERVGLLEHANRQAGNL-----------AYGQQRRLEIARCMVT 170
|
170
....*....|....*.
gi 1001866046 1067 GAEVVLLDEPTAHLDP 1082
Cdd:PRK11300 171 QPEILMLDEPAAGLNP 186
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
923-1127 |
3.93e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 58.70 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGwtggpDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGfLAPRVGSAAVAG-PVAWCP----------- 990
Cdd:COG4138 1 LQLNDVAVA-----GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGrPLSDWSaaelarhrayl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 --QESHLFDSTVRGNLAVardrdHAPSDAELEAVLARVGLLehVRSLpgGLDARIGSRGAFLSGGQRQRLAVARTLL--- 1065
Cdd:COG4138 75 sqQQSPPFAMPVFQYLAL-----HQPAGASSEAVEQLLAQL--AEAL--GLEDKLSRPLTQLSGGEWQRVRLAAVLLqvw 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1066 ----AGAEVVLLDEPTAHLDpesgLALVAALHG-----ALADRTVVMVTH-------HATE--LMPGDTLVRLGARERVL 1127
Cdd:COG4138 146 ptinPEGQLLLLDEPMNSLD----VAQQAALDRllrelCQQGITVVMSSHdlnhtlrHADRvwLLKQGKLVASGETAEVM 221
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
627-736 |
4.72e-09 |
|
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: 59.03 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 627 TLSGWLIVRASEQPPILY---LLTAITGVRFFGIARAVLRYRERLVLHSAVLSTLTELRERLW---ALLSVRGLSARRll 700
Cdd:cd18585 13 ALSGWFISAAALAGLAAPtfnYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYrklEPLAPARLQKYR-- 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 1001866046 701 vPGAALEALVGDAEAVRDQLPRVLAPITTAVLVAAG 736
Cdd:cd18585 91 -SGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILA 125
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
953-1107 |
5.05e-09 |
|
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: 57.62 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 953 VVAGPSGSGKSTLL-AL---LTGFLAPRvgsaavagpvawcpqeshlfdstvrgnlavARDRDHAPSDAELEAVLARVGL 1028
Cdd:cd03240 26 LIVGQNGAGKTTIIeALkyaLTGELPPN------------------------------SKGGAHDPKLIREGEVRAQVKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1029 -LEH--------VRSLP----------GGLDARIGSRGAFLSGGQRQ------RLAVARTLLAGAEVVLLDEPTAHLDPE 1083
Cdd:cd03240 76 aFENangkkytiTRSLAilenvifchqGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE 155
|
170 180
....*....|....*....|....*..
gi 1001866046 1084 S---GLALVAALHGALADRTVVMVTHH 1107
Cdd:cd03240 156 NieeSLAEIIEERKSQKNFQLIVITHD 182
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
938-1103 |
5.51e-09 |
|
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: 58.91 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRvgsAAVAGPVAWCPQEshLFD------STVRGN-------- 1003
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPP---GITSGEILFDGED--LLKlsekelRKIRGReiqmifqd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1004 ------------------LAVARDRDHAPSDAELEAVLARVGL---LEHVRSLPGGLdarigsrgaflSGGQRQRLAVAR 1062
Cdd:COG0444 95 pmtslnpvmtvgdqiaepLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHEL-----------SGGMRQRVMIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1063 TLLAGAEVVLLDEPTAHLDP---------------ESGLALV-----AALHGALADRTVVM 1103
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVtiqaqilnllkdlqrELGLAILfithdLGVVAEIADRVAVM 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
359-553 |
6.29e-09 |
|
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: 57.50 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 359 GLTVWYDGAAEPAVGPLDFTAPAG-RVTVLaGPSGSGKTTVLAALAGLVrDGVGASVRgsVDGPDP---------RRIAW 428
Cdd:cd03244 7 NVSLRYRPNLPPVLKNISFSIKPGeKVGIV-GRTGSGKSSLLLALFRLV-ELSSGSIL--IDGVDIskiglhdlrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 429 VPQHPQFSERTVAAEL-------------ALyAGAAGEGAVPGEPGALvrelldqlglGGLEAADPAELSPGQQRRVAVA 495
Cdd:cd03244 83 IPQDPVLFSGTIRSNLdpfgeysdeelwqAL-ERVGLKEFVESLPGGL----------DTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 496 RGLARvadGAGLLLLDEPTAHLDDASAALVERAI-AALAGRvTVLLVSHEPRTAALADR 553
Cdd:cd03244 152 RALLR---KSKILVLDEATASVDPETDALIQKTIrEAFKDC-TVLTIAHRLDTIIDSDR 206
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
921-1081 |
6.31e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 56.67 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVgwtggPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGpvawcpQESHLFDSTV 1000
Cdd:cd03215 3 PVLEVRGLSV-----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG------KPVTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 RGNLAVArdrdHAPSDAELEAVLARVGLLEHVrslpggldarigSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHL 1080
Cdd:cd03215 72 AIRAGIA----YVPEDRKREGLVLDLSVAENI------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
.
gi 1001866046 1081 D 1081
Cdd:cd03215 136 D 136
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
938-1107 |
6.81e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.12 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGfLAPRVGSAAVAGPVAWCPQ---------------------ESHLF 996
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGRVEFFNQniyerrvnlnrlrrqvsmvhpKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 997 DSTVRGNLAVARD----RDHAPSDAELEAVLARVGLLEHVRSlpggldaRIGSRGAFLSGGQRQRLAVARTLLAGAEVVL 1072
Cdd:PRK14258 101 PMSVYDNVAYGVKivgwRPKLEIDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1001866046 1073 LDEPTAHLDPESGLALVAALHGAL--ADRTVVMVTHH 1107
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHN 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
952-1092 |
7.30e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 952 IV-VAGPSGSGKSTLLALLTGFLAPRVGSAAVAgpvawcpqeshlfdSTVRgnLA-VARDRDH-APSDAELEAVlarvgl 1028
Cdd:PRK11819 352 IVgIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--------------ETVK--LAyVDQSRDAlDPNKTVWEEI------ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1029 lehvrslPGGLDA-RIG-----SR---GAF-------------LSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGL 1086
Cdd:PRK11819 410 -------SGGLDIiKVGnreipSRayvGRFnfkggdqqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLR 482
|
....*.
gi 1001866046 1087 ALVAAL 1092
Cdd:PRK11819 483 ALEEAL 488
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
382-545 |
9.34e-09 |
|
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: 56.48 E-value: 9.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 382 GRVTVLAGPSGSGKTTVLAALAGLVRDGVgasVRGS--VDGPD-----PRRIAWVPQHPQFsertvaaelalyagaageg 454
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAGV---ITGEilINGRPldknfQRSTGYVEQQDVH------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 455 avpgEPGALVRELLDQlglggleAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALA- 533
Cdd:cd03232 91 ----SPNLTVREALRF-------SALLRGLSVEQRKRLTIGVELAAKPS---ILFLDEPTSGLDSQAAYNIVRFLKKLAd 156
|
170
....*....|...
gi 1001866046 534 -GRvTVLLVSHEP 545
Cdd:cd03232 157 sGQ-AILCTIHQP 168
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
355-557 |
9.65e-09 |
|
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: 56.91 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYdgAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRGSVDGPDPR-RIAWVPQh 432
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEvLFDGKPLDIAARnRIGYLPE- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 433 pqfsER------TVAAELALYAGAAGEGavPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVArglARVADGAG 506
Cdd:cd03269 78 ----ERglypkmKVIDQLVYLAQLKGLK--KEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFI---AAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 507 LLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHEPRTA-ALADRTVEL 557
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVeELCDRVLLL 201
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
948-1081 |
1.00e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.41 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 948 PGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG--PVAWCPQESHLFDSTVRgNLAVARDRDHAPSDAELEAVLAR 1025
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQETPALPQPAL-EYVIDGDREYRQLEAQLHDANER 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 1026 vGLLEHVRSLPGGLDA----RIGSRGAFL------------------SGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:PRK10636 105 -NDGHAIATIHGKLDAidawTIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
481-602 |
1.09e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.35 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 481 PAELSPGQQRRVAVARGLarvADGAGLLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHEPRTAALADRTVELAP 559
Cdd:PRK10535 142 PSQLSGGQQQRVSIARAL---MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRD 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 560 SSSAASARFRADVPDAPAADRGVPAPAAVRR----------GAWL-------RTLASLLG 602
Cdd:PRK10535 219 GEIVRNPPAQEKVNVAGGTEPVVNTASGWRQfvsgfrealtMAWRamaankmRTLLTMLG 278
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
921-1082 |
1.11e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWTGGPdVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVA------------ 987
Cdd:PRK15439 10 PLLCARSISKQYSGVE-VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnPCArltpakahqlgi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 988 -WCPQESHLFDS-TVRGNLAVARDRdHAPSDAELEAVLARVGLlehvrSLpgGLDARIGSrgafLSGGQRQRLAVARTLL 1065
Cdd:PRK15439 89 yLVPQEPLLFPNlSVKENILFGLPK-RQASMQKMKQLLAALGC-----QL--DLDSSAGS----LEVADRQIVEILRGLM 156
|
170
....*....|....*..
gi 1001866046 1066 AGAEVVLLDEPTAHLDP 1082
Cdd:PRK15439 157 RDSRILILDEPTASLTP 173
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
165-306 |
1.14e-08 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 57.82 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 165 DWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKGRTMA 244
Cdd:cd18552 138 DWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMK 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 245 TLRVAFLSALALELISTISVAVVAVFIGIRLVHGDMTLE---AGLLALILApecFQPLRDLGTAH 306
Cdd:cd18552 218 IARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGefiSFITALLLL---YQPIKRLSNVN 279
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
376-555 |
1.31e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 376 DFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRG-SVDGPDPRR-----IAWVPQHPQ-FSERTVAAELALy 447
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEiLLDGePVRFRSPRDaqaagIAIIHQELNlVPNLSVAENIFL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 448 agaageGAVPGEPGAL----VRELLDQLGLGGLEAADP----AELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDD 519
Cdd:COG1129 103 ------GREPRRGGLIdwraMRRRARELLARLGLDIDPdtpvGDLSVAQQQLVEIARALSR---DARVLILDEPTASLTE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1001866046 520 ASAALVERAIAALAGR-VTVLLVSH---EprTAALADR-TV 555
Cdd:COG1129 174 REVERLFRIIRRLKAQgVAIIYISHrldE--VFEIADRvTV 212
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
954-1112 |
1.48e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.33 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 954 VAGPSGSGKSTLLALLTGFLAPRVGSAAVA---------------------GPVAWCPqESHLFDSTVRGNLAVArdrdh 1012
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipanlkkikevkrlrkeiGLVFQFP-EYQLFQETIEKDIAFG----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1013 aPSD--AELEAVLARVGLLEHVRSLPggldARIGSRGAF-LSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP---ESGL 1086
Cdd:PRK13645 116 -PVNlgENKQEAYKKVPELLKLVQLP----EDYVKRSPFeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeEDFI 190
|
170 180
....*....|....*....|....*.
gi 1001866046 1087 ALVAALHGALADRtVVMVTHHATELM 1112
Cdd:PRK13645 191 NLFERLNKEYKKR-IIMVTHNMDQVL 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
939-1127 |
1.58e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.86 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 939 LAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLaPRVGSAAVAGPV-------------AW-CPQESHLFDSTVRGNL 1004
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPleawsaaelarhrAYlSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1005 AVardrdHAPSDAELEAVLARVGLLehVRSLpgGLDARIGSRGAFLSGG--QRQRLA-----VARTLLAGAEVVLLDEPT 1077
Cdd:PRK03695 91 TL-----HQPDKTRTEAVASALNEV--AEAL--GLDDKLGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 1078 AHLDpesgLALVAAL-----HGALADRTVVMVTH-------HATE--LMPGDTLVRLGARERVL 1127
Cdd:PRK03695 162 NSLD----VAQQAALdrllsELCQQGIAVVMSSHdlnhtlrHADRvwLLKQGKLLASGRRDEVL 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
380-555 |
1.64e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.79 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 380 PAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDGPD-------PRRIAWVPQH-PQFSERTVAAELALyagaa 451
Cdd:PRK10851 26 PSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG---HIRFHGTDvsrlharDRKVGFVFQHyALFRHMTVFDNIAF----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 452 GEGAVP--GEPGALVRELLDQLGLGGLEAAD-----PAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAAL 524
Cdd:PRK10851 98 GLTVLPrrERPNAAAIKAKVTQLLEMVQLAHladryPAQLSGGQKQRVALARALAVEPQ---ILLLDEPFGALDAQVRKE 174
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 525 VERAIAALAG--RVTVLLVSHEPRTAA-LADRTV 555
Cdd:PRK10851 175 LRRWLRQLHEelKFTSVFVTHDQEEAMeVADRVV 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
921-1118 |
1.68e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 56.92 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWTGG-PDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAwcpQESHLFD-- 997
Cdd:PRK13632 6 VMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 998 ----------------STVRGNLAVARDRDHAPSD---AELEAVLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRL 1058
Cdd:PRK13632 83 kkigiifqnpdnqfigATVEDDIAFGLENKKVPPKkmkDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 1059 AVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHG--ALADRTVVMVTHHATELMPGDTLV 1118
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVI 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
947-1106 |
1.81e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 947 RPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSaaVAGPVAW----------------------------CPQESHL--- 995
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPSWdevlkrfrgtelqnyfkklyngeikvvhKPQYVDLipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 996 -FDSTVRGNLAVARDRDhapsdaELEAVLARVGLlEHVrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLD 1074
Cdd:PRK13409 175 vFKGKVRELLKKVDERG------KLDEVVERLGL-ENI------LDRDISE----LSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|..
gi 1001866046 1075 EPTAHLDPESGLALVAALHGALADRTVVMVTH 1106
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
368-543 |
1.97e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 368 AEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVD----------GPDPRRIAWVPQHP--QF 435
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeiKPVRKKVGVVFQFPesQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 436 SERTVAAELALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAAdPAELSPGQQRRVAVARGLARVADgagLLLLDEPTA 515
Cdd:PRK13643 98 FEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKS-PFELSGGQMRRVAIAGILAMEPE---VLVLDEPTA 173
|
170 180 190
....*....|....*....|....*....|
gi 1001866046 516 HLDDASAALVERAIAAL--AGRvTVLLVSH 543
Cdd:PRK13643 174 GLDPKARIEMMQLFESIhqSGQ-TVVLVTH 202
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
375-555 |
1.99e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.03 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASvrgSVDGPD---------PRRIAWVPQHP--QFSERTVAAE 443
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV---KIDGELltaenvwnlRRKIGMVFQNPdnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 444 LALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAA 523
Cdd:PRK13642 103 VAF--GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE---IIILDESTSMLDPTGRQ 177
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 524 LVERAIAALAGR--VTVLLVSHEPRTAALADRTV 555
Cdd:PRK13642 178 EIMRVIHEIKEKyqLTVLSITHDLDEAASSDRIL 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
355-543 |
2.05e-08 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 55.69 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVG-ASVRGSVDG---PDPRRIAWVP 430
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGeITFDGKSYQkniEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 431 QHPQF-SERTVAAELALYAgaagegAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLL 509
Cdd:cd03268 79 EAPGFyPNLTARENLRLLA------RLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD---LLI 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1001866046 510 LDEPTAHLDDASAALVERAIAALAGR-VTVLLVSH 543
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQgITVLISSH 184
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
146-282 |
2.64e-08 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 56.65 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 146 ALVQTAVLPLLVGARILGADWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAA 225
Cdd:cd18541 120 YLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEE 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 226 EQRRALGELSRAYKGRTMatlRVAFLSAL---ALELISTISVAVVAVFIGIRLVHGDMTL 282
Cdd:cd18541 200 AEIERFDKLNEEYVEKNL---RLARVDALffpLIGLLIGLSFLIVLWYGGRLVIRGTITL 256
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
915-1110 |
3.27e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 915 DAPGRGPGITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGfLAPRVGSAAVAGPV-------- 986
Cdd:PRK14271 14 DVDAAAPAMAAVNLTLGF-AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNR-MNDKVSGYRYSGDVllggrsif 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 987 ------------AWCPQESHLFDSTVRGN-LAVARDRDHAPSD---AELEAVLARVGLLEHVRSlpggldaRIGSRGAFL 1050
Cdd:PRK14271 92 nyrdvlefrrrvGMLFQRPNPFPMSIMDNvLAGVRAHKLVPRKefrGVAQARLTEVGLWDAVKD-------RLSDSPFRL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1051 SGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHgALADR-TVVMVTHHATE 1110
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR-SLADRlTVIIVTHNLAQ 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
956-1107 |
3.94e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.96 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 956 GPSGSGKSTLLALLTGFLAPRVGSAAVAGPVA---WCPQESHL----FDSTVRGNLAVARD--RDHAPSDAELEAV-LAR 1025
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdLCTYQKQLcfvgHRSGINPYLTLRENclYDIHFSPGAVGITeLCR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1026 VGLLEHVRSLPGGLdarigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMVT 1105
Cdd:PRK13540 114 LFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLT 183
|
..
gi 1001866046 1106 HH 1107
Cdd:PRK13540 184 SH 185
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
377-544 |
4.03e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.41 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 377 FTAPAGRVTVLAGPSGSGKTTVLAALAGLvrdgvgasvrgsvDGPDPRRIAWVPQHPQFSERTVAAELALYAGAAG---- 452
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRVLNLL-------------EMPRSGTLNIAGNHFDFSKTPSDKAIRELRRNVGmvfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 453 ---------------EGAVP----GEPGALVRELLDQLGLGGLEAAD--PAELSPGQQRRVAVARGLARVADgagLLLLD 511
Cdd:PRK11124 90 qynlwphltvqqnliEAPCRvlglSKDQALARAEKLLERLRLKPYADrfPLHLSGGQQQRVAIARALMMEPQ---VLLFD 166
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 512 EPTAHLDDASAALVERAIAALAGR-VTVLLVSHE 544
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAETgITQVIVTHE 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
949-1106 |
4.81e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 949 GDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP--VAWCPQESHLFD--STVRGNLAvardrdhapsDAELEAVLA 1024
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKleVAYFDQHRAELDpeKTVMDNLA----------EGKQEVMVN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1025 rvGLLEHVRS-----LPGGLDARIGSRGafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESgLALVAALhgaLADR 1099
Cdd:PRK11147 415 --GRPRHVLGylqdfLFHPKRAMTPVKA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET-LELLEEL---LDSY 486
|
....*....
gi 1001866046 1100 --TVVMVTH 1106
Cdd:PRK11147 487 qgTVLLVSH 495
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
923-1112 |
5.97e-08 |
|
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: 56.73 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQ----ESHLFDS 998
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEKcgyvERPSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 T---VRGNLAVARDRDH-APSDAELEAVLARVGL--------------LEHV-RSLP----GGLDA-------------- 1041
Cdd:TIGR03269 80 EpcpVCGGTLEPEEVDFwNLSDKLRRRIRKRIAImlqrtfalygddtvLDNVlEALEeigyEGKEAvgravdliemvqls 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 1042 -RIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRTVVMV-THHATELM 1112
Cdd:TIGR03269 160 hRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVlTSHWPEVI 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
161-543 |
6.11e-08 |
|
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: 57.23 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 161 ILGADWVSAL----ILVLTLPLVPVFMIL------IGRHTLEAVAEAQQSLLrlgSHLVELAQGLPVLVGLGRAA--EQ- 227
Cdd:TIGR01271 1013 VLGAIFVVSVlqpyIFIAAIPVAVIFIMLrayflrTSQQLKQLESEARSPIF---SHLITSLKGLWTIRAFGRQSyfETl 1089
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 228 -RRALgELSRAYKGRTMATLRvAFLsaLALELISTIsVAVVAVFIGIrLVHGDMTLEAGLLaLILApecfqpLRDLGTAH 306
Cdd:TIGR01271 1090 fHKAL-NLHTANWFLYLSTLR-WFQ--MRIDIIFVF-FFIAVTFIAI-GTNQDGEGEVGII-LTLA------MNILSTLQ 1156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 307 HA--SEDGAEALRRTRAR----IGAPRGTVLLAAGHGRVQDA-----ERPPAGQAAPAG--LRVAGLTVWYDGAAEPAVG 373
Cdd:TIGR01271 1157 WAvnSSIDVDGLMRSVSRvfkfIDLPQEEPRPSGGGGKYQLStvlviENPHAQKCWPSGgqMDVQGLTAKYTEAGRAVLQ 1236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 374 PLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLvrdgvgASVRG--SVDGpdprrIAW--------------VPQ------ 431
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL------LSTEGeiQIDG-----VSWnsvtlqtwrkafgvIPQkvfifs 1305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 432 ---------HPQFSER---TVAAELALyagaagEGAVPGEPGALVRELLDQLGLggleaadpaeLSPGQQRRVAVARGla 499
Cdd:TIGR01271 1306 gtfrknldpYEQWSDEeiwKVAEEVGL------KSVIEQFPDKLDFVLVDGGYV----------LSNGHKQLMCLARS-- 1367
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1001866046 500 rVADGAGLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSH 543
Cdd:TIGR01271 1368 -ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
370-555 |
6.26e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 55.38 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 370 PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGPDPRR-------IAWVPQHP--QFSERTV 440
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlqgirklVGIVFQNPetQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 441 AAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDA 520
Cdd:PRK13644 96 EEDLAF--GPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE---CLIFDEVTSMLDPD 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1001866046 521 SAALVERAIAALAGR-VTVLLVSHEPRTAALADRTV 555
Cdd:PRK13644 171 SGIAVLERIKKLHEKgKTIVYITHNLEELHDADRII 206
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
956-1081 |
6.34e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.04 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 956 GPSGSGKSTLLALLTGFLAPRVGSAAVAGPV-------AWCP----------QESHLFDS-TVRGNL--AVARDrdhapS 1015
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgICLPpekrrigyvfQDARLFPHyKVRGNLryGMAKS-----M 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 1016 DAELEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:PRK11144 106 VAQFDKIVALLGIEPLLDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
355-557 |
6.62e-08 |
|
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: 54.34 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDGPD---------PRR 425
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEG---KIEIDGIDistipledlRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 IAWVPQHPQFSERTVAAELALYAGAAGE---GAVPGEPGALvrelldqlglggleaadpaELSPGQQRRVAVARGLARVA 502
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLDPFDEYSDEeiyGALRVSEGGL-------------------NLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 503 DgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:cd03369 145 R---VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVM 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
941-1127 |
6.74e-08 |
|
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: 56.73 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 941 GLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAP-------RVGSAAV----AGP---------VAWCPQESHLF-DST 999
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPtsgevnvRVGDEWVdmtkPGPdgrgrakryIGILHQEYDLYpHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1000 VRGNLAVARDRDHAPSDAELEAV--LARVGLLEH--VRSLPGGLDArigsrgafLSGGQRQRLAVARTLLAGAEVVLLDE 1075
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKAVitLKMVGFDEEkaEEILDKYPDE--------LSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 1076 PTAHLDPESGLALVAALHGALAD--RTVVMVTHHA---------TELMPGDTLVRLGARERVL 1127
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMdfvldvcdrAALMRDGKIVKIGDPEEIV 516
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
938-1106 |
8.67e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.09 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSA----------AVAGPVAWCPQ---------------- 991
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEKVLEklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 992 -------------ESHLFDSTVRGNLAVArDRDHAPSDAELEAVLARVglLEHVrslpgGLDARIGSRGAF-LSGGQRQR 1057
Cdd:PRK13651 102 eirrrvgvvfqfaEYQLFEQTIEKDIIFG-PVSMGVSKEEAKKRAAKY--IELV-----GLDESYLQRSPFeLSGGQKRR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 1058 LAVARTLLAGAEVVLLDEPTAHLDPESG---LALVAALHgaLADRTVVMVTH 1106
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVkeiLEIFDNLN--KQGKTIILVTH 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
355-553 |
9.90e-08 |
|
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: 53.09 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGlvrdgvgasvrgsvdgpdprriAWVPQHpq 434
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG----------------------DLKPQQ-- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 435 fSERTVA-AELALYAGAAGE--GAVPGEP---GALVRELLDqlglggleaadpAELSPGQQRRVAVARGLARVADgagLL 508
Cdd:cd03247 57 -GEITLDgVPVSDLEKALSSliSVLNQRPylfDTTLRNNLG------------RRFSGGERQRLALARILLQDAP---IV 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 509 LLDEPTAHLDdasaALVERAIAALAGRV----TVLLVSHEPRTAALADR 553
Cdd:cd03247 121 LLDEPTVGLD----PITERQLLSLIFEVlkdkTLIWITHHLTGIEHMDK 165
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
370-543 |
1.12e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.75 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 370 PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVD----------GPDPRRIAWVPQHP--QFSE 437
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdiKQIRKKVGLVFQFPesQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 438 RTVAAELALyaGAAGEGAVPGEPGALVRELLDQL-GLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAH 516
Cdd:PRK13649 101 ETVLKDVAF--GPQNFGVSQEEAEALAREKLALVgISESLFEKNPFELSGGQMRRVAIAGILAMEPK---ILVLDEPTAG 175
|
170 180
....*....|....*....|....*...
gi 1001866046 517 LDDASAALVERAIAAL-AGRVTVLLVSH 543
Cdd:PRK13649 176 LDPKGRKELMTLFKKLhQSGMTIVLVTH 203
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
882-1082 |
1.14e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 882 AVQQLPALRSAlvRVAAEEQAVRDAAEERDDLQdAPGRGPG---ITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPS 958
Cdd:PRK10522 282 AVGALPTLLSA--QVAFNKLNKLALAPYKAEFP-RPQAFPDwqtLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGN 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 959 GSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCPQES------------HLFDSTVrgnlavaRDRDHAPSDAELEAVLAR 1025
Cdd:PRK10522 359 GSGKSTLAMLLTGLYQPQSGEILLDGkPVTAEQPEDyrklfsavftdfHLFDQLL-------GPEGKPANPALVEKWLER 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 1026 VGLLEHVRsLPGG--LDARigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:PRK10522 432 LKMAHKLE-LEDGriSNLK-------LSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
947-1107 |
1.15e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.29 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 947 RPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSaaVAGPVAWCPQESHL--------FDSTVRGNLAVARDR---DHAPS 1015
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDWDEILDEFrgselqnyFTKLLEGDVKVIVKPqyvDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1016 --DAELEAVLARV---GLLEHV---RSLPGGLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLA 1087
Cdd:cd03236 102 avKGKVGELLKKKderGKLDELvdqLELRHVLDRNIDQ----LSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180
....*....|....*....|
gi 1001866046 1088 LVAALHGALADRTVVMVTHH 1107
Cdd:cd03236 178 AARLIRELAEDDNYVLVVEH 197
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
952-1127 |
1.33e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 952 IVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPvawcpqeshlfdstvrgnlavarDRDHAPSDAELEAVLarvglleh 1031
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-----------------------EDILEEVLDQLLLII-------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1032 vrslpggldarIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGAL-------ADRTVVMV 1104
Cdd:smart00382 54 -----------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkseKNLTVILT 122
|
170 180
....*....|....*....|...
gi 1001866046 1105 THHATELMPGDTLVRLGARERVL 1127
Cdd:smart00382 123 TNDEKDLGPALLRRRFDRRIVLL 145
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
938-1137 |
1.36e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQE-------SHL----FDSTVRGNLAV 1006
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRsrfmaylGHLpglkADLSTLENLHF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1007 -----ARDRDHAPSDAeleavLARVGLLEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:PRK13543 106 lcglhGRRAKQMPGSA-----LAIVGLAGYEDTLV-----------RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 1082 PEsGLALVAAlhgaladrtvvMVTHHatelmpgdtlVRLGARERVLHHAARAAAPV 1137
Cdd:PRK13543 170 LE-GITLVNR-----------MISAH----------LRGGGAALVTTHGAYAAPPV 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
934-1107 |
1.48e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.91 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVgsaaVAGPVawcpqeshLFDSTVRGNLAVaRDRdha 1013
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEV----TEGEI--------LFKGEDITDLPP-EER--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1014 psdaeleavlARVGL---------------LEHVRSLPGGldarigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTA 1078
Cdd:cd03217 75 ----------ARLGIflafqyppeipgvknADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190
....*....|....*....|....*....|.
gi 1001866046 1079 HLDPESgLALVAALHGALAD--RTVVMVTHH 1107
Cdd:cd03217 134 GLDIDA-LRLVAEVINKLREegKSVLIITHY 163
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
375-544 |
1.62e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 53.48 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGL--VRDGVGASVRGSVD---GPDPRRIAWVPQ-------------HPQFS 436
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLetPDSGQLNIAGHQFDfsqKPSEKAIRLLRQkvgmvfqqynlwpHLTVM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 437 ERTVAAELALyAGAAGEGAVPGEPGALVRelldqlgLGGLEAAD--PAELSPGQQRRVAVARGLARVADgagLLLLDEPT 514
Cdd:COG4161 101 ENLIEAPCKV-LGLSKEQAREKAMKLLAR-------LRLTDKADrfPLHLSGGQQQRVAIARALMMEPQ---VLLFDEPT 169
|
170 180 190
....*....|....*....|....*....|.
gi 1001866046 515 AHLDDASAALVERAIAALAGR-VTVLLVSHE 544
Cdd:COG4161 170 AALDPEITAQVVEIIRELSQTgITQVIVTHE 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
367-553 |
2.08e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.40 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 367 AAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVrDGVGaSVRgsVDGPD---------PRRIAWVPQH--PQF 435
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSG-SIQ--FAGQPleawsaaelARHRAYLSQQqtPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 436 SeRTVAAELALYAGAageGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRV---AVARGLARVADGAG-LLLLD 511
Cdd:PRK03695 83 A-MPVFQYLTLHQPD---KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaAVVLQVWPDINPAGqLLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1001866046 512 EPTAHLDDASAALVERAIAALAGR-VTVLLVSHE-PRTAALADR 553
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQQgIAVVMSSHDlNHTLRHADR 202
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
355-518 |
2.30e-07 |
|
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: 53.90 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEP--AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDgvGASVRGSV--DGPD-------- 422
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPP--PGITSGEIlfDGEDllklseke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 423 -----PRRIAWVPQHPQFS-------ERTVAAELALYAGAAGEGAVpgepgALVRELLDQLG-LGGLEAAD--PAELSPG 487
Cdd:COG0444 80 lrkirGREIQMIFQDPMTSlnpvmtvGDQIAEPLRIHGGLSKAEAR-----ERAIELLERVGlPDPERRLDryPHELSGG 154
|
170 180 190
....*....|....*....|....*....|....
gi 1001866046 488 QQRRVAVARGLA---RvadgagLLLLDEPTAHLD 518
Cdd:COG0444 155 MRQRVMIARALAlepK------LLIADEPTTALD 182
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
956-1106 |
2.40e-07 |
|
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: 54.79 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 956 GPSGSGKSTLLALLTGFLAPRVGSaaVAGPVAWcpQE-------SHLFD---STVRGNLAVARDR---DHAPS--DAELE 1020
Cdd:COG1245 106 GPNGIGKSTALKILSGELKPNLGD--YDEEPSW--DEvlkrfrgTELQDyfkKLANGEIKVAHKPqyvDLIPKvfKGTVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1021 AVLARV---GLLEHVR---SLPGGLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHG 1094
Cdd:COG1245 182 ELLEKVderGKLDELAeklGLENILDRDISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
|
170
....*....|...
gi 1001866046 1095 -ALADRTVVMVTH 1106
Cdd:COG1245 258 lAEEGKYVLVVEH 270
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
375-557 |
2.41e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGV---GASVRGSV--DGP-----DPRRIAW----VPQHPQ----FS 436
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprGARVTGDVtlNGEplaaiDAPRLARlravLPQAAQpafaFS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 437 ERTVAAeLALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARV------ADGAGLLLL 510
Cdd:PRK13547 100 AREIVL-LGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLwpphdaAQPPRYLLL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 511 DEPTAHLDDASAALVERAIAALAG--RVTVLLVSHEPRTAAL-ADRTVEL 557
Cdd:PRK13547 179 DEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARhADRIAML 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
382-543 |
2.46e-07 |
|
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: 54.79 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 382 GRVTVLAGPSGSGKTTVLAALAGLVRDgvgasVRGSVDGPDprRIAWVPQHPQ-FSERTVAAELalyagaagEGAVPGE- 459
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKP-----DEGEVDEDL--KISYKPQYISpDYDGTVEEFL--------RSANTDDf 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 460 PGALVRElldqlglgglEAADP-----------AELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERA 528
Cdd:COG1245 431 GSSYYKT----------EIIKPlgleklldknvKDLSGGELQRVAIAACLSRDAD---LYLLDEPSAHLDVEQRLAVAKA 497
|
170
....*....|....*..
gi 1001866046 529 IAALA--GRVTVLLVSH 543
Cdd:COG1245 498 IRRFAenRGKTAMVVDH 514
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
372-543 |
2.65e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.66 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 372 VGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRG-SVDGPDPR---RIAWVPQ----HPQFserTVAA 442
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSiSLCGePVPSRARHarqRVGVVPQfdnlDPDF---TVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 443 ELALYAGAAGEGAvpGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASA 522
Cdd:PRK13537 100 NLLVFGRYFGLSA--AAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD---VLVLDEPTTGLDPQAR 174
|
170 180
....*....|....*....|..
gi 1001866046 523 ALV-ERAIAALAGRVTVLLVSH 543
Cdd:PRK13537 175 HLMwERLRSLLARGKTILLTTH 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
479-543 |
2.67e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 2.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 479 ADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGrvTVLLVSH 543
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPD---MLLLDEPTNHLDAESVAWLEQFLHDYPG--TVVAVTH 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
375-552 |
2.72e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.73 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVrgsVDGPD---------PRRIAWVPQHPQFSERTVAAELA 445
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL---LDGVPlvqydhhylHRQVALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 446 L---YAGAAGEGAVPGEPGA--LVRELLDQLGLGGLEAAdpAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDA 520
Cdd:TIGR00958 577 YgltDTPDEEIMAAAKAANAhdFIMEFPNGYDTEVGEKG--SQLSGGQKQRIAIARALVR---KPRVLILDEATSALDAE 651
|
170 180 190
....*....|....*....|....*....|..
gi 1001866046 521 SAALVERAiAALAGRvTVLLVSHEPRTAALAD 552
Cdd:TIGR00958 652 CEQLLQES-RSRASR-TVLLIAHRLSTVERAD 681
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
375-551 |
2.83e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 53.96 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVrgsVDGPD-------PRRIAWVPQH----PQFSertvAAE 443
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF---IDGEDvthrsiqQRDICMVFQSyalfPHMS----LGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 444 LALYaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLA---RVadgaglLLLDEPTAHLDda 520
Cdd:PRK11432 98 NVGY-GLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIlkpKV------LLFDEPLSNLD-- 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1001866046 521 saALVERA----IAALAGR--VTVLLVSHEpRTAALA 551
Cdd:PRK11432 169 --ANLRRSmrekIRELQQQfnITSLYVTHD-QSEAFA 202
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
165-303 |
3.01e-07 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 53.63 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 165 DWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKgrtMA 244
Cdd:cd18545 139 NVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENR---KA 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 245 TLRVAFLSAL---ALELISTISVAVVAVFIGIRLVHGDMTLeaG-LLALILAPECF-QPLRDLG 303
Cdd:cd18545 216 NMRAVRLNALfwpLVELISALGTALVYWYGGKLVLGGAITV--GvLVAFIGYVGRFwQPIRNLS 277
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
935-1084 |
3.03e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.97 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 935 GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP--------------VAWCPQESHLFDS-T 999
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1000 VRGNL-AVARDRDHAPSDAELEAV--LARVGLLEHVRSlpggldarigSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEP 1076
Cdd:PRK10895 95 VYDNLmAVLQIRDDLSAEQREDRAneLMEEFHIEHLRD----------SMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
....*...
gi 1001866046 1077 TAHLDPES 1084
Cdd:PRK10895 165 FAGVDPIS 172
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
938-1106 |
3.73e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRV---GSAAVAGP---------VAWCPQES-HLFDSTVRGNL 1004
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitgGDRLVNGRpldssfqrsIGYVQQQDlHLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1005 ---AVARDRDHAPSDAELEAVLARVGLLEhVRSLPgglDARIGSRGAFLSGGQRQRLAVARTLLAG-AEVVLLDEPTAHL 1080
Cdd:TIGR00956 858 rfsAYLRQPKSVSKSEKMEYVEEVIKLLE-MESYA---DAVVGVPGEGLNVEQRKRLTIGVELVAKpKLLLFLDEPTSGL 933
|
170 180
....*....|....*....|....*...
gi 1001866046 1081 DPESGLALVAALHgALAD--RTVVMVTH 1106
Cdd:TIGR00956 934 DSQTAWSICKLMR-KLADhgQAILCTIH 960
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
371-544 |
6.68e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.41 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 371 AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA--------SVRGSVDGPDPRR-IAWVPQ-HPQFSERTV 440
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKiwfsghdiTRLKNREVPFLRRqIGMIFQdHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 441 AAELAL---YAGAAGEGAVPGEPGALVRELLDQLGLGGleaadPAELSPGQQRRVAVARGlarVADGAGLLLLDEPTAHL 517
Cdd:PRK10908 97 YDNVAIpliIAGASGDDIRRRVSAALDKVGLLDKAKNF-----PIQLSGGEQQRVGIARA---VVNKPAVLLADEPTGNL 168
|
170 180
....*....|....*....|....*...
gi 1001866046 518 DDASAALVERAIAALAG-RVTVLLVSHE 544
Cdd:PRK10908 169 DDALSEGILRLFEEFNRvGVTVLMATHD 196
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
899-1083 |
7.69e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.21 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 899 EEQAVRDAAEERDDLQDA---PGRGP------GITLRGVTVGWTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALL 969
Cdd:TIGR00954 419 KRPRVEEIESGREGGRNSnlvPGRGIveyqdnGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 970 TGFLAPRVGSAAVAGPVA--WCPQESHLFDSTVRGNL----AVARDRDHAPSDAELEAVLARVGLlEHVRSLPGGLDArI 1043
Cdd:TIGR00954 499 GELWPVYGGRLTKPAKGKlfYVPQRPYMTLGTLRDQIiypdSSEDMKRRGLSDKDLEQILDNVQL-THILEREGGWSA-V 576
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1001866046 1044 GSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPE 1083
Cdd:TIGR00954 577 QDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
941-1081 |
7.87e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 52.43 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 941 GLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS-------AAVAGPVAWCPQESHL-------FDS-----TVR 1001
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEilfdgqdITGLSGRELRPLRRRMqmvfqdpYASlnprmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 GNLA----VARDRDHAPSDAELEAVLARVGLL-EHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEP 1076
Cdd:COG4608 116 DIIAeplrIHGLASKAERRERVAELLELVGLRpEHADRYPHEF-----------SGGQRQRIGIARALALNPKLIVCDEP 184
|
....*
gi 1001866046 1077 TAHLD 1081
Cdd:COG4608 185 VSALD 189
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
376-555 |
8.01e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.51 E-value: 8.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 376 DFTAPAG-RVTVLaGPSGSGKTTVLAALAGLVrdgvgASVRGS--VDG-------PDPRRIAWVPQ-HPQFSERTVAAEL 444
Cdd:PRK10771 19 DLTVERGeRVAIL-GPSGAGKSTLLNLIAGFL-----TPASGSltLNGqdhtttpPSRRPVSMLFQeNNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 445 ALyagaageGAVPG-----EPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDD 519
Cdd:PRK10771 93 GL-------GLNPGlklnaAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP---ILLLDEPFSALDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1001866046 520 ASAA----LVERAIAalAGRVTVLLVSHEPRTAA-LADRTV 555
Cdd:PRK10771 163 ALRQemltLVSQVCQ--ERQLTLLMVSHSLEDAArIAPRSL 201
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
371-518 |
8.11e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.93 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 371 AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGP----------DPRR-IAWVPQHPQFS--E 437
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkkikevkRLRKeIGLVFQFPEYQlfQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 438 RTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAA-DPAELSPGQQRRVAVARGLArvADGaGLLLLDEPTAH 516
Cdd:PRK13645 106 ETIEKDIAF--GPVNLGENKQEAYKKVPELLKLVQLPEDYVKrSPFELSGGQKRRVALAGIIA--MDG-NTLVLDEPTGG 180
|
..
gi 1001866046 517 LD 518
Cdd:PRK13645 181 LD 182
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
370-555 |
8.42e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 51.56 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 370 PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDGPDP--------RRIAWV-PQHPQFSERTV 440
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG---EVRVAGLVPwkrrkkflRRIGVVfGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 441 AAElALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDA 520
Cdd:cd03267 112 VID-SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE---ILFLDEPTIGLDVV 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 1001866046 521 SAALVERAIAALAG--RVTVLLVSHEPR-TAALADRTV 555
Cdd:cd03267 188 AQENIRNFLKEYNRerGTTVLLTSHYMKdIEALARRVL 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
371-557 |
1.07e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 51.66 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 371 AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRGSVDGPDP-----RRIAWVPQHP--QFSERTVAA 442
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRvKVMGREVNAENekwvrSKVGLVFQDPddQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 443 ELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASA 522
Cdd:PRK13647 100 DVAF--GPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD---VIVLDEPMAYLDPRGQ 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1001866046 523 ALVERAIAALAGR-VTVLLVSHEPRTAA-LADRTVEL 557
Cdd:PRK13647 175 ETLMEILDRLHNQgKTVIVATHDVDLAAeWADQVIVL 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
382-543 |
1.13e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 382 GRVTVLAGPSGSGKTTVLAALAGLVRDgvgasVRGSVDgPDPrRIAWVPQhpqfsertvaaelalYAGAAGEGAVpgepG 461
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKP-----DEGEVD-PEL-KISYKPQ---------------YIKPDYDGTV----E 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 462 ALVRELLDQLGLG--GLEAADP-----------AELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERA 528
Cdd:PRK13409 419 DLLRSITDDLGSSyyKSEIIKPlqlerlldknvKDLSGGELQRVAIAACLSRDAD---LYLLDEPSAHLDVEQRLAVAKA 495
|
170
....*....|....*..
gi 1001866046 529 IAALA--GRVTVLLVSH 543
Cdd:PRK13409 496 IRRIAeeREATALVVDH 512
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
374-522 |
1.13e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 50.34 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 374 PLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVrdGVGASVRGSV--DGPD--------PRRIAWVPQHP-QFSERTVAA 442
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT--EGNVSVEGDIhyNGIPykefaekyPGEIIYVSEEDvHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 443 ELALYAGAAGEGAVPGepgalvrelldqlglggleaadpaeLSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASA 522
Cdd:cd03233 103 TLDFALRCKGNEFVRG-------------------------ISGGERKRVSIAEALVS---RASVLCWDNSTRGLDSSTA 154
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
379-544 |
1.28e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.12 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 379 APAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRGSV-------DGP----DPR-------RIAWVPQHPQFSERT 439
Cdd:PRK10619 28 ANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSiVVNGQTinlvrdkDGQlkvaDKNqlrllrtRLTMVFQHFNLWSHM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 440 VAAELALYAGAAGEGAVPGEpgALVRELLDQLGLGGLEAAD---PAELSPGQQRRVAVARGLARVADgagLLLLDEPTAH 516
Cdd:PRK10619 108 TVLENVMEAPIQVLGLSKQE--ARERAVKYLAKVGIDERAQgkyPVHLSGGQQQRVSIARALAMEPE---VLLFDEPTSA 182
|
170 180 190
....*....|....*....|....*....|
gi 1001866046 517 LDDASAALVERAIAALA--GRvTVLLVSHE 544
Cdd:PRK10619 183 LDPELVGEVLRIMQQLAeeGK-TMVVVTHE 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
941-1081 |
1.30e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 52.38 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 941 GLDLAARPGDWIVVAGPSGSGKSTL-LALLTgfLAPRVGSAAVAG-------PVAWCPQESHL-------FDS-----TV 1000
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLgLALLR--LIPSEGEIRFDGqdldglsRRALRPLRRRMqvvfqdpFGSlsprmTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 R-----GNLAVARDRDHAPSDAELEAVLARVGLlehvrslpgglDARIGSR--GAFlSGGQRQRLAVARTLLAGAEVVLL 1073
Cdd:COG4172 382 GqiiaeGLRVHGPGLSAAERRARVAEALEEVGL-----------DPAARHRypHEF-SGGQRQRIAIARALILEPKLLVL 449
|
....*...
gi 1001866046 1074 DEPTAHLD 1081
Cdd:COG4172 450 DEPTSALD 457
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
938-1081 |
1.33e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTL-LALLTgfLAPRVGSAAVAGpvawcpQESHLFD------------------- 997
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTgLALLR--LINSQGEIWFDG------QPLHNLNrrqllpvrhriqvvfqdpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 998 STVRGNLAVARD-----RDHAP--SDAELEAVLARVglLEHVrslpgGLDARIGSR-GAFLSGGQRQRLAVARTLLAGAE 1069
Cdd:PRK15134 373 SSLNPRLNVLQIieeglRVHQPtlSAAQREQQVIAV--MEEV-----GLDPETRHRyPAEFSGGQRQRIAIARALILKPS 445
|
170
....*....|..
gi 1001866046 1070 VVLLDEPTAHLD 1081
Cdd:PRK15134 446 LIILDEPTSSLD 457
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
948-1103 |
1.64e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.69 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 948 PGDWIVVAGPSGSGKSTLLALLTGFLAPRvgsaavAGPVAWCPQESHLFDSTvrgNLAVARDR----------DHAPSDA 1017
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPD------AGEVHYRMRDGQLRDLY---ALSEAERRrllrtewgfvHQHPRDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1018 -------------ELEAVLAR---------VGLLEHVRSLPggldARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDE 1075
Cdd:PRK11701 102 lrmqvsaggnigeRLMAVGARhygdirataGDWLERVEIDA----ARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1001866046 1076 PTAHLD---------------PESGLALVAALHG-----ALADRTVVM 1103
Cdd:PRK11701 178 PTGGLDvsvqarlldllrglvRELGLAVVIVTHDlavarLLAHRLLVM 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
939-1081 |
1.85e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 939 LAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS-------AAVAGPVAWC------------PQES----HL 995
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGElyyqgqdLLKADPEAQKllrqkiqivfqnPYGSlnprKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 996 FDSTVRGNLAVARDRDHAPSDAELEAVLARVGLL-EHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAEVVLLD 1074
Cdd:PRK11308 111 VGQILEEPLLINTSLSAAERREKALAMMAKVGLRpEHYDRYP-----------HMFSGGQRQRIAIARALMLDPDVVVAD 179
|
....*..
gi 1001866046 1075 EPTAHLD 1081
Cdd:PRK11308 180 EPVSALD 186
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
944-1131 |
2.54e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.19 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 944 LAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-----------------PVAWCPQESHLFDS-TVRGNLA 1005
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHmTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1006 VARDRDHAPSDAELEA---VLARVGLLEHVRSLPGGldarigsrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:PRK10070 129 FGMELAGINAEERREKaldALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 1083 ------ESGLALVAALHgalaDRTVVMVTHHATE---------LMPGDTLVRLGARERVLHHAA 1131
Cdd:PRK10070 198 lirtemQDELVKLQAKH----QRTIVFISHDLDEamrigdriaIMQNGEVVQVGTPDEILNNPA 257
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
355-544 |
2.78e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 50.62 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEPAVGPLD---FTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRGSVDGPDP------- 423
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELVALNnisYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTiQVGDIYIGDKKnnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 424 --------------RRIAWVPQHP--QFSERTVAAELALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAAdPAELSPG 487
Cdd:PRK13631 102 npyskkiknfkelrRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERS-PFGLSGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 488 QQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAI-AALAGRVTVLLVSHE 544
Cdd:PRK13631 181 QKRRVAIAGILAIQPE---ILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHT 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
904-1077 |
2.79e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.17 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 904 RDAAEERDDLQDAPGRgPGITLRGVTVgwtggPDVLAGLDLAARPGDwIV-VAGPSGSGKSTLLALLTGFLAPRVGSAAV 982
Cdd:COG1129 239 RELEDLFPKRAAAPGE-VVLEVEGLSV-----GGVVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 983 AG-------P-------VAWCPQESH---LF-DSTVRGNLAVARDRDHAPS---DAELEAVLARvgllEHVRSL---PGG 1038
Cdd:COG1129 312 DGkpvrirsPrdairagIAYVPEDRKgegLVlDLSIRENITLASLDRLSRGgllDRRRERALAE----EYIKRLrikTPS 387
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 1039 LDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPT 1077
Cdd:COG1129 388 PEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
373-557 |
3.29e-06 |
|
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: 48.51 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 373 GPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVrdgVGASVRGSVDGPDPRRIaWVPQhpqfsertVAAELALyagaag 452
Cdd:cd03227 12 VPNDVTFGEGSLTIITGPNGSGKSTILDAIGLAL---GGAQSATRRRSGVKAGC-IVAA--------VSAELIF------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 453 egAVPGepgalvrelldqlglggleaadpaeLSPGQQRRVAVAR--GLARVaDGAGLLLLDEPTAHLDDASAALVERAIA 530
Cdd:cd03227 74 --TRLQ-------------------------LSGGEKELSALALilALASL-KPRPLYILDEIDRGLDPRDGQALAEAIL 125
|
170 180
....*....|....*....|....*...
gi 1001866046 531 ALA-GRVTVLLVSHEPRTAALADRTVEL 557
Cdd:cd03227 126 EHLvKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
375-545 |
3.32e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.03 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--DGV----GASVRGsvDGPDPRR-IAWVPQHPQFSERTVAAE-LAL 446
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARpdAGEvlwqGEPIRR--QRDEYHQdLLYLGHQPGIKTELTALEnLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 447 YAGAAGEGAVPGEPGALVRelldqLGLGGLEAADPAELSPGQQRRVAvargLARVA-DGAGLLLLDEPTAHLDDASAALV 525
Cdd:PRK13538 98 YQRLHGPGDDEALWEALAQ-----VGLAGFEDVPVRQLSAGQQRRVA----LARLWlTRAPLWILDEPFTAIDKQGVARL 168
|
170 180
....*....|....*....|.
gi 1001866046 526 ERAIAA-LAGRVTVLLVSHEP 545
Cdd:PRK13538 169 EALLAQhAEQGGMVILTTHQD 189
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
920-1080 |
3.38e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 920 GPGITLRGVTVGWtggPDV--LAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS--------------AAVA 983
Cdd:PRK11288 2 SPYLSFDGIGKTF---PGVkaLDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSilidgqemrfasttAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 984 GPVAWCPQESHLF-DSTVRGNLAVArdrdHAPSDAEL---EAVLARVGL-LEHVrslpgGLDARIGSRGAFLSGGQRQRL 1058
Cdd:PRK11288 79 AGVAIIYQELHLVpEMTVAENLYLG----QLPHKGGIvnrRLLNYEAREqLEHL-----GVDIDPDTPLKYLSIGQRQMV 149
|
170 180
....*....|....*....|..
gi 1001866046 1059 AVARTLLAGAEVVLLDEPTAHL 1080
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSL 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
364-557 |
3.55e-06 |
|
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: 49.41 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 364 YDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTvLAALagLVRDGVGASVRGSVDGPD---------PRRIAWVPQHPQ 434
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKST-LTKL--IQRFYVPENGRVLVDGHDlaladpawlRRQVGVVLQENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 435 FSERTVAAELALYAGAAG-----EGAVPGEPGALVRELLDQLGLGGLEAAdpAELSPGQQRRVAVARGLarvADGAGLLL 509
Cdd:cd03252 87 LFNRSIRDNIALADPGMSmerviEAAKLAGAHDFISELPEGYDTIVGEQG--AGLSGGQRQRIAIARAL---IHNPRILI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1001866046 510 LDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVM 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
376-518 |
4.09e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.02 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 376 DFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGS---VDGPDPR-------RIAWVPQHP--QFSERTVAAE 443
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErviTAGKKNKklkplrkKVGIVFQFPehQLFEETVEKD 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 444 LALyaGAAGEGAVPGEPGALVRELLDQL-GLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLD 518
Cdd:PRK13634 107 ICF--GPMNFGVSEEDAKQKAREMIELVgLPEELLARSPFELSGGQMRRVAIAGVLAMEPE---VLVLDEPTAGLD 177
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
921-1106 |
4.11e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESHlfdstv 1000
Cdd:PRK10636 311 PLLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH------ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 rgNLAVARdRDHAPsdAELEAVLARVGLLEHVRSLPGGLdariGSRG-------AFLSGGQRQRLAVARTLLAGAEVVLL 1073
Cdd:PRK10636 384 --QLEFLR-ADESP--LQHLARLAPQELEQKLRDYLGGF----GFQGdkvteetRRFSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190
....*....|....*....|....*....|....*.
gi 1001866046 1074 DEPTAHLDPESGLALVAAL---HGALadrtvVMVTH 1106
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEALidfEGAL-----VVVSH 485
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
904-1099 |
4.38e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 904 RDAAEERDDLQDAPGRgPGITLRGVTVGWTGGPDVLAGLDLAARPGDwIV-VAGPSGSGKSTLLALLTGFLAPRVGSAAV 982
Cdd:COG3845 240 REVLLRVEKAPAEPGE-VVLEVENLSVRDDRGVPALKDVSLEVRAGE-ILgIAGVAGNGQSELAEALAGLRPPASGSIRL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 983 AG-------P-------VAWCPQESHLF----DSTVRGNLaVARDRDHAPsdaeleavLARVGLL------EHVRSL--- 1035
Cdd:COG3845 318 DGeditglsPrerrrlgVAYIPEDRLGRglvpDMSVAENL-ILGRYRRPP--------FSRGGFLdrkairAFAEELiee 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 1036 ----PGGLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESglalVAALHGALADR 1099
Cdd:COG3845 389 fdvrTPGPDTPARS----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGA----IEFIHQRLLEL 448
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
350-542 |
4.74e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 350 AAPAGLRVAGLTV-WYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRGSVDGPDPRR-- 425
Cdd:PRK15056 2 MQQAGIVVNDVTVtWRNG--HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKiSILGQPTRQALQKnl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 426 IAWVPQHPQFS-ERTVAAELALYAGAAGEGAVPGEPGA----LVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLAR 500
Cdd:PRK15056 80 VAYVPQSEEVDwSFPVLVEDVVMMGRYGHMGWLRRAKKrdrqIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1001866046 501 VADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVS 542
Cdd:PRK15056 160 QGQ---VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVS 198
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
938-1081 |
5.20e-06 |
|
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: 49.42 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-------------------------PVAWCPQE 992
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrdvqlvfqdsPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 993 ShlFDSTVRGNLAVARDRDHAPSDAELEAVLARVGL-LEHVRSLPggldarigsrgAFLSGGQRQRLAVARTLLAGAEVV 1071
Cdd:TIGR02769 106 T--VRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLP-----------RQLSGGQLQRINIARALAVKPKLI 172
|
170
....*....|
gi 1001866046 1072 LLDEPTAHLD 1081
Cdd:TIGR02769 173 VLDEAVSNLD 182
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
483-554 |
6.39e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.26 E-value: 6.39e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 483 ELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHE-PRTAALADRT 554
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPK---VLLMDEPCFGLDPIASMKVESLIQSLRLRseLTMVIVSHNlHQVSRLSDFT 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
925-1093 |
6.82e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.21 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 925 LRG--VTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPvawcpQESHLFDSTVRG 1002
Cdd:PRK10253 8 LRGeqLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE-----HIQHYASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1003 NLAVARDRDHAPSDAELEAVLARvGLLEH----VRSLPGGLDARIGSRGAF------------LSGGQRQRLAVARTLLA 1066
Cdd:PRK10253 82 RIGLLAQNATTPGDITVQELVAR-GRYPHqplfTRWRKEDEEAVTKAMQATgithladqsvdtLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1001866046 1067 GAEVVLLDEPTAHLD---------------PESGLALVAALH 1093
Cdd:PRK10253 161 ETAIMLLDEPTTWLDishqidllellselnREKGYTLAAVLH 202
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
355-518 |
7.08e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 49.56 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVD----GPDPRRIAWVP 430
Cdd:PRK09452 15 VELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithvPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 431 QH-PQFSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGlarVADGAGLLL 509
Cdd:PRK09452 93 QSyALFPHMTVFENVAF--GLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA---VVNKPKVLL 167
|
....*....
gi 1001866046 510 LDEPTAHLD 518
Cdd:PRK09452 168 LDESLSALD 176
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
165-291 |
7.10e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 49.02 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 165 DWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKGRTMA 244
Cdd:cd18546 138 DPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLR 217
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1001866046 245 TLRVAFLSALALELISTISVAVVAVFIGIRLVHGDMTLEAgLLALIL 291
Cdd:cd18546 218 AQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGV-LVAFLL 263
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
947-1106 |
7.75e-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: 48.01 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 947 RPGDWIVVAGPSGSGKSTLLALLTG-----------FLAPRVGSAAVAGPVAWCPQES-HLFDSTVRGNLavardrdhap 1014
Cdd:cd03232 31 KPGTLTALMGESGAGKTTLLDVLAGrktagvitgeiLINGRPLDKNFQRSTGYVEQQDvHSPNLTVREAL---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1015 sdaELEAVLarvgllehvrslpggldarigsRGafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHG 1094
Cdd:cd03232 101 ---RFSALL----------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
|
170
....*....|...
gi 1001866046 1095 -ALADRTVVMVTH 1106
Cdd:cd03232 154 lADSGQAILCTIH 166
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
925-1110 |
8.06e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 49.33 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 925 LRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGP-----------VAWCPQES 993
Cdd:PRK11432 9 LKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 994 HLFDSTVRG-NLAVARDRDHAPSDAELEAV---LARVGLlehvrslpGGLDARIGSRgafLSGGQRQRLAVARTLLAGAE 1069
Cdd:PRK11432 88 ALFPHMSLGeNVGYGLKMLGVPKEERKQRVkeaLELVDL--------AGFEDRYVDQ---ISGGQQQRVALARALILKPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1070 VVLLDEPTAHLDpesglalvAALHGALADR----------TVVMVTHHATE 1110
Cdd:PRK11432 157 VLLFDEPLSNLD--------ANLRRSMREKirelqqqfniTSLYVTHDQSE 199
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
370-544 |
8.11e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.41 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 370 PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVrgsVDGPD------------PRRIAWVPQHpqF-- 435
Cdd:PRK11153 19 HALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVL---VDGQDltalsekelrkaRRQIGMIFQH--Fnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 436 -SERTVAAELALYAGAAGEGAvpGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLA---RVadgaglLLLD 511
Cdd:PRK11153 94 lSSRTVFDNVALPLELAGTPK--AEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAsnpKV------LLCD 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 512 EPTAHLDDASAalveRAIAALAGRV------TVLLVSHE 544
Cdd:PRK11153 166 EATSALDPATT----RSILELLKDInrelglTIVLITHE 200
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
953-1129 |
8.35e-06 |
|
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: 46.97 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 953 VVAGPSGSGKSTL-----LALLTGFLAPRVGSAAVAGPVAWCPqeshlfdstvrgnlavardrdhapsdaELEAVLARVG 1027
Cdd:cd03227 25 IITGPNGSGKSTIldaigLALGGAQSATRRRSGVKAGCIVAAV---------------------------SAELIFTRLQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1028 LlehvrslpggldarigsrgaflSGGQRQRLAVArTLLAGAEV-----VLLDEPTAHLDPESGLALVAALHGALADRTVV 1102
Cdd:cd03227 78 L----------------------SGGEKELSALA-LILALASLkprplYILDEIDRGLDPRDGQALAEAILEHLVKGAQV 134
|
170 180
....*....|....*....|....*...
gi 1001866046 1103 MVTHHATELM-PGDTLVRLGARERVLHH 1129
Cdd:cd03227 135 IVITHLPELAeLADKLIHIKKVITGVYK 162
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
938-1081 |
9.83e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.53 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAWCPQESH---------LF-DS-------- 998
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGePLAKLNRAQRkafrrdiqmVFqDSisavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 TVRGNLAVA----RDRDHAPSDAELEAVLARVGL-LEHVRSLPGGldarigsrgafLSGGQRQRLAVARTLLAGAEVVLL 1073
Cdd:PRK10419 107 TVREIIREPlrhlLSLDKAERLARASEMLRAVDLdDSVLDKRPPQ-----------LSGGQLQRVCLARALAVEPKLLIL 175
|
....*...
gi 1001866046 1074 DEPTAHLD 1081
Cdd:PRK10419 176 DEAVSNLD 183
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
342-553 |
9.86e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.57 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 342 AERPPAGQAApaglRVAGLTVW------YDGAAePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAAL-------AGLVR- 407
Cdd:PRK13657 320 RDPPGAIDLG----RVKGAVEFddvsfsYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILi 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 408 DGVG------ASVRgsvdgpdpRRIAWVPQHPQFSERTVA------------AELALYAGAA-----------GEGAVPG 458
Cdd:PRK13657 395 DGTDirtvtrASLR--------RNIAVVFQDAGLFNRSIEdnirvgrpdatdEEMRAAAERAqahdfierkpdGYDTVVG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 459 EPGalvrelldqlglggleaadpAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALAGRVTV 538
Cdd:PRK13657 467 ERG--------------------RQLSGGERQRLAIARALLK---DPPILILDEATSALDVETEAKVKAALDELMKGRTT 523
|
250
....*....|....*
gi 1001866046 539 LLVSHEPRTAALADR 553
Cdd:PRK13657 524 FIIAHRLSTVRNADR 538
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
935-1106 |
1.03e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 48.63 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 935 GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVG-------------SAAVAGPVAWCPQESHLFDS-TV 1000
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGeilldaqpleswsSKAFARKVAYLPQQLPAAEGmTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1001 RGNLAVAR-------DRDHAPSDAELEAVLARVGLLEHVRSLpggLDArigsrgafLSGGQRQRLAVARTLLAGAEVVLL 1073
Cdd:PRK10575 103 RELVAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRL---VDS--------LSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1001866046 1074 DEPTAHLDPESGLALVAALHGALADR--TVVMVTH 1106
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERglTVIAVLH 206
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
382-545 |
1.32e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 382 GRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGPD-----PRRIAWVPQHP------------QFS-------- 436
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPldssfQRSIGYVQQQDlhlptstvreslRFSaylrqpks 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 437 ------ERTVAA-----ELALYAgaageGAVPGEPGalvrelldqlglggleaadpAELSPGQQRRVAVARGLarVADGA 505
Cdd:TIGR00956 869 vsksekMEYVEEvikllEMESYA-----DAVVGVPG--------------------EGLNVEQRKRLTIGVEL--VAKPK 921
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1001866046 506 GLLLLDEPTAHLDDASAALVERAIAALA--GRvTVLLVSHEP 545
Cdd:TIGR00956 922 LLLFLDEPTSGLDSQTAWSICKLMRKLAdhGQ-AILCTIHQP 962
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
941-1111 |
1.36e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.55 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 941 GLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAprvgsaAVAGPVAWCPQEshLFDSTVRGNLAVARD----------- 1009
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK------ATDGEVAWLGKD--LLGMKDDEWRAVRSDiqmifqdplas 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1010 ---------------RDHAP--SDAELE----AVLARVGLLEHVrslpggldarIGSRGAFLSGGQRQRLAVARTLLAGA 1068
Cdd:PRK15079 111 lnprmtigeiiaeplRTYHPklSRQEVKdrvkAMMLKVGLLPNL----------INRYPHEFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 1069 EVVLLDEPTAHLD---------------PESGLALVAALHGA-----LADRTVVMVTHHATEL 1111
Cdd:PRK15079 181 KLIICDEPVSALDvsiqaqvvnllqqlqREMGLSLIFIAHDLavvkhISDRVLVMYLGHAVEL 243
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
379-545 |
1.41e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.28 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 379 APAGRVTVLAGPSGSGKTTVLAALAGLVRDGVgaSVRGSV-------DGPDPRRI-AWVPQH----PQFSER---TVAAE 443
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGV--KGSGSVllngmpiDAKEMRAIsAYVQQDdlfiPTLTVRehlMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 444 LALYAGAAGEGAVpgepgALVREllDQLGLGGLEAAD-----PAE---LSPGQQRRVAVARGLarVADGAgLLLLDEPTA 515
Cdd:TIGR00955 126 LRMPRRVTKKEKR-----ERVDE--VLQALGLRKCANtrigvPGRvkgLSGGERKRLAFASEL--LTDPP-LLFCDEPTS 195
|
170 180 190
....*....|....*....|....*....|.
gi 1001866046 516 HLDDASAALVERAIAALA-GRVTVLLVSHEP 545
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAqKGKTIICTIHQP 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
481-553 |
1.43e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.14 E-value: 1.43e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 481 PAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTA-ALADR 553
Cdd:PRK11247 131 PAALSGGQKQRVALARALIH---RPGLLLLDEPLGALDALTRIEMQDLIESLWQQhgFTVLLVTHDVSEAvAMADR 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
483-557 |
1.53e-05 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 49.03 E-value: 1.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 483 ELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAI--AALAGRVTVLLVSHEPRTAA-LADRTVEL 557
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAK---EPFLFLADEPTGTLDPQTAKLVHNALeeAVKASGISMVLTSHWPEVIEdLSDKAIWL 242
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
370-518 |
1.90e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 48.30 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 370 PAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGaSVRgsVDGPD---------PRRIAWVPQHP----QFS 436
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAG-TVL--VAGDDvealsaraaSRRVASVPQDTslsfEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 437 ERTVaAELALYAGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAH 516
Cdd:PRK09536 94 VRQV-VEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP---VLLLDEPTAS 169
|
..
gi 1001866046 517 LD 518
Cdd:PRK09536 170 LD 171
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
365-555 |
1.97e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.77 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 365 DGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVrgsVDGPDP----------RRIAWVPQHP- 433
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVY---VDGLDTsdeenlwdirNKAGMVFQNPd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 434 -QFSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDE 512
Cdd:PRK13633 96 nQIVATIVEEDVAF--GPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE---CIIFDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1001866046 513 PTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAALADRTV 555
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRII 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
377-557 |
2.00e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.12 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 377 FTAPAGRVTVLAGPSGSGKTTVLAALAGL--------VRDGVGASVRGSVDGPDPR--RIAWVPQH----PQFSERTVAA 442
Cdd:PRK11629 30 FSIGEGEMMAIVGSSGSGKSTLLHLLGGLdtptsgdvIFNGQPMSKLSSAAKAELRnqKLGFIYQFhhllPDFTALENVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 443 ELALYAGAAgegavPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLarvADGAGLLLLDEPTAHLDDASA 522
Cdd:PRK11629 110 MPLLIGKKK-----PAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL---VNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1001866046 523 alveRAIAALAGRVTV------LLVSHEPRTAALADRTVEL 557
Cdd:PRK11629 182 ----DSIFQLLGELNRlqgtafLVVTHDLQLAKRMSRQLEM 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
389-553 |
2.12e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 47.80 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 389 GPSGSGKTTVLAALAGLVRDGVGASVrgsVDGP--------DPRR-IAWVPQHP--QFSERTVAAELALyaGAAGEGAVP 457
Cdd:PRK13650 40 GHNGSGKSTTVRLIDGLLEAESGQII---IDGDllteenvwDIRHkIGMVFQNPdnQFVGATVEDDVAF--GLENKGIPH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 458 GEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVArglARVADGAGLLLLDEPTAHLDDASAALVERAIAALAGR-- 535
Cdd:PRK13650 115 EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA---GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyq 191
|
170
....*....|....*...
gi 1001866046 536 VTVLLVSHEPRTAALADR 553
Cdd:PRK13650 192 MTVISITHDLDEVALSDR 209
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
141-291 |
2.21e-05 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 47.81 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 141 TQYLPALVqTAVLpLLVGARILGA--DWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPvL 218
Cdd:cd18551 111 TSGLPQLV-TGVL-TVVGAVVLMFllDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIR-T 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 219 VGLGRA--AEQRRALGELSRAYKgrtmATLRVAFLSAL---ALELISTISVAVVAVFIGIRLVHGDMTLeAGLLALIL 291
Cdd:cd18551 188 VKASNAeeRETKRGGEAAERLYR----AGLKAAKIEALigpLMGLAVQLALLVVLGVGGARVASGALTV-GTLVAFLL 260
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1050-1106 |
2.38e-05 |
|
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: 46.03 E-value: 2.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 1050 LSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGAL--ADRTVVMVTH 1106
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEH 130
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
484-555 |
2.78e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 2.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 484 LSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGRV--TVLLVSHEPRTAALADRTV 555
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPK---ILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIV 1429
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
934-1082 |
2.86e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.80 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 934 GGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGflAPRVGSAAVA----------------GPVAWCPQESHLFD 997
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVfdgkditdwqtakimrEAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 998 S-TVRGNLAVArdrdhaPSDAELEAVLARVgllEHVRSLPGGLDARIGSRGAFLSGGQRQRLAVARTLLAGAEVVLLDEP 1076
Cdd:PRK11614 94 RmTVEENLAMG------GFFAERDQFQERI---KWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
....*.
gi 1001866046 1077 TAHLDP 1082
Cdd:PRK11614 165 SLGLAP 170
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
922-1106 |
3.14e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.00 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 922 GITLRGVTVgwTGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPrvGSAAVAGPVAWCPQESHLfdSTVR 1001
Cdd:PRK10418 4 QIELRNIAL--QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDGKPVAP--CALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 GNLA-------------VARDRDHA----------PSDAELEAVLARVGLLEhvrslpgglDARIGSRGAF-LSGGQRQR 1057
Cdd:PRK10418 78 GRKIatimqnprsafnpLHTMHTHAretclalgkpADDATLTAALEAVGLEN---------AARVLKLYPFeMSGGMLQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 1058 LAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRT--VVMVTH 1106
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTH 199
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
938-1106 |
3.21e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.30 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALL---------------TGFLAPRVGSAAVAGpvaWCPQ----------- 991
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrktggyiegdiriSGFPKKQETFARISG---YCEQndihspqvtvr 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 992 ESHLFDSTVRGNLAVARDRDHAPSDAELEAVLarvglLEHVRSLPGGLDARIGsrgafLSGGQRQRLAVARTLLAGAEVV 1071
Cdd:PLN03140 972 ESLIYSAFLRLPKEVSKEEKMMFVDEVMELVE-----LDNLKDAIVGLPGVTG-----LSTEQRKRLTIAVELVANPSII 1041
|
170 180 190
....*....|....*....|....*....|....*.
gi 1001866046 1072 LLDEPTAHLDPESGLALVAALHGAL-ADRTVVMVTH 1106
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIH 1077
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
943-1084 |
3.52e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 943 DLAARPGDWIVVAGPSGSGKSTLLALLTGFLA---------------------PRvgsaAVAGPVawcpqeshlFDSTVR 1001
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLlddgriiyeqdlivarlqqdpPR----NVEGTV---------YDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1002 GNLAVA----------RDRDHAPSDAELEAvLARV-GLLEHVrslpGG--LDARIG-----------SRGAFLSGGQRQR 1057
Cdd:PRK11147 90 GIEEQAeylkryhdisHLVETDPSEKNLNE-LAKLqEQLDHH----NLwqLENRINevlaqlgldpdAALSSLSGGWLRK 164
|
170 180
....*....|....*....|....*..
gi 1001866046 1058 LAVARTLLAGAEVVLLDEPTAHLDPES 1084
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
935-1107 |
3.56e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.71 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 935 GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGF-------------------LAP--RVGSA---AVAGPVAWCP 990
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedyevtggtvefkgkdlleLSPedRAGEGifmAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 991 QESHLFDSTVRGnlAVARDRDHAPSDA-ELEAVL-ARVGLLEhvrsLPGGLDARIGSRGafLSGGQRQRLAVARTLLAGA 1068
Cdd:PRK09580 93 VSNQFFLQTALN--AVRSYRGQEPLDRfDFQDLMeEKIALLK----MPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1001866046 1069 EVVLLDEPTAHLDPESgLALVAALHGALAD--RTVVMVTHH 1107
Cdd:PRK09580 165 ELCILDESDSGLDIDA-LKIVADGVNSLRDgkRSFIIVTHY 204
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
953-1121 |
3.60e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 953 VVAGPSGSGKSTLLalLTGFLAprVGSAAVAGpvawcpqeshlFDSTVRGNLAVARDrdhapsdaELEAVLArVGLlehv 1032
Cdd:cd03238 25 VVTGVSGSGKSTLV--NEGLYA--SGKARLIS-----------FLPKFSRNKLIFID--------QLQFLID-VGL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1033 rslpGGLdaRIGSRGAFLSGGQRQRLAVARTLLAGAE--VVLLDEPTAHLDPESGLALVAALHGaLADR--TVVMVTHHA 1108
Cdd:cd03238 77 ----GYL--TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKG-LIDLgnTVILIEHNL 149
|
170
....*....|...
gi 1001866046 1109 TELMPGDTLVRLG 1121
Cdd:cd03238 150 DVLSSADWIIDFG 162
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
938-1106 |
4.16e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.03 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDwiVVA--GPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAW--------CPQESHLF-DSTVRGNLA 1005
Cdd:COG4152 16 AVDDVSFTVPKGE--IFGllGPNGAGKTTTIRIILGILAPDSGEVLWDGePLDPedrrrigyLPEERGLYpKMKVGEQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1006 -VARDRDHAPSDA--ELEAVLARVGLLEHvrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:COG4152 94 yLARLKGLSKAEAkrRADEWLERLGLGDR-------ANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPFSGLDP 162
|
170 180
....*....|....*....|....*.
gi 1001866046 1083 ESGLALVAALHgALADR--TVVMVTH 1106
Cdd:COG4152 163 VNVELLKDVIR-ELAAKgtTVIFSSH 187
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
344-557 |
4.57e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 344 RPPAGQAAPAGLRVAGLTVWYDGAAEPAVGPLDF-TAPAGRVTVLaGPSGSGKTTVLAALAGLVRDGVGasvRGSVDGPD 422
Cdd:PLN03232 1224 RPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFfVSPSEKVGVV-GRTGAGKSSMLNALFRIVELEKG---RIMIDDCD 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 423 ---------PRRIAWVPQHPQFSERTVAAELALYAGAAGEGAVPGEPGALVRELLDQLG-LGGLEAADPAE-LSPGQQRR 491
Cdd:PLN03232 1300 vakfgltdlRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPfGLDAEVSEGGEnFSVGQRQL 1379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 492 VAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSHEPRTAALADRTVEL 557
Cdd:PLN03232 1380 LSLARALLRRSK---ILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVL 1442
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1033-1107 |
4.62e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1033 RSLPGGLDArigsrgafLSGGQRQ------RLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALHGALADRT----VV 1102
Cdd:PRK01156 793 GGMVEGIDS--------LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipqVI 864
|
....*
gi 1001866046 1103 MVTHH 1107
Cdd:PRK01156 865 MISHH 869
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
331-518 |
4.70e-05 |
|
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: 47.37 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 331 LLAAGHGRvqdaERPPAGQAAPAGLRVAGLTVWYDG---------AAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAA 401
Cdd:COG4172 256 LLAAEPRG----DPRPVPPDAPPLLEARDLKVWFPIkrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 402 LAGLVRDGVGASVRG-SVDGPDP-------RRIAWVPQHPqFS--------ERTVAAELALYAgaagegavPGEPGALVR 465
Cdd:COG4172 332 LLRLIPSEGEIRFDGqDLDGLSRralrplrRRMQVVFQDP-FGslsprmtvGQIIAEGLRVHG--------PGLSAAERR 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 466 ELLDQLGLG---GLEAAD--PAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLD 518
Cdd:COG4172 403 ARVAEALEEvglDPAARHryPHEFSGGQRQRIAIARALILEPK---LLVLDEPTSALD 457
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
938-1106 |
5.42e-05 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 45.60 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESHLFDS--TVRGNlAVARDRDHAPS 1015
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFNPelTGREN-IYLNGRLLGLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1016 DAELEAVLARV----GLLEHvrslpggLDARIGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAA 1091
Cdd:cd03220 116 RKEIDEKIDEIiefsELGDF-------IDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRR 184
|
170
....*....|....*.
gi 1001866046 1092 LHGALAD-RTVVMVTH 1106
Cdd:cd03220 185 LRELLKQgKTVILVSH 200
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1024-1121 |
5.93e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.71 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1024 ARVGLLEHVRSLPG-GLDARIGSRGA-FLSGGQRQRLAVARTLLAGAEVVL--LDEPTAHLDPESGLALVAALHgALAD- 1098
Cdd:cd03270 110 ARVGIRERLGFLVDvGLGYLTLSRSApTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLK-RLRDl 188
|
90 100
....*....|....*....|....
gi 1001866046 1099 -RTVVMVTHHATELMPGDTLVRLG 1121
Cdd:cd03270 189 gNTVLVVEHDEDTIRAADHVIDIG 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
923-1080 |
6.05e-05 |
|
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: 47.13 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 923 ITLRGVTVGWtGGPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAprvgSAAVAGPVAWCPQE---SHLFDST 999
Cdd:TIGR02633 2 LEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYP----HGTWDGEIYWSGSPlkaSNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1000 VRGNLAVARDRDHAPSDAELEAVlarvgLLEHVRSLPGG-------------------LDARIGSRGAF-LSGGQRQRLA 1059
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENI-----FLGNEITLPGGrmaynamylraknllrelqLDADNVTRPVGdYGGGQQQLVE 151
|
170 180
....*....|....*....|.
gi 1001866046 1060 VARTLLAGAEVVLLDEPTAHL 1080
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSL 172
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
479-552 |
6.64e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 6.64e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 479 ADPAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALAG---RVTVlLVSHEPRTAALAD 552
Cdd:PTZ00265 575 SNASKLSGGQKQRISIARAIIR---NPKILILDEATSSLDNKSEYLVQKTINNLKGnenRITI-IIAHRLSTIRYAN 647
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
376-552 |
6.66e-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: 45.29 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 376 DFTAPagrVTVLAGPSGSGKTTVLAAL-AGLVRDGVgASVRGSVDGPDP----RRIAWVpqHPQFSER-----TVAAELA 445
Cdd:cd03240 19 EFFSP---LTLIVGQNGAGKTTIIEALkYALTGELP-PNSKGGAHDPKLiregEVRAQV--KLAFENAngkkyTITRSLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 446 LYAGAA----GEGAVPgepgaLVRElldqlglggleaadPAELSPGQqrRVAVA---R-GLARVADG-AGLLLLDEPTAH 516
Cdd:cd03240 93 ILENVIfchqGESNWP-----LLDM--------------RGRCSGGE--KVLASliiRlALAETFGSnCGILALDEPTTN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1001866046 517 LDDAS--AALVE--RAIAALAGRvTVLLVSHEPRTAALAD 552
Cdd:cd03240 152 LDEENieESLAEiiEERKSQKNF-QLIVITHDEELVDAAD 190
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
375-544 |
7.06e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.84 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVrgsVDGPD-----------PRRIAWVPQHP--QFSERTVA 441
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL---IKGEPikydkksllevRKTVGIVFQNPddQLFAPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 442 AELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDAS 521
Cdd:PRK13639 98 EDVAF--GPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE---IIVLDEPTSGLDPMG 172
|
170 180
....*....|....*....|....
gi 1001866046 522 AALVERAIAALAGR-VTVLLVSHE 544
Cdd:PRK13639 173 ASQIMKLLYDLNKEgITIIISTHD 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
484-543 |
7.53e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 46.74 E-value: 7.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 484 LSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDdasaALVERAIAAL-----AGRvTVLLVSH 543
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAP---LLLLDEPTEGLD----AETERQILELlaehaQNK-TVLMITH 532
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
482-518 |
8.70e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 8.70e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1001866046 482 AELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLD 518
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPD---VLLLDEPTNHLD 188
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
938-988 |
8.97e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.46 E-value: 8.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAW 988
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSA 91
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
382-554 |
1.07e-04 |
|
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: 43.52 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 382 GRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRgsVDGPDPRRIAWVpqhpqfsertvaaelalyagaagegavpgepg 461
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLD-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 462 alvrelldqlgLGGLEAADPAELSPGQQRRVAVARGLARvADGAGLLLLDEPTAHLDDASAALVERAI-------AALAG 534
Cdd:smart00382 48 -----------QLLLIIVGGKKASGSGELRLRLALALAR-KLKPDVLILDEITSLLDAEQEALLLLLEelrllllLKSEK 115
|
170 180
....*....|....*....|...
gi 1001866046 535 RVTVLLVSH---EPRTAALADRT 554
Cdd:smart00382 116 NLTVILTTNdekDLGPALLRRRF 138
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
371-525 |
1.10e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 45.39 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 371 AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR---------DGVGASV-RGSVDGPDPRR----IAWVPQHPQFS 436
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshiELLGRTVqREGRLARDIRKsranTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 437 ERTVAAELALYagaageGAVPGEP--GALVRELLDQLGLGGLEAADP-----------AELSPGQQRRVAVARGLARVAD 503
Cdd:PRK09984 99 NRLSVLENVLI------GALGSTPfwRTCFSWFTREQKQRALQALTRvgmvhfahqrvSTLSGGQQQRVAIARALMQQAK 172
|
170 180
....*....|....*....|..
gi 1001866046 504 gagLLLLDEPTAHLDDASAALV 525
Cdd:PRK09984 173 ---VILADEPIASLDPESARIV 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
921-1133 |
1.14e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 921 PGITLRGVTVGWTGGPdVLAGLDLAARPGD--WIVvaGPSGSGKSTLLALLTG-----------FLAPRVGSaavaGPVA 987
Cdd:PRK10938 259 PRIVLNNGVVSYNDRP-ILHNLSWQVNPGEhwQIV--GPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS----GETI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 988 W--------CPQESHL---FDSTVRgNLAVARDRD-----HAPSDAELEAVLARVGLLehvrslpgGLDARIGSrGAF-- 1049
Cdd:PRK10938 332 WdikkhigyVSSSLHLdyrVSTSVR-NVILSGFFDsigiyQAVSDRQQKLAQQWLDIL--------GIDKRTAD-APFhs 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1050 LSGGQrQRLA-VARTLLAGAEVVLLDEPTAHLDPesglalvaaLHGALADRTV-VMVTHHATELMpgdtlvrlgareRVL 1127
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDP---------LNRQLVRRFVdVLISEGETQLL------------FVS 459
|
....*.
gi 1001866046 1128 HHAARA 1133
Cdd:PRK10938 460 HHAEDA 465
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-544 |
1.35e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.98 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAepAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDgVGASVRgsVDGpdpRRIAWVPQHP- 433
Cdd:PRK11300 6 LSVSGLMMRFGGLL--AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKP-TGGTIL--LRG---QHIEGLPGHQi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 434 -------------QFSERT------VAAELALYAGA-AGEGAVPG----EPGALVRELLDQLGLGGLEAAD-PA-ELSPG 487
Cdd:PRK11300 78 armgvvrtfqhvrLFREMTvienllVAQHQQLKTGLfSGLLKTPAfrraESEALDRAATWLERVGLLEHANrQAgNLAYG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 488 QQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHE 544
Cdd:PRK11300 158 QQRRLEIARCMVTQPE---ILMLDEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHD 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
376-555 |
1.41e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.79 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 376 DFTAPAGRVTVLAGPSGSGKTTVLAALAGLVR--------DGVGASVRGSVD----GpdprrIAWVPQHPQFSER-TVAA 442
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQpdsgeiliDGKPVRIRSPRDaialG-----IGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 443 ELALyagaageGAVPGEPGALVRELLDQLGLGGLE----AADP----AELSPGQQRRVAVARGLARvadGAGLLLLDEPT 514
Cdd:COG3845 100 NIVL-------GLEPTKGGRLDRKAARARIRELSEryglDVDPdakvEDLSVGEQQRVEILKALYR---GARILILDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1001866046 515 AHLDDASAALVERAIAALAGR-VTVLLVSH---EPRtaALADR-TV 555
Cdd:COG3845 170 AVLTPQEADELFEILRRLAAEgKSIIFITHklrEVM--AIADRvTV 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
374-549 |
1.65e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.78 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 374 PLDFTAPAGRVTVLAGPSGSGKTTVLAALAglvRDGVGASVRGSVDGPD---------PRRIAWVPQHPQFSERTVAAEL 444
Cdd:PRK10575 29 PLSLTFPAGKVTGLIGHNGSGKSTLLKMLG---RHQPPSEGEILLDAQPleswsskafARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 445 ALYAGAAGEGAVpGEPGALVRELLDqlglgglEAADPAELSPGQQRRVAVARGLAR--------VADGAGLLLLDEPTAH 516
Cdd:PRK10575 106 VAIGRYPWHGAL-GRFGAADREKVE-------EAISLVGLKPLAHRLVDSLSGGERqrawiamlVAQDSRCLLLDEPTSA 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1001866046 517 LDDASAALVERAIAALAGR--VTVLLVSHEPRTAA 549
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAA 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
481-557 |
1.80e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.38 E-value: 1.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 481 PAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAALADRTVEL 557
Cdd:PRK10584 144 PAQLSGGEQQRVALARAFNGRPD---VLFADEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRL 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
941-1081 |
1.88e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.08 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 941 GLDLAARPGDwiVVA--GPSGSGKSTLLALLTGFLAPRVGSAAVAGPVAWCPQESHLFD-STVRGNlavardR-----DH 1012
Cdd:COG4586 40 DISFTIEPGE--IVGfiGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRiGVVFGQ------RsqlwwDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1013 AP-------------SDAELEAVLAR-VGLLE-------HVRSlpggldarigsrgafLSGGQRQR--LAVArtLLAGAE 1069
Cdd:COG4586 112 PAidsfrllkaiyriPDAEYKKRLDElVELLDlgelldtPVRQ---------------LSLGQRMRceLAAA--LLHRPK 174
|
170
....*....|..
gi 1001866046 1070 VVLLDEPTAHLD 1081
Cdd:COG4586 175 ILFLDEPTIGLD 186
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
335-544 |
2.02e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.40 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 335 GHGRVQDAERPPAGQAAPAgLRVAGLTVWyDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-S 413
Cdd:COG3845 239 GREVLLRVEKAPAEPGEVV-LEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSiR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 414 VRG-SVDGPDPRR-----IAWVPQhpqfsERTvaaelalyagaaGEGAVPGEP------------------GALVRELLD 469
Cdd:COG3845 317 LDGeDITGLSPRErrrlgVAYIPE-----DRL------------GRGLVPDMSvaenlilgryrrppfsrgGFLDRKAIR 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 470 QLGLGGLEAAD--------PAE-LSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGR-VTVL 539
Cdd:COG3845 380 AFAEELIEEFDvrtpgpdtPARsLSGGNQQKVILARELSRDPK---LLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVL 456
|
....*
gi 1001866046 540 LVSHE 544
Cdd:COG3845 457 LISED 461
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
143-282 |
2.05e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 44.78 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 143 YLPALVQTAVLPLLVGARILGADWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLG 222
Cdd:cd18543 115 FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFG 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 223 RAAEQRRALGELSRAYKGRTMATLRVAFLSALALELISTISVAVVAVFIGIRLVHGDMTL 282
Cdd:cd18543 195 RERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTL 254
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
956-1082 |
2.28e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 956 GPSGSGKSTLLALLTGFLAPRVGSAAVAG-PVAwcPQE----------SHLF----DSTVRGNLAV-ARDRDHAPSDAE- 1018
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGqPVD--AGDiatrrrvgymSQAFslygELTVRQNLELhARLFHLPAAEIAa 376
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 1019 -LEAVLARVGLLEHVRSLPGGLdarigsrgaflSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDP 1082
Cdd:NF033858 377 rVAEMLERFDLADVADALPDSL-----------PLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
483-543 |
2.30e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 2.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 483 ELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSH 543
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDAD---FYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
481-518 |
2.36e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 44.69 E-value: 2.36e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1001866046 481 PAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLD 518
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPD---FLVFDEPTAGLD 197
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
382-557 |
2.42e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 44.64 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 382 GRVTVLAGPSGSGKTTVLAALAGLVRDGVG----ASVRGSVDGPDPRRIAWVPQ----HPQFSertVAAELALyaGAAGE 453
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGdlfiGEKRMNDVPPAERGVGMVFQsyalYPHLS---VAENMSF--GLKLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 454 GAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALA 533
Cdd:PRK11000 104 GAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS---VFLLDEPLSNLDAALRVQMRIEISRLH 180
|
170 180
....*....|....*....|....*..
gi 1001866046 534 GRV--TVLLVSHEPRTA-ALADRTVEL 557
Cdd:PRK11000 181 KRLgrTMIYVTHDQVEAmTLADKIVVL 207
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
973-1121 |
2.44e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 973 LAPRVGSAAVAGPVAWCPQESHLFDSTVRGNlavarDRDHAPSDAELEAVLARVGLLEHVrslpgGLDARIGSRGA-FLS 1051
Cdd:TIGR00630 421 LAVTVGGKSIADVSELSIREAHEFFNQLTLT-----PEEKKIAEEVLKEIRERLGFLIDV-----GLDYLSLSRAAgTLS 490
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1001866046 1052 GGQRQRLAVARTLLAGAEVVL--LDEPTAHLDPESGLALVAALHGaLAD--RTVVMVTHHATELMPGDTLVRLG 1121
Cdd:TIGR00630 491 GGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKR-LRDlgNTLIVVEHDEDTIRAADYVIDIG 563
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
935-1103 |
3.15e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 935 GPDVLAGLDLAARPGDWIVVAGPSGSGKSTLLALLTGFLAPRVGS--------------AAVAGPVAWCPqESHLFD--- 997
Cdd:PRK11288 265 GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQvyldgkpidirsprDAIRAGIMLCP-EDRKAEgii 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 998 --STVRGNLAVARDRDHAPS----DAELEAVLARvgllEHVRSLpggldaRIGSRGA-----FLSGGQRQRLAVARTLLA 1066
Cdd:PRK11288 344 pvHSVADNINISARRHHLRAgcliNNRWEAENAD----RFIRSL------NIKTPSReqlimNLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 1067 GAEVVLLDEPTAHLD--------------PESGLALVAALHG-----ALADRTVVM 1103
Cdd:PRK11288 414 DMKVILLDEPTRGIDvgakheiynviyelAAQGVAVLFVSSDlpevlGVADRIVVM 469
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
364-557 |
3.55e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.59 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 364 YDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-----SVRGSVDGPDPRR-IAWVPQHP--QF 435
Cdd:PRK13648 17 YQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEifynnQAITDDNFEKLRKhIGIVFQNPdnQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 436 SERTVAAELALyagAAGEGAVPGEP-GALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPT 514
Cdd:PRK13648 97 VGSIVKYDVAF---GLENHAVPYDEmHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS---VIILDEAT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1001866046 515 AHLDDASAALVERAIAALAG--RVTVLLVSHEPRTAALADRTVEL 557
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVM 215
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
165-302 |
3.98e-04 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 43.93 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 165 DWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQRRALGELSRAYKGrtmA 244
Cdd:cd18547 144 SPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYK---A 220
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 245 TLRVAFLSAL---ALELISTISVAVVAVFIGIRLVHGDMTLeaGLLA--LILAPECFQPLRDL 302
Cdd:cd18547 221 SFKAQFYSGLlmpIMNFINNLGYVLVAVVGGLLVINGALTV--GVIQafLQYSRQFSQPINQI 281
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
362-557 |
4.58e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.16 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 362 VWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVrgsVDGPD-----PRR----IAWVPQH 432
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLL---FEGEDistlkPEIyrqqVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 433 PQFSERTVAAELALYAGAAGEGAvpgEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLA---RVadgaglLL 509
Cdd:PRK10247 90 PTLFGDTVYDNLIFPWQIRNQQP---DPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQfmpKV------LL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 510 LDEPTAHLDDASAALVERAIAALA--GRVTVLLVSHEPRTAALADRTVEL 557
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
258-553 |
5.02e-04 |
|
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: 44.04 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 258 LISTISVAVVAVFIGIRLVHGDMTLeaGLLALI--LAPECFQPLRDLGTAHhasedgaealRRTR-ARIGAPRGTVLLAA 334
Cdd:COG5265 271 LIIALGLTAMMLMAAQGVVAGTMTV--GDFVLVnaYLIQLYIPLNFLGFVY----------REIRqALADMERMFDLLDQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 335 gHGRVQDAERPPAGQAAPAGLRVAGLTVWYDgAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTvLAALagLVR--DGVGA 412
Cdd:COG5265 339 -PPEVADAPDAPPLVVGGGEVRFENVSFGYD-PERPILKGVSFEVPAGKTVAIVGPSGAGKST-LARL--LFRfyDVTSG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 413 SVRgsVDGPDPRR---------IAWVPQHPQFSERTVAAELAlYagaagegavpGEPGALVRElldqlglgGLEAADPAE 483
Cdd:COG5265 414 RIL--IDGQDIRDvtqaslraaIGIVPQDTVLFNDTIAYNIA-Y----------GRPDASEEE--------VEAAARAAQ 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 484 ----------------------LSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLV 541
Cdd:COG5265 473 ihdfieslpdgydtrvgerglkLSGGEKQRVAIARTLLK---NPPILIFDEATSALDSRTERAIQAALREVARGRTTLVI 549
|
330
....*....|..
gi 1001866046 542 SHEPRTAALADR 553
Cdd:COG5265 550 AHRLSTIVDADE 561
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
351-543 |
5.10e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.13 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 351 APAGLRVAGLTVWYdgaaePAVGPLD---FTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVG-----------ASVRG 416
Cdd:PRK11288 1 SSPYLSFDGIGKTF-----PGVKALDdisFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGsilidgqemrfASTTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 417 SVDGPdprrIAWVPQHPQFS-ERTVAAELALyagaageGAVPGEPGALVRELLDQLGLGGLEA----ADP----AELSPG 487
Cdd:PRK11288 76 ALAAG----VAIIYQELHLVpEMTVAENLYL-------GQLPHKGGIVNRRLLNYEAREQLEHlgvdIDPdtplKYLSIG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 488 QQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAAL--AGRVtVLLVSH 543
Cdd:PRK11288 145 QRQMVEIAKALAR---NARVIAFDEPTSSLSAREIEQLFRVIRELraEGRV-ILYVSH 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
377-518 |
5.49e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.18 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 377 FTAPAGRVTVLAGPSGSGKTTVLAALAGLVrdgvgASVRGSVDGPDPRRIAWVPQHPQFSER---TVAAELALYAGAAGE 453
Cdd:PRK09544 25 LELKPGKILTLLGPNGAGKSTLVRVVLGLV-----APDEGVIKRNGKLRIGYVPQKLYLDTTlplTVNRFLRLRPGTKKE 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 454 GAVPgepgALVRELLDQLGLGGLEaadpaELSPGQQRRVAVARGLarvADGAGLLLLDEPTAHLD 518
Cdd:PRK09544 100 DILP----ALKRVQAGHLIDAPMQ-----KLSGGETQRVLLARAL---LNRPQLLVLDEPTQGVD 152
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
150-318 |
5.58e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 43.29 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 150 TAVLPLL-VGARILGADWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAEQR 228
Cdd:cd18778 123 TNVLTLVgVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 229 RALGELSRAYkgrTMATLRVAFLSAL---ALELISTISVAVVaVFIGIRLV-HGDMTLeAGLLALILAPECF-QPLRDLG 303
Cdd:cd18778 203 KRFEALSRRY---RKAQLRAMKLWAIfhpLMEFLTSLGTVLV-LGFGGRLVlAGELTI-GDLVAFLLYLGLFyEPITSLH 277
|
170
....*....|....*
gi 1001866046 304 TAHHASEDGAEALRR 318
Cdd:cd18778 278 GLNEMLQRALAGAER 292
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
484-544 |
5.68e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 5.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 484 LSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALAGrvTVLLVSHE 544
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSN---LLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSHD 496
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
355-543 |
6.42e-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: 44.23 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAG--LVRDG----VGASVRGSVDGPDpRRIAW 428
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGdtTVTSGdatvAGKSILTNISDVH-QNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 429 VPQHPQFSERTVAAE-LALYAGAAGegaVPGEPGALVRELLDQLGLGGLEAADPA-ELSPGQQRRVAVARGLARVADgag 506
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREhLYLYARLRG---VPAEEIEKVANWSIQSLGLSLYADRLAgTYSGGNKRKLSTAIALIGCPP--- 2090
|
170 180 190
....*....|....*....|....*....|....*....
gi 1001866046 507 LLLLDEPTAHLDDASAALVERAIAAL--AGRvTVLLVSH 543
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIirEGR-AVVLTSH 2128
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
353-555 |
7.27e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.29 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 353 AGLRVAGLTVWYDGAAePAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGL--VRDG---VGASVRGSVDgPDPRRIA 427
Cdd:PRK11650 2 AGLKLQAVRKSYDGKT-QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLerITSGeiwIGGRVVNELE-PADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 428 WVPQ----HPQFSertVAAELAlYAGAagegaVPGEPGALVRELLDqlglgglEAAD-----------PAELSPGQQRRV 492
Cdd:PRK11650 80 MVFQnyalYPHMS---VRENMA-YGLK-----IRGMPKAEIEERVA-------EAARileleplldrkPRELSGGQRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1001866046 493 AVARglARVADGAgLLLLDEPTAHLDdasAAL-----VEraIAALAGR--VTVLLVSH---EPRTaaLADRTV 555
Cdd:PRK11650 144 AMGR--AIVREPA-VFLFDEPLSNLD---AKLrvqmrLE--IQRLHRRlkTTSLYVTHdqvEAMT--LADRVV 206
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1051-1106 |
7.57e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 7.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1001866046 1051 SGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGLALVAALhgALADRTVVMVTH 1106
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
375-544 |
7.84e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 43.39 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVG----------ASVRGSVDGPDPRRIAWVP-----QHPQFSERT 439
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGtieigetvklAYVDQSRDALDPNKTVWEEisgglDIIKLGKRE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 440 VAAELalYAGAAG-EGavpGEPGALVrelldqlglggleaadpAELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLD 518
Cdd:TIGR03719 421 IPSRA--YVGRFNfKG---SDQQKKV-----------------GQLSGGERNRVHLAKTLKS---GGNVLLLDEPTNDLD 475
|
170 180
....*....|....*....|....*.
gi 1001866046 519 DASAALVERAIAALAGrvTVLLVSHE 544
Cdd:TIGR03719 476 VETLRALEEALLNFAG--CAVVISHD 499
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
337-553 |
8.90e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 337 GR-VQDAERPPAGQAAPAGLRVAGLTVwydgaaEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SV 414
Cdd:COG1129 238 GReLEDLFPKRAAAPGEVVLEVEGLSV------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEiRL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 415 RG-SVDGPDPR-----RIAWVPQ-------HPQFS--ERTVAAELALYAGAageGAVPgePGALVRELLDQLGLGGLEAA 479
Cdd:COG1129 312 DGkPVRIRSPRdairaGIAYVPEdrkgeglVLDLSirENITLASLDRLSRG---GLLD--RRRERALAEEYIKRLRIKTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 480 DP----AELSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHE-PRTAALADR 553
Cdd:COG1129 387 SPeqpvGNLSGGNQQKVVLAKWLAT---DPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVISSElPELLGLSDR 463
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
480-545 |
9.27e-04 |
|
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: 42.76 E-value: 9.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 480 DPAELSPGQQRRVAVARGLARVADGAGLLLLDEPTAHLD-DASAALVERAIAALAGRVTVLLVSHEP 545
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSALPKGGLLLIDEPESGLHpKLLRRLLELLKELSRNGAQLILTTHSP 299
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
355-553 |
9.57e-04 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 42.14 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYdgAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVD---GPDPRR----IA 427
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitkLPMHKRarlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 428 WVPQHPQ-FSERTVAAELAlyagAAGEGAVPGEPGALVRELLDQLGLGGLEAADP--AELSPGQQRRVAVARGLARvadG 504
Cdd:cd03218 79 YLPQEASiFRKLTVEENIL----AVLEIRGLSKKEREEKLEELLEEFHITHLRKSkaSSLSGGERRRVEIARALAT---N 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1001866046 505 AGLLLLDEPTAHLDDASAALVERAIAALAGR-VTVLLVSHEPR-TAALADR 553
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRgIGVLITDHNVReTLSITDR 202
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
357-543 |
1.35e-03 |
|
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: 42.15 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 357 VAGLTVWYDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVrdgvgaSVRG--SVDGPDPRRIA---W--- 428
Cdd:cd03289 5 VKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL------NTEGdiQIDGVSWNSVPlqkWrka 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 429 ---VPQHPQFSERTVAAELALYAGAAGEG--AVPGEPG-ALVRELLDQLGLGGLEAADPAeLSPGQQRRVAVARGlarVA 502
Cdd:cd03289 79 fgvIPQKVFIFSGTFRKNLDPYGKWSDEEiwKVAEEVGlKSVIEQFPGQLDFVLVDGGCV-LSHGHKQLMCLARS---VL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1001866046 503 DGAGLLLLDEPTAHLDDASAALVERAIAALAGRVTVLLVSH 543
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEH 195
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
146-290 |
1.41e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 42.08 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 146 ALVQTAVLPLLVGARILGADWVSALILVLTLPLVPVFMILIGRHTLEAVAEaQQSLLRlgSHLVELAQGLPVLVGLGRAA 225
Cdd:cd18585 119 ALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLGKKIGQQLVQ-LRAELR--TELVDGLQGMAELLIFGALE 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001866046 226 EQRRALGELSRAYkgrTMATLRVAFLSALALELISTIS-VAVVAV-FIGIRLVHGDmTLEAGLLALI 290
Cdd:cd18585 196 RQRQQLEQLSDAL---IKEQRRLARLSGLSQALMILLSgLTVWLVlWLGAPLVQNG-ALDGALLAML 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
341-518 |
1.42e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.77 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 341 DAERPPAGQAAPAGLRVAGLTVWYDG---------AAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDgvg 411
Cdd:PRK15134 262 SGDPVPLPEPASPLLDVEQLQVAFPIrkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS--- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 412 asvRGSV--DG------------PDPRRIAWVPQHPQFSERTVAAELALYAgaagEGAVPGEPGALVRELLDQLGLGGLE 477
Cdd:PRK15134 339 ---QGEIwfDGqplhnlnrrqllPVRHRIQVVFQDPNSSLNPRLNVLQIIE----EGLRVHQPTLSAAQREQQVIAVMEE 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1001866046 478 AA--------DPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLD 518
Cdd:PRK15134 412 VGldpetrhrYPAEFSGGQRQRIAIARALILKPS---LIILDEPTSSLD 457
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
364-553 |
1.48e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 41.90 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 364 YDGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASvrgSVDG--------PDPR-RIAWVPQHP- 433
Cdd:PRK13632 17 YPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI---KIDGitiskenlKEIRkKIGIIFQNPd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 434 -QFSERTVAAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDE 512
Cdd:PRK13632 94 nQFIGATVEDDIAF--GLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE---IIIFDE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1001866046 513 PTAHLDDASAALVERAIAALA--GRVTVLLVSHEPRTAALADR 553
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRktRKKTLISITHDMDEAILADK 211
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
382-553 |
1.60e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.63 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 382 GRVTVLAGPSGSGKTTVLAALAGLVRDgvgasvRGSVDGPDPRRIAWVPQHpqfsertvaaelalyagaagegavpgepg 461
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIP------NGDNDEWDGITPVYKPQY----------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 462 alvrelldqlglggleaadpAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALVERAIAALA--GRVTVL 539
Cdd:cd03222 70 --------------------IDLSGGELQRVAIAAALLRNAT---FYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTAL 126
|
170
....*....|....*
gi 1001866046 540 LVSHEPRTAA-LADR 553
Cdd:cd03222 127 VVEHDLAVLDyLSDR 141
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
371-544 |
1.63e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 41.69 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 371 AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVG----------ASVRGSVDGPDPRRIAWVPQHP--QFSER 438
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvddititHKTKDKYIRPVRKRIGMVFQFPesQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 439 TVAAELALYagaagegavPGEPGALVRELLDQLGLGGLE--------AADPAELSPGQQRRVAVARGLARVADgagLLLL 510
Cdd:PRK13646 102 TVEREIIFG---------PKNFKMNLDEVKNYAHRLLMDlgfsrdvmSQSPFQMSGGQMRKIAIVSILAMNPD---IIVL 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1001866046 511 DEPTAHLDDASAALVERAIAALA--GRVTVLLVSHE 544
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHD 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
371-550 |
2.06e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 41.37 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 371 AVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRG------SVDGPDPRR--IAWVPQHP--QFSERTV 440
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpidySRKGLMKLResVGMVFQDPdnQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 441 AAELALyaGAAGEGAVPGEPGALVRELLDQLGLGGLEAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDA 520
Cdd:PRK13636 101 YQDVSF--GAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK---VLVLDEPTAGLDPM 175
|
170 180 190
....*....|....*....|....*....|..
gi 1001866046 521 SAALVERAIAALAGR--VTVLLVSHEPRTAAL 550
Cdd:PRK13636 176 GVSEIMKLLVEMQKElgLTIIIATHDIDIVPL 207
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
387-544 |
2.14e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 387 LAGPSGSGKTTVLAALAGLVRDGVGASVRGSvdgpdPRRIAWVPQHpQFSERTVAAELALYAGAAgegaVPGEPGALVRE 466
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRSA-----KVRMAVFSQH-HVDGLDLSSNPLLYMMRC----FPGVPEQKLRA 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 467 LLDQLGLGGLEAADPA-ELSPGQQRRVAVARglaRVADGAGLLLLDEPTAHLD-DASAALVERAIAALAGrvtVLLVSHE 544
Cdd:PLN03073 610 HLGSFGVTGNLALQPMyTLSGGQKSRVAFAK---ITFKKPHILLLDEPSNHLDlDAVEALIQGLVLFQGG---VLMVSHD 683
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
141-303 |
2.27e-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: 41.34 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 141 TQYLPALVQTAVLPLLVGARILGA--------DWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELA 212
Cdd:cd18564 121 VGAIQDLLVSGVLPLLTNLLTLVGmlgvmfwlDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 213 QGLPVLVGLGRAAEQRRALGELSRAYKGRTMATLRVAFLSALALELISTISVAVVAVFIGIRLVHGDMTLEAGLLALILA 292
Cdd:cd18564 201 SAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYL 280
|
170
....*....|.
gi 1001866046 293 PECFQPLRDLG 303
Cdd:cd18564 281 KNLYKPVRDLA 291
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1039-1081 |
2.28e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.91 E-value: 2.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1001866046 1039 LDARIGsrgaFLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLD 1081
Cdd:PRK10762 389 MEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
333-557 |
2.28e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 333 AAGHGrvQDAERPPAGQAAPAGLRVAGLTVWYDGA---AEPAVGPLDFTA--PAGRVTVLAGPSGSGKTTVLAALAGL-- 405
Cdd:PTZ00243 634 ASRHI--VEGGTGGGHEATPTSERSAKTPKMKTDDffeLEPKVLLRDVSVsvPRGKLTVVLGATGSGKSTLLQSLLSQfe 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 406 VRDG-VGASvrgsvdgpdpRRIAWVPQHPQFSERTV-----------AAELALYAGAAG-EGAVPGEPGALVRELldqlg 472
Cdd:PTZ00243 712 ISEGrVWAE----------RSIAYVPQQAWIMNATVrgnilffdeedAARLADAVRVSQlEADLAQLGGGLETEI----- 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 473 lggleAADPAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALV--ERAIAALAGRvTVLLVSHEPRTAAL 550
Cdd:PTZ00243 777 -----GEKGVNLSGGQKARVSLARAVYANRD---VYLLDDPLSALDAHVGERVveECFLGALAGK-TRVLATHQVHVVPR 847
|
....*..
gi 1001866046 551 ADRTVEL 557
Cdd:PTZ00243 848 ADYVVAL 854
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
375-552 |
2.61e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.90 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGPDPRRIAWVPQHPQFSERTVAAELALYAGAAGEG 454
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 455 AVP-GEPGALVRELLDQLGLGGLEAAD--------PAELSPGQQRRVAVARGLARVADgagLLLLDEPTAHLDDASAALV 525
Cdd:PRK11831 106 AYPlREHTQLPAPLLHSTVMMKLEAVGlrgaaklmPSELSGGMARRAALARAIALEPD---LIMFDEPFVGQDPITMGVL 182
|
170 180 190
....*....|....*....|....*....|
gi 1001866046 526 ERAIAAL--AGRVTVLLVSHE-PRTAALAD 552
Cdd:PRK11831 183 VKLISELnsALGVTCVVVSHDvPEVLSIAD 212
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
375-403 |
3.04e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 3.04e-03
10 20
....*....|....*....|....*....
gi 1001866046 375 LDFTAPAgRVTVLAGPSGSGKTTVLAALA 403
Cdd:COG3950 19 IDFDNPP-RLTVLVGENGSGKTTLLEAIA 46
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
372-553 |
3.20e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 40.65 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 372 VGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGasvRGSVDGPD----------PRRIAWVPQHPQFSERtva 441
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAG---NIIIDDEDisllplharaRRGIGYLPQEASIFRR--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 442 aeLALYAGAAgegAVPGEPGALVRELLDQLGLGGLEAADPAE--------LSPGQQRRVAVARGLARvadGAGLLLLDEP 513
Cdd:PRK10895 93 --LSVYDNLM---AVLQIRDDLSAEQREDRANELMEEFHIEHlrdsmgqsLSGGERRRVEIARALAA---NPKFILLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1001866046 514 TAHLDDASAALVERAIAALAGR-VTVLLVSHEPR-TAALADR 553
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVReTLAVCER 206
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
373-518 |
3.26e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.01 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 373 GPLDFTA----PAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGS---VDG-------PDPRRIAWVPQ-HPQFSE 437
Cdd:PRK11144 11 GDLCLTVnltlPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAekgiclpPEKRRIGYVFQdARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 438 RTVAAELaLYAGAAgegAVPGEPGALVR----ELLDQLGlggleaadPAELSPGQQRRVAVARGLARVADgagLLLLDEP 513
Cdd:PRK11144 91 YKVRGNL-RYGMAK---SMVAQFDKIVAllgiEPLLDRY--------PGSLSGGEKQRVAIGRALLTAPE---LLLMDEP 155
|
....*
gi 1001866046 514 TAHLD 518
Cdd:PRK11144 156 LASLD 160
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
359-552 |
3.62e-03 |
|
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: 40.39 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 359 GLTVWydGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGAsVRGSVDGPDPRRIAWVPQHPQFSER 438
Cdd:cd03290 6 GYFSW--GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK-VHWSNKNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 439 TVAAELALYAGAAGEGAVPGEP------GALVRELLDQLGLGGLEAADPAE-------LSPGQQRRVAVARGLARvadGA 505
Cdd:cd03290 83 YAAQKPWLLNATVEENITFGSPfnkqryKAVTDACSLQPDIDLLPFGDQTEigerginLSGGQRQRICVARALYQ---NT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1001866046 506 GLLLLDEPTAHLD-DASAALVERAIAALA--GRVTVLLVSHEPRTAALAD 552
Cdd:cd03290 160 NIVFLDDPFSALDiHLSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHAD 209
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
382-402 |
3.72e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 39.67 E-value: 3.72e-03
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1038-1106 |
3.77e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.68 E-value: 3.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001866046 1038 GLD-ARIGSRGAFLSGGQRQRLAVARTLL---AGAEVVLLDEPTAHLDPESGLALVAALHgALADR--TVVMVTH 1106
Cdd:cd03271 157 GLGyIKLGQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQ-RLVDKgnTVVVIEH 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
375-543 |
3.87e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 40.58 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 375 LDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGA-SVRGSVDGPDP---------RRIAWVPQHP--QFSERTVAA 442
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTiTIAGYHITPETgnknlkklrKKVSLVFQFPeaQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 443 ELALyaGAAGEGAVPGEP-GALVRELLDQLGLGGLEAADPAELSPGQQRRVAVArglARVADGAGLLLLDEPTAHLD-DA 520
Cdd:PRK13641 106 DVEF--GPKNFGFSEDEAkEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIA---GVMAYEPEILCLDEPAAGLDpEG 180
|
170 180
....*....|....*....|...
gi 1001866046 521 SAALVERAIAALAGRVTVLLVSH 543
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTH 203
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
147-282 |
4.44e-03 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 40.49 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 147 LVQTAVLPLLVGARILGADWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELAQGLPVLVGLGRAAE 226
Cdd:cd18542 120 LVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDY 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1001866046 227 QRRALGELSRAYKGRTMatlRVAFLSAL---ALELISTISVAVVAVFIGIRLVHGDMTL 282
Cdd:cd18542 200 EIEKFDKENEEYRDLNI---KLAKLLAKywpLMDFLSGLQIVLVLWVGGYLVINGEITL 255
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
53-456 |
4.61e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.16 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 53 LSAATLVAAAGVLLRAAAEWGTSTVGRWAAVGVKEELRsQLLEAALEGGAAPASAAGPVDDGAARVASSPAATAVLAGRG 132
Cdd:COG3903 528 LRAALRWALAHGDAELALRLAAALAPFWFLRGLLREGR-RWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAA 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 133 LDGLDALYTQYLPALVQTAVLPLLVGARILGADWVSALILVLTLPLVPVFMILIGRHTLEAVAEAQQSLLRLGSHLVELA 212
Cdd:COG3903 607 AAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAA 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 213 QGLPVLVGLGRAAEQRRALGELSRAYKGRTMATLRVAFLSALALELISTISVAVVAVFIGIRLVHGDMTLEAGLLALILA 292
Cdd:COG3903 687 LAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAA 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 293 PECFQPLRDLGTAHHASEDGAEALRRTRARIGAPRGTVLLAAGHGRVQDAERPPAGQAAPAGLRVAGLTVWYDGAAEPAV 372
Cdd:COG3903 767 AAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAA 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 373 GPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGVGASVRGSVDGPDPRRIAWVPQHPQFSERTVAAELALYAGAAG 452
Cdd:COG3903 847 AAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAA 926
|
....
gi 1001866046 453 EGAV 456
Cdd:COG3903 927 AAAA 930
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
941-1110 |
4.68e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 941 GLDLAARPGDWIVVAGPSGSgkstllALLTGFLAprvgsAAVAGPVA---------WCPQESHLFDS------------- 998
Cdd:NF000106 31 GVDLDVREGTVLGVLGP*GA------A**RGALP-----AHV*GPDAgrrpwrf*tWCANRRALRRTig*hrpvr*grre 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 999 --TVRGNL-AVARDRDHAPSDAELEA--VLARVGLLEHVrslpggldariGSRGAFLSGGQRQRLAVARTLLAGAEVVLL 1073
Cdd:NF000106 100 sfSGRENLyMIGR*LDLSRKDARARAdeLLERFSLTEAA-----------GRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1001866046 1074 DEPTAHLDPESGLALVAALHGALADRTVVMVTHHATE 1110
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYME 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
355-518 |
5.05e-03 |
|
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: 40.82 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 355 LRVAGLTVWYDGAAE--PAVGPLDFTAPAGRVTVLAGPSGSGKT-TVLAALaGLVRDGvGASVRGSV--DG------PDP 423
Cdd:COG4172 7 LSVEDLSVAFGQGGGtvEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDP-AAHPSGSIlfDGqdllglSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 424 -------RRIAWVPQHPQFS-------ERTVAAELALYAGAAGEGAVpgepgALVRELLDQLGLGGLE---AADPAELSP 486
Cdd:COG4172 85 elrrirgNRIAMIFQEPMTSlnplhtiGKQIAEVLRLHRGLSGAAAR-----ARALELLERVGIPDPErrlDAYPHQLSG 159
|
170 180 190
....*....|....*....|....*....|..
gi 1001866046 487 GQQRRVAVARGLARVADgagLLLLDEPTAHLD 518
Cdd:COG4172 160 GQRQRVMIAMALANEPD---LLIADEPTTALD 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
938-1081 |
5.21e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.84 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 938 VLAGLDLAARPGDWIVVAGPSGSGKS-TLLALLTGFLAPRV----GSAAVAGPVAWCPQESHLfdSTVRGN--------- 1003
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLHASEQTL--RGVRGNkiamifqep 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1004 -----------------LAVARDRDHAPSDAELEAVLARVGLLEHVRslpggldaRIGSRGAFLSGGQRQRLAVARTLLA 1066
Cdd:PRK15134 102 mvslnplhtlekqlyevLSLHRGMRREAARGEILNCLDRVGIRQAAK--------RLTDYPHQLSGGERQRVMIAMALLT 173
|
170
....*....|....*
gi 1001866046 1067 GAEVVLLDEPTAHLD 1081
Cdd:PRK15134 174 RPELLIADEPTTALD 188
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
11-405 |
5.74e-03 |
|
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: 40.55 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 11 SRRALVLLGVLAAAKAVGL-ALVAQGVASGLAALAAGAVRPGVLSAATLVAaagvllRAAAEWGTSTVGRwaavGVKEEL 89
Cdd:COG4615 14 LLLLALLLGLLSGLANAGLiALINQALNATGAALARLLLLFAGLLVLLLLS------RLASQLLLTRLGQ----HAVARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 90 RSQLLE-------AALEGGaapasaagpvddGAARVasspaatavlagrgldgLDALyTQYLPALVQTAV-LPLLV--GA 159
Cdd:COG4615 84 RLRLSRrilaaplERLERI------------GAARL-----------------LAAL-TEDVRTISQAFVrLPELLqsVA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 160 RILGA-------DWVSALILVLTLPL-VPVFMILIGR--HTLEAVAEAQQSLLRLGSHLVELAQGLpvlvGLGRAAEQR- 228
Cdd:COG4615 134 LVLGClaylawlSPPLFLLTLVLLGLgVAGYRLLVRRarRHLRRAREAEDRLFKHFRALLEGFKEL----KLNRRRRRAf 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 229 --RALGELSRAYKGRTMATLRVaFLSALALELISTISVAVVAVFIGIRLVHGDMTLEAGLLALIL---AP--ECFQPLRD 301
Cdd:COG4615 210 fdEDLQPTAERYRDLRIRADTI-FALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFVLVLLflrGPlsQLVGALPT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 302 LGTAHHAsedgAEALRRTRARIGAPRgtvllaaghgRVQDAERPPAGQAAPAGLRVAGLTVWYDGAAEP---AVGPLDFT 378
Cdd:COG4615 289 LSRANVA----LRKIEELELALAAAE----------PAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegfTLGPIDLT 354
|
410 420
....*....|....*....|....*..
gi 1001866046 379 APAGRVTVLAGPSGSGKTTVLAALAGL 405
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGL 381
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1043-1127 |
6.10e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 1043 IGSrgafLSGGQRQRLAVARTLLAGAEVVLLDEPTAHLDPESGL---ALVAALhgALADRTVVMVTHHATELmpgdtlvr 1119
Cdd:PRK10982 389 IGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFeiyQLIAEL--AKKDKGIIIISSEMPEL-------- 454
|
....*...
gi 1001866046 1120 LGARERVL 1127
Cdd:PRK10982 455 LGITDRIL 462
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
483-557 |
6.15e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.91 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 483 ELSPGQQRRVAVARGLARVADGAGLLLLDEPTA--HLDDasaalVERAIAALAGRV----TVLLVSHEPRTAALADRTVE 556
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTGKTLYILDEPTTglHFHD-----VKKLLEVLQRLVdkgnTVVVIEHNLDVIKCADWIID 243
|
.
gi 1001866046 557 L 557
Cdd:cd03271 244 L 244
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
352-553 |
7.12e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 39.68 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 352 PAGLRVAGLTVwydGAAEPAVGPLDFTAPAGRVTVLAGPSGSGKTTVLAALAGLVRDGV---------------GASVRG 416
Cdd:PRK10418 2 PQQIELRNIAL---QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVrqtagrvlldgkpvaPCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001866046 417 svdgpdpRRIAWVPQHPQFS---ERTVAAElalyagAAGEGAVPGEPGALVRELLDQLGLGGLEAAD-----PAELSPGQ 488
Cdd:PRK10418 79 -------RKIATIMQNPRSAfnpLHTMHTH------ARETCLALGKPADDATLTAALEAVGLENAARvlklyPFEMSGGM 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001866046 489 QRRVAVArgLARVADgAGLLLLDEPTAHLDDASAALVERAIAALAGR--VTVLLVSHEPRTAA-LADR 553
Cdd:PRK10418 146 LQRMMIA--LALLCE-APFIIADEPTTDLDVVAQARILDLLESIVQKraLGMLLVTHDMGVVArLADD 210
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
484-543 |
7.30e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 7.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001866046 484 LSPGQQRRVAVARGLARvadGAGLLLLDEPTAHLDDASAALVERAIAALA--GRVTVLLVSH 543
Cdd:PRK10938 402 LSWGQQRLALIVRALVK---HPTLLILDEPLQGLDPLNRQLVRRFVDVLIseGETQLLFVSH 460
|
|
| |
