|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-573 |
0e+00 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 935.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 1 MRDLLPYIKLYKKHWFGLTLGMLLSFATLFASIGLLTISGWFISASAIAGLTIArETFNYMLPAGAVRGFSIGRTAGRWG 80
Cdd:PRK11160 1 MRALLPFLKLYKRHWFMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGL-YSFNYMLPAAGVRGAAIGRTAGRYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 81 ERVVSHNATFKLLTELRIFFFKKLIPLIPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPIIVGTLGIIGLTAFLAWFD 160
Cdd:PRK11160 80 ERLVSHDATFRVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 161 ITIGLTLGAILLSLLLIWPTLFYKLGKHNGSELTQNKATLRIKTLDWLQGNAELRIFGAEAQYRQRILDAQTALLANQHR 240
Cdd:PRK11160 160 LTLALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 241 MAALTGLANGLLLLANGWTLLLMLWIAGDGIAGMT-PDPMVAMVAFATMASFELLMPIAGAFQYLGQTLSSARRLNEIIT 319
Cdd:PRK11160 240 QANLTGLSQALMILANGLTVVLMLWLAAGGVGGNAqPGALIALFVFAALAAFEALMPVAGAFQHLGQVIASARRINEITE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 320 AEPDTVFDENGVDQAIKGNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAI 399
Cdd:PRK11160 320 QKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 400 DGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEAL-TTDEGLNAWLGDGGRQLSGG 478
Cdd:PRK11160 400 NGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLlEDDKGLNAWLGEGGRQLSGG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 479 ERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDS 558
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQE 559
|
570
....*....|....*
gi 1906086718 559 LLSLKGAYHQLWQRF 573
Cdd:PRK11160 560 LLAQQGRYYQLKQRL 574
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-572 |
0e+00 |
|
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: 702.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 2 RDLLPYIKLYKKHWFGLTLGMLLSFATLFASIGLLTISGWFISASAIAGLTiaretFNYMLPAGAVRGFSIGRTAGRWGE 81
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPPI-----LNLFVPIVGVRAFAIGRTVFRYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 82 RVVSHNATFKLLTELRIFFFKKLIPLIPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPIIVGTLGIIGLTAFLAWFDI 161
Cdd:COG4987 76 RLVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 162 TIGLTLGAILLSLLLIWPTLFYKLGKHNGSELTQNKATLRIKTLDWLQGNAELRIFGAEAQYRQRILDAQTALLANQHRM 241
Cdd:COG4987 156 ALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 242 AALTGLANGLLLLANGWTLLLMLWIAGDGIA-GMTPDPMVAMVAFATMASFELLMPIAGAFQYLGQTLSSARRLNEIITA 320
Cdd:COG4987 236 ARLSALAQALLQLAAGLAVVAVLWLAAPLVAaGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 321 EPDTVFDENGVDQAIKGNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAID 400
Cdd:COG4987 316 PPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 401 GVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEAL--TTDEGLNAWLGDGGRQLSGG 478
Cdd:COG4987 396 GVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWlaALPDGLDTWLGEGGRRLSGG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 479 ERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDS 558
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEE 555
|
570
....*....|....
gi 1906086718 559 LLSLKGAYHQLWQR 572
Cdd:COG4987 556 LLAQNGRYRQLYQR 569
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-533 |
1.91e-130 |
|
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: 391.72 E-value: 1.91e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 4 LLPYIKLYKKHWFGLTLGMLLSFATLFASIGLLTISGWFISASAIAGLTIAretfnYMLPAGAVRGFSIGRTAGRWGERV 83
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLY-----LSVAAVAVRAFGIGRAVFRYLERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 84 VSHNATFKLLTELRIFFFKKLIPLIPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPIIVGTLGIIGLTAFLAWFDITI 163
Cdd:TIGR02868 76 VGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 164 GLTLGAILLSLLLIWPTLFYKLGKHNGSELTQNKATLRIKTLDWLQGNAELRIFGAEAQYRQRILDAQTALLANQHRMAA 243
Cdd:TIGR02868 156 ALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 244 LTGLANGLLLLANGWTLLLMLWIAGDGIAGMTPDPMV-AMVAFATMASFELLMPIAGAFQYLGQTLSSARRLNEIITAE- 321
Cdd:TIGR02868 236 ATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTlAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAg 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 322 --PDTVFDENGVDQAIKGNLTISNVDYQYmDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAI 399
Cdd:TIGR02868 316 pvAEGSAPAAGAVGLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 400 DGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEAL--TTDEGLNAWLGDGGRQLSG 477
Cdd:TIGR02868 395 DGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWlrALPDGLDTVLGEGGARLSG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 478 GERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRL 533
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
25-315 |
1.77e-127 |
|
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: 375.28 E-value: 1.77e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 25 SFATLFASIGLLTISGWFISASAIAGLTIAreTFNYMLPAGAVRGFSIGRTAGRWGERVVSHNATFKLLTELRIFFFKKL 104
Cdd:cd18585 1 GLLTLLASIGLLALSGWFISAAALAGLAAP--TFNYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 105 IPLIPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPIIVGTLGIIGLTAFLAWFDITIGLTLGAILLSLLLIWPTLFYK 184
Cdd:cd18585 79 EPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 185 LGKHNGSELTQNKATLRIKTLDWLQGNAELRIFGAEAQYRQRILDAQTALLANQHRMAALTGLANGLLLLANGWTLLLML 264
Cdd:cd18585 159 LGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 265 WIAGDGI-AGMTPDPMVAMVAFATMASFELLMPIAGAFQYLGQTLSSARRLN 315
Cdd:cd18585 239 WLGAPLVqNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRLF 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-572 |
3.15e-116 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 356.78 E-value: 3.15e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 1 MRDLLPYIKLYKKHwfgLTLGMLLSFATLFASIGLLTISGWFISAsaiaglTIARETFNYMLP-AGAVRGFSIGRTAGRW 79
Cdd:COG1132 9 LRRLLRYLRPYRGL---LILALLLLLLSALLELLLPLLLGRIIDA------LLAGGDLSALLLlLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 80 GERVVSHNATFKLLTELRIFFFKKLIPLIPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPIIVGTLGIIGLTAFLAWF 159
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 160 DITigLTLGAILLSLLLIWPTLFY-KLGKHNGSELTQNKATLRIKTLDWLQGNAELRIFGAEAQYRQRILDAQTALLANQ 238
Cdd:COG1132 160 DWR--LALIVLLVLPLLLLVLRLFgRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 239 HRMAALTGLANGLLLLANGWTLLLMLWIAGDGIAG--MTPDPMVAMVAFATMAsFELLMPIAGAFQYLGQTLSSARRLNE 316
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSgsLTVGDLVAFILYLLRL-FGPLRQLANVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 317 IITAEPDTVFDENGVD-QAIKGNLTISNVDYQYmDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSG 395
Cdd:COG1132 317 LLDEPPEIPDPPGAVPlPPVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 396 YIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGL----EALttDEGLNAWLGDG 471
Cdd:COG1132 396 RILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAhefiEAL--PDGYDTVVGER 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 472 GRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIV 551
Cdd:COG1132 474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
570 580
....*....|....*....|.
gi 1906086718 552 EQGTHDSLLSLKGAYHQLWQR 572
Cdd:COG1132 554 EQGTHEELLARGGLYARLYRL 574
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-572 |
4.54e-91 |
|
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: 294.82 E-value: 4.54e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 2 RDLLPYIKLYKKH-WFGLTLGMLLSFATLFASIGLLTISGWFISASAIAGLTIAretfnymlpAGAVRGFSIGRTAGRWG 80
Cdd:COG2274 145 RWFLRLLRRYRRLlLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVL---------AIGLLLALLFEGLLRLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 81 ERVVSHNATFKLLTELRIFFFKKLIPLIPGRFSKLRDADLLNRLvadvdaMDHVYLR------LVSPIIVGTLGIIGLtA 154
Cdd:COG2274 216 RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF------RDVESIRefltgsLLTALLDLLFVLIFL-I 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 155 FLAWFDITIGL-TLGAILLSLLLIWptLFYKLGKHNGSELTQNKATLRIKTLDWLQGNAELRIFGAEAQYRQRILDAQTA 233
Cdd:COG2274 289 VLFFYSPPLALvVLLLIPLYVLLGL--LFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 234 LLANQHRMAALTGLANGLLLLANGWTLLLMLWIAGDG-IAG-MTpdpMVAMVAFATMASFeLLMPI---AGAFQYLGQTL 308
Cdd:COG2274 367 YLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLvIDGqLT---LGQLIAFNILSGR-FLAPVaqlIGLLQRFQDAK 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 309 SSARRLNEIITAEPDTVFDENGVDQ-AIKGNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLT 387
Cdd:COG2274 443 IALERLDDILDLPPEREEGRSKLSLpRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 388 RQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTTD--EGLN 465
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEAlpMGYD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 466 AWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLM 545
Cdd:COG2274 603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVL 682
|
570 580
....*....|....*....|....*..
gi 1906086718 546 DHGEIVEQGTHDSLLSLKGAYHQLWQR 572
Cdd:COG2274 683 DKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-564 |
5.63e-88 |
|
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: 282.80 E-value: 5.63e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 2 RDLLPYIKLYKKHwfgLTLGMLLSFATLFASIGLLtisgWFIsASAIAGLTIARETFNYMLPA-GAVRGFSIGRTAGRWG 80
Cdd:COG4988 6 KRLKRLARGARRW---LALAVLLGLLSGLLIIAQA----WLL-ASLLAGLIIGGAPLSALLPLlGLLLAVLLLRALLAWL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 81 ERVVSHNATFKLLTELRIFFFKKLIPLIPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPIIVGTLGIIGLTAFLAWFD 160
Cdd:COG4988 78 RERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 161 ITIGLTLGAillsllliwpT-----LFY--------KLGKHNGSELTQNKATLriktLDWLQGNAELRIFGAEAQYRQRI 227
Cdd:COG4988 158 WLSGLILLV----------TaplipLFMilvgkgaaKASRRQWRALARLSGHF----LDRLRGLTTLKLFGRAKAEAERI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 228 ldaqtALLANQHR---MAALTGlangllllangwTLL--LMLwiagDGIAGMTpdpmVAMVAFatMASFELL---MPIAG 299
Cdd:COG4988 224 -----AEASEDFRkrtMKVLRV------------AFLssAVL----EFFASLS----IALVAV--YIGFRLLggsLTLFA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 300 AF-------------QYLG-------QTLSSARRLNEIITAEPDTVFDENGVDQAIKGN-LTISNVDYQYmDADTNAINA 358
Cdd:COG4988 277 ALfvlllapefflplRDLGsfyharaNGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPsIELEDVSFSY-PGGRPALDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLAD 438
Cdd:COG4988 356 LSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 439 DTASDEKLIKTLNQVGLEALTTD--EGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSV 516
Cdd:COG4988 436 PDASDEELEAALEAAGLDEFVAAlpDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1906086718 517 LNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKG 564
Cdd:COG4988 516 LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-569 |
1.12e-68 |
|
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: 232.30 E-value: 1.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 2 RDLLPYIKLYKKHWFGLTLGMLLSFAT--LFASIGLLTISGWFISASAIAGLTiaretfnymLPAGAVrGFSIGRTAGRW 79
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATesTLAALLKPLLDDGFGGRDRSVLWW---------VPLVVI-GLAVLRGICSF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 80 GERVVSHNATFKLLTELRIFFFKKLIPLIPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPIIVGTLGIIGLTAFLAWF 159
Cdd:TIGR02203 73 VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 160 DITIGLTLGAILLSLLLIwPTLFYKLGKHNGSELTQNKATLRIKTLDWLQGNAELRIFGAEAQYRQRILDAQTALLANQH 239
Cdd:TIGR02203 153 SWQLTLIVVVMLPVLSIL-MRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 240 RM----AALTGLANGLLLLANGWTLLLMLWIAGDG--IAGMTPDPMVAMVAFatMASFELLMPIAGAFQylgQTLSSARR 313
Cdd:TIGR02203 232 KMtsagSISSPITQLIASLALAVVLFIALFQAQAGslTAGDFTAFITAMIAL--IRPLKSLTNVNAPMQ---RGLAAAES 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 314 LNEIITAEPDTvfDENGVD-QAIKGNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDP 392
Cdd:TIGR02203 307 LFTLLDSPPEK--DTGTRAiERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 393 KSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLAD-DTASDEKLIKTLNQVGLEALT--TDEGLNAWLG 469
Cdd:TIGR02203 385 DSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVdkLPLGLDTPIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 470 DGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGE 549
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570 580
....*....|....*....|
gi 1906086718 550 IVEQGTHDSLLSLKGAYHQL 569
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQL 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
339-570 |
1.07e-66 |
|
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: 216.33 E-value: 1.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTT--DEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIV 496
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMelPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 497 LLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQLW 570
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
339-554 |
2.02e-66 |
|
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: 213.71 E-value: 2.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESsLRSAMSV 418
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNGSLRDNLlladdtasdekliktlnqvglealttdeglnawlgdgGRQLSGGERRRIGIARALLHDAPIVLL 498
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 499 DEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQG 554
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
342-572 |
2.97e-63 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 207.47 E-value: 2.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 342 SNVDYQYmDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQ 421
Cdd:cd03253 4 ENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 422 RVDILNGSLRDNLLLADDTASDEKLIKT--LNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLD 499
Cdd:cd03253 83 DTVLFNDTIGYNIRYGRPDATDEEVIEAakAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 500 EPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQLWQR 572
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
339-549 |
1.25e-62 |
|
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: 203.38 E-value: 1.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNGSLRDNLLladdtasdekliktlnqvglealttdeglnawlgdggrqlSGGERRRIGIARALLHDAPIVLL 498
Cdd:cd03228 81 VPQDPFLFSGTIRENIL----------------------------------------SGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 499 DEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGE 549
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
340-572 |
3.43e-62 |
|
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: 204.70 E-value: 3.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 340 TISNVDYQYMD-ADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:cd03249 2 EFKNVSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTTD--EGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIV 496
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSlpDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 497 LLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQLWQR 572
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
279-565 |
7.58e-61 |
|
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: 213.57 E-value: 7.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 279 MVAMVAfATMASFELLMP---IAGAFQYLGQTLSSARRLNEIITAEPDTVFDENGVDQ-AIKGNLTISNVDYQYMDADTN 354
Cdd:TIGR03375 401 MGGLIA-CVMLSGRALAPlgqLAGLLTRYQQAKTALQSLDELMQLPVERPEGTRFLHRpRLQGEIEFRNVSFAYPGQETP 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNL 434
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNI 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 435 LLADDTASDEKLIKTLNQVGLEALTTD--EGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQ 512
Cdd:TIGR03375 560 ALGAPYADDEEILRAAELAGVTEFVRRhpDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEER 639
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 513 IMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLS-LKGA 565
Cdd:TIGR03375 640 FKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLEaLRKG 693
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
337-564 |
2.07e-60 |
|
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: 199.76 E-value: 2.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 337 GNLTISNVDYQYmDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAM 416
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEAL--TTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAP 494
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFimKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 495 IVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKG 564
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
337-554 |
3.08e-59 |
|
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: 196.27 E-value: 3.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 337 GNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAM 416
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTTDE--GLNAWLGDGGRQLSGGERRRIGIARALLHDAP 494
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHpnGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 495 IVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQG 554
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
64-569 |
9.48e-59 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 205.70 E-value: 9.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 64 AGAVRGFSIGRTagrwGERVVshnatfkllTELRIFFFKKLIPLIPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPII 143
Cdd:TIGR02204 74 GTAARFYLVTWL----GERVV---------ADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 144 VGTLGIIGltAFLAWFDITIGLTLGAILLSLLLIWPTLFY-----KLGKHNGSELTQNKA----TLR-IKTLdwlqgnae 213
Cdd:TIGR02204 141 RNALMCIG--GLIMMFITSPKLTSLVLLAVPLVLLPILLFgrrvrKLSRESQDRIADAGSyageTLGaIRTV-------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 214 lRIFGAEAQYRQRILDA-QTALLANQHRMAALTGLANGLLLLANGwTLLLMLWIAG-DGIAG-MTPDPMVAMVAFATMA- 289
Cdd:TIGR02204 211 -QAFGHEDAERSRFGGAvEKAYEAARQRIRTRALLTAIVIVLVFG-AIVGVLWVGAhDVIAGkMSAGTLGQFVFYAVMVa 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 290 -SFELLMPIAGAFQylgQTLSSARRLNEIITAEPDTVFDENGVD--QAIKGNLTISNVDYQY-MDADTNAINAISLDLLS 365
Cdd:TIGR02204 289 gSIGTLSEVWGELQ---RAAGAAERLIELLQAEPDIKAPAHPKTlpVPLRGEIEFEQVNFAYpARPDQPALDGLNLTVRP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 366 GQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADDTASDEK 445
Cdd:TIGR02204 366 GETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 446 LIKTLNQVG----LEALttDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHI 521
Cdd:TIGR02204 446 VEAAARAAHahefISAL--PEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLM 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1906086718 522 EHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQL 569
Cdd:TIGR02204 524 KGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-545 |
3.15e-58 |
|
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: 202.90 E-value: 3.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 18 LTLGMLLSFATLFASIglltISGWFISASAIAGLTIAretfnymlpAGAVRGFSIGRTAGRWGERVVSHNATFKLLTELR 97
Cdd:TIGR02857 14 LGALLIIAQAWLLARV----VDGLISAGEPLAELLPA---------LGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 98 IFFFKKLIPLIPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPIIVGTLGIIGLTAFLAWFDITIGLTLgailLSLLLI 177
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLIL----LLTAPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 178 WPTLFYKLGKHNGSELTQNKATL-RI--KTLDWLQGNAELRIFGAEAQYRQRILDAQTAL-------LanqhRMAALTgl 247
Cdd:TIGR02857 157 IPIFMILIGWAAQAAARKQWAALsRLsgHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYrertmrvL----RIAFLS-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 248 angllllangwTLLLMLwIAGDGIAgmtpdpMVAM-----VAFATMASFE-----LLMP--------IAGAFQYLGQTLS 309
Cdd:TIGR02857 231 -----------SAVLEL-FATLSVA------LVAVyigfrLLAGDLDLATglfvlLLAPefylplrqLGAQYHARADGVA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 310 SARRLNEIITAEPDTVFDENGVDQAIKGNLTISNVDYQYMDADtNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQ 389
Cdd:TIGR02857 293 AAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 390 WDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTTD--EGLNAW 467
Cdd:TIGR02857 372 VDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAlpQGLDTP 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 468 LGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLM 545
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
336-569 |
1.27e-57 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 202.56 E-value: 1.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 336 KGNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSA 415
Cdd:PRK11176 339 KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 416 MSVVSQRVDILNGSLRDNLLLA-DDTASDEKLIKTLNQV-GLEALTT-DEGLNAWLGDGGRQLSGGERRRIGIARALLHD 492
Cdd:PRK11176 419 VALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAyAMDFINKmDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 493 APIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQL 569
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
280-569 |
6.47e-54 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 192.48 E-value: 6.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 280 VAMVAFATMasfeLLMPIAGAFQYLGQTLSSARRLNEIITAEpDTVFD----ENGVD-QAIKGNLTISNVDYQYmDADTN 354
Cdd:PRK13657 276 VAFVGFATL----LIGRLDQVVAFINQVFMAAPKLEEFFEVE-DAVPDvrdpPGAIDlGRVKGAVEFDDVSFSY-DNSRQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNL 434
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNI 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 435 LLADDTASDEKLIKTLNQVglEAL----TTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTE 510
Cdd:PRK13657 430 RVGRPDATDEEMRAAAERA--QAHdfieRKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 511 QQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQL 569
Cdd:PRK13657 508 AKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
339-571 |
1.01e-53 |
|
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: 182.69 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTTD--EGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIV 496
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISElpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 497 LLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQLWQ 571
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
260-572 |
3.79e-53 |
|
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: 190.80 E-value: 3.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 260 LLLMLWIAGDGIAG--MTPDPMVAMVAFAtmasFELLMPIagafQYLG-------QTLSSARRLNEIITAEPDTVFDENG 330
Cdd:COG5265 277 LTAMMLMAAQGVVAgtMTVGDFVLVNAYL----IQLYIPL----NFLGfvyreirQALADMERMFDLLDQPPEVADAPDA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 331 VDQAIK-GNLTISNVDYQYmDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKE 409
Cdd:COG5265 349 PPLVVGgGEVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 410 SSLRSAMSVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEA--LTTDEGLNAWLGDGGRQLSGGERRRIGIAR 487
Cdd:COG5265 428 ASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDfiESLPDGYDTRVGERGLKLSGGEKQRVAIAR 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 488 ALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYH 567
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
....*
gi 1906086718 568 QLWQR 572
Cdd:COG5265 588 QMWAR 592
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
337-555 |
1.51e-50 |
|
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: 173.45 E-value: 1.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 337 GNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAM 416
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRVDILNGSLRDNLllaD--DTASDEKLIKTLNQVGLEALTTD--EGLNAWLGDGGRQLSGGERRRIGIARALLHD 492
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNL---DpfGEYSDEELWQALERVGLKEFVESlpGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 493 APIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGT 555
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
218-569 |
8.45e-48 |
|
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: 177.44 E-value: 8.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 218 GAEAQYRQRILDAQTALLANQHRMAALTGLANGLLLLANGWTLLLMLWIAG----DGiaGMTpdpMVAMVAFAT-MASF- 291
Cdd:TIGR03796 349 GLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVGGlrvmEG--QLT---IGMLVAFQSlMSSFl 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 292 ---ELLMPIAGAFQYLGQTLSsarRLNEIITAEPDTVFDENGVDQA-------IKGNLTISNVDYQYMDADTNAINAISL 361
Cdd:TIGR03796 424 epvNNLVGFGGTLQELEGDLN---RLDDVLRNPVDPLLEEPEGSAAtsepprrLSGYVELRNITFGYSPLEPPLIENFSL 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 362 DLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADDTA 441
Cdd:TIGR03796 501 TLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTI 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 442 SDEKLIKTLNqvglEALTTDE------GLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMS 515
Cdd:TIGR03796 581 PDADLVRACK----DAAIHDVitsrpgGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDD 656
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 516 VLNKhiEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQL 569
Cdd:TIGR03796 657 NLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
359-569 |
4.45e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 173.88 E-value: 4.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTrQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLAD 438
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALL-GFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 439 DTASDEKLIKTLNQVG----LEALTtdEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIM 514
Cdd:PRK11174 448 PDASDEQLQQALENAWvsefLPLLP--QGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 515 SVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQL 569
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
302-572 |
1.51e-45 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 169.30 E-value: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 302 QYLGQTLSSARRLNEIITAEpDTVFDENGVDQA-----IKGNLTISNVDYQYMDAdTNAINAISLDLLSGQKMAIVGQTG 376
Cdd:TIGR01192 294 GFITQIFEARAKLEDFFDLE-DSVFQREEPADApelpnVKGAVEFRHITFEFANS-SQGVFDVSFEAKAGQTVAIVGPTG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 377 SGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLE 456
Cdd:TIGR01192 372 AGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAH 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 457 ALTTDE--GLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLV 534
Cdd:TIGR01192 452 DFILKRsnGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLS 531
|
250 260 270
....*....|....*....|....*....|....*...
gi 1906086718 535 NLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQLWQR 572
Cdd:TIGR01192 532 TVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
313-569 |
1.19e-43 |
|
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: 165.68 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 313 RLNEIITAEPDtvFDENGVDQA---IKGNLTISNVDYQYMDADtNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQ 389
Cdd:TIGR01193 447 RLNEVYLVDSE--FINKKKRTElnnLNGDIVINDVSYSYGYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 390 WDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLL-ADDTASDEKLIKTLN--QVGLEALTTDEGLNA 466
Cdd:TIGR01193 524 FQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEiaEIKDDIENMPLGYQT 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 467 WLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKhIEHKTVVFITHRLVNLEQMDHICLMD 546
Cdd:TIGR01193 604 ELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLD 682
|
250 260
....*....|....*....|...
gi 1906086718 547 HGEIVEQGTHDSLLSLKGAYHQL 569
Cdd:TIGR01193 683 HGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
337-571 |
3.52e-40 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 154.49 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 337 GNLTISNVDYQYMDaDTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAM 416
Cdd:PRK10790 339 GRIDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRVDILNGSLRDNLLLADDTaSDEKLIKTLNQVGLEAL--TTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAP 494
Cdd:PRK10790 418 AMVQQDPVVLADTFLANVTLGRDI-SEEQVWQALETVQLAELarSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 495 IVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQLWQ 571
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
320-570 |
5.78e-40 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 153.33 E-value: 5.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 320 AEPDTVFDENGVDQAIKGNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAI 399
Cdd:PRK10789 295 AEAPVVKDGSEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 400 DGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADDTASDEKL--IKTLNQVGLEALTTDEGLNAWLGDGGRQLSG 477
Cdd:PRK10789 375 HDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIehVARLASVHDDILRLPQGYDTEVGERGVMLSG 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 478 GERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHD 557
Cdd:PRK10789 455 GQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHD 534
|
250
....*....|...
gi 1906086718 558 SLLSLKGAYHQLW 570
Cdd:PRK10789 535 QLAQQSGWYRDMY 547
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
339-561 |
5.21e-39 |
|
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: 142.47 E-value: 5.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDaDTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVD--ILNGSLRD-------NLLLADDTAsDEKLIKTLNQVGLEALttdeglnawlgdGGR---QLSGGERRRIGIA 486
Cdd:COG1122 80 VFQNPDdqLFAPTVEEdvafgpeNLGLPREEI-RERVEEALELVGLEHL------------ADRpphELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 487 RALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRL--VnLEQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLdlV-AELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
333-550 |
1.58e-38 |
|
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: 141.07 E-value: 1.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 333 QAIKGNLTISNVDYQYMD-ADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESS 411
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 412 LRSAMSVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTTD--EGLNAWLGDGGRQLSGGERRRIGIARAL 489
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISElaSGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 490 LHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEI 550
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
339-561 |
3.20e-37 |
|
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: 144.66 E-value: 3.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNAINA---ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESS---L 412
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRAvddVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 413 RSAMSVVSQ----------RV-DILNGSLRdNLLLADDTASDEKLIKTLNQVGLEAlttdeglnawlGDGGR---QLSGG 478
Cdd:COG1123 341 RRRVQMVFQdpysslnprmTVgDIIAEPLR-LHGLLSRAERRERVAELLERVGLPP-----------DLADRyphELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 479 ERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEH-KTVVFITH--RLVnlEQM-DHICLMDHGEIVEQ 553
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlQRELgLTYLFISHdlAVV--RYIaDRVAVMYDGRIVED 486
|
....*...
gi 1906086718 554 GTHDSLLS 561
Cdd:COG1123 487 GPTEEVFA 494
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
28-311 |
3.24e-37 |
|
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: 139.72 E-value: 3.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 28 TLFASIGLLTISGWFIsASAIAGLTIARETFNYMLPAGAVRGFSIGRTAGRWGERVVSHNATFKLLTELRIFFFKKLIPL 107
Cdd:cd18561 4 LGLLITALYIAQAWLL-ARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 108 IPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPIIVGTLGIIGLTAFLAWFDITIGLtLGAILLSLLLIWPTLFYKLGK 187
Cdd:cd18561 83 GPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVAL-ILLVFALLIPLSPALWDRLAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 188 HNGSELTQNKATLRIKTLDWLQGNAELRIFGAEAQYRQRILDAQTALLANQHRMAALTGLANGLLLLANGWTLLLMLWIA 267
Cdd:cd18561 162 DTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1906086718 268 GDGIAGMTPDPMVAMVAFATMASFELLMPIAGAFQYLGQTLSSA 311
Cdd:cd18561 242 ALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
341-549 |
1.15e-36 |
|
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: 135.67 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 341 ISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVS 420
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 421 QRVD--ILNGSLRD-------NLLLADDTAsDEKLIKTLNQVGLEALTTDEglnawlgdgGRQLSGGERRRIGIARALLH 491
Cdd:cd03225 82 QNPDdqFFGPTVEEevafgleNLGLPEEEI-EERVEEALELVGLEGLRDRS---------PFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 492 DAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRLVNL-EQMDHICLMDHGE 549
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
339-554 |
1.60e-36 |
|
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: 135.71 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDAD--TNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSL---R 413
Cdd:cd03257 2 LEVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 414 SAMSVVSQ----------RV-DILNGSLRDNLLLADDTASDEKLIKTLNQVGLEAlttdeglnAWLGDGGRQLSGGERRR 482
Cdd:cd03257 82 KEIQMVFQdpmsslnprmTIgEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPE--------EVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 483 IGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHK-TVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlQEELGlTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
339-561 |
1.27e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 133.65 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESsLRSAMSV 418
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNG-SLRDNLLLA------DDTASDEKLIKTLNQVGLEAlttdeglnaWLGDGGRQLSGGERRRIGIARALLH 491
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFarlyglPRKEARERIDELLELFGLTD---------AADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 492 DAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
339-550 |
4.21e-35 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 131.46 E-value: 4.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTN--AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSL---- 412
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 413 RSAMSVVSQRVDILNG-SLRDNLLLA------DDTASDEKLIKTLNQVGLEALttdeglnawLGDGGRQLSGGERRRIGI 485
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPlllagvPKKERRERAEELLERVGLGDR---------LNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 486 ARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK--HIEHKTVVFITHRLVNLEQMDHICLMDHGEI 550
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
339-561 |
1.12e-34 |
|
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: 131.32 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNG-SLRDNLLL---------ADDTASDEKLI-KTLNQVGLEALTtDEGLNawlgdggrQLSGGERRRIGIAR 487
Cdd:COG1120 80 VPQEPPAPFGlTVRELVALgryphlglfGRPSAEDREAVeEALERTGLEHLA-DRPVD--------ELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 488 ALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK--HIEHKTVVFITHRLvNL--EQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDL-NLaaRYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
340-554 |
1.96e-34 |
|
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: 128.32 E-value: 1.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 340 TISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVV 419
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 420 SQrvdilngslrdnllladdtasdeklikTLNQVGLEALTtDEGLNawlgdggrQLSGGERRRIGIARALLHDAPIVLLD 499
Cdd:cd03214 79 PQ---------------------------ALELLGLAHLA-DRPFN--------ELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 500 EPTEGLDQKTEQQIMSVLNKHIEH--KTVVFITHRLvNLEQM--DHICLMDHGEIVEQG 554
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErgKTVVMVLHDL-NLAARyaDRVILLKDGRIVAQG 180
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
339-550 |
5.27e-34 |
|
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: 126.95 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNGSLRDNLlladdtasdekliktlnqvglealttdeglnawlgdggrqLSGGERRRIGIARALLHDAPIVLL 498
Cdd:cd03246 81 LPQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 499 DEPTEGLDQKTEQQIMSVL-NKHIEHKTVVFITHRLVNLEQMDHICLMDHGEI 550
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
306-569 |
1.17e-33 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 136.39 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 306 QTLSSARRLNEIITAEPDTvfdENGVDQA---IKGNLTISNVDYQYMDADTNAI-NAISLDLLSGQKMAIVGQTGSGKST 381
Cdd:TIGR00958 446 QAVGASEKVFEYLDRKPNI---PLTGTLAplnLEGLIEFQDVSFSYPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKST 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 382 LLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTTD 461
Cdd:TIGR00958 523 VAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIME 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 462 --EGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSvlNKHIEHKTVVFITHRLVNLEQM 539
Cdd:TIGR00958 603 fpNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERA 680
|
250 260 270
....*....|....*....|....*....|
gi 1906086718 540 DHICLMDHGEIVEQGTHDSLLSLKGAYHQL 569
Cdd:TIGR00958 681 DQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
274-561 |
1.58e-33 |
|
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: 134.49 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 274 MTPDPMVA---MVAFAtMASFELLMpiaGAFQYLGQTLSSARRLNEIITAEPDtvfDENGVDQ-AIKGNLTISNVDYQYM 349
Cdd:COG4618 269 ITPGAMIAasiLMGRA-LAPIEQAI---GGWKQFVSARQAYRRLNELLAAVPA---EPERMPLpRPKGRLSVENLTVVPP 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 350 DADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGS 429
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGT 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 430 LRDNL-LLADdtASDEKLIKTLNQVGLEA--LTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLD 506
Cdd:COG4618 422 IAENIaRFGD--ADPEKVVAAAKLAGVHEmiLRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 507 QKTEQQIMSVLNKHIEHK-TVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:COG4618 500 DEGEAALAAAIRALKARGaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
339-561 |
2.92e-33 |
|
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: 127.23 E-value: 2.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVD--YQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAM 416
Cdd:COG1124 2 LEVRNLSvsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQ----------RVDilnGSLRDNLLLADDTASDEKLIKTLNQVGLEAlttdeglnAWLGDGGRQLSGGERRRIGIA 486
Cdd:COG1124 82 QMVFQdpyaslhprhTVD---RILAEPLRIHGLPDREERIAELLEQVGLPP--------SFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 487 RALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHK-TVVFITHrlvNLEQMDHIC----LMDHGEIVEQGTHDSLL 560
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDlREERGlTYLFVSH---DLAVVAHLCdrvaVMQNGRIVEELTVADLL 227
|
.
gi 1906086718 561 S 561
Cdd:COG1124 228 A 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
339-560 |
3.73e-33 |
|
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: 127.03 E-value: 3.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTnAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:cd03295 1 IEFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDIL-------NGSLRDNLLLADDTASDEKLIKTLNQVGLEALTtdeglnaWLGDGGRQLSGGERRRIGIARALLH 491
Cdd:cd03295 80 VIQQIGLFphmtveeNIALVPKLLKWPKEKIRERADELLALVGLDPAE-------FADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 492 DAPIVLLDEPTEGLDQKTE---QQIMSVLNKHIeHKTVVFITH------RLVnleqmDHICLMDHGEIVEQGTHDSLL 560
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRdqlQEEFKRLQQEL-GKTIVFVTHdideafRLA-----DRIAIMKNGEIVQVGTPDEIL 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
339-553 |
4.35e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 126.31 E-value: 4.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYM--DADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQL---LTRqwdPKSGYIAIDGVKLPKWKESSL- 412
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 413 ---RSAMSVVSQRVDILNG-SLRDNLLLA------DDTASDEKLIKTLNQVGLEAlttdeglnaWLGDGGRQLSGGERRR 482
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPElTALENVALPlllagvSRKERRERARELLERVGLGD---------RLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 483 IGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIE--HKTVVFITHRLVNLEQMDHICLMDHGEIVEQ 553
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
339-555 |
8.27e-33 |
|
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: 125.77 E-value: 8.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDA--DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSA- 415
Cdd:cd03258 2 IELKNVSKVFGDTggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 416 --MSVVSQRVDILNG-SLRDNLLLA------DDTASDEKLIKTLNQVGLEalttdEGLNAWLGdggrQLSGGERRRIGIA 486
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALPleiagvPKAEIEERVLELLELVGLE-----DKADAYPA----QLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 487 RALLHDAPIVLLDEPTEGLDQKTEQQIMSVLnKHIEHK---TVVFITHRL-VNLEQMDHICLMDHGEIVEQGT 555
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALL-RDINRElglTIVLITHEMeVVKRICDRVAVMEKGEVVEEGT 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
339-561 |
8.82e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 131.95 E-value: 8.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPK---SGYIAIDGVKLPKWKESSLRSA 415
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 416 MSVVSQRVDI-LNGS-----LRDNLLLADDTASD--EKLIKTLNQVGLEALttdeglnawLGDGGRQLSGGERRRIGIAR 487
Cdd:COG1123 85 IGMVFQDPMTqLNPVtvgdqIAEALENLGLSRAEarARVLELLEAVGLERR---------LDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 488 ALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEH--KTVVFITHRL-VNLEQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
339-550 |
1.92e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNGSLRDNLL----LADDTASDEKLIKTLNQVGL--EALTTDEglnawlgdggRQLSGGERRRIGIARALLHD 492
Cdd:COG4619 79 VPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLERLGLppDILDKPV----------ERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 493 APIVLLDEPTEGLDQKTEQQIMSVLNKHIEHK--TVVFITHrlvNLEQ----MDHICLMDHGEI 550
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSH---DPEQiervADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
340-549 |
1.93e-32 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 121.97 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 340 TISNVDYQYMDAdtNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVV 419
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 420 SQrvdilngslrdnllladdtasdekliktlnqvglealttdeglnawlgdggrqLSGGERRRIGIARALLHDAPIVLLD 499
Cdd:cd00267 79 PQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 500 EPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQ-MDHICLMDHGE 549
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
339-564 |
9.86e-32 |
|
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: 123.04 E-value: 9.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKwKESSLRSAMSV 418
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDI-LNGSLRDNLL----LADDtaSDEKLIKTLNQVgLEALTTDEGLNAWLGDggrqLSGGERRRIGIARALLHDA 493
Cdd:COG4555 79 LPDERGLyDRLTVRENIRyfaeLYGL--FDEELKKRIEEL-IELLGLEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 494 PIVLLDEPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLSLKG 564
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
356-502 |
1.34e-31 |
|
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: 119.67 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNG-SLRDNL 434
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 435 LLA------DDTASDEKLIKTLNQVGLEALTTDEglnawLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPT 502
Cdd:pfam00005 81 RLGlllkglSKREKDARAEEALEKLGLGDLADRP-----VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
359-549 |
1.86e-31 |
|
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: 121.04 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGyiaidgvklpkwkESSLRSAMSVVSQRVDILNGSLRDNLLLAD 438
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG-------------SVSVPGSIAYVSQEPWIQNGTIRENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 439 DTasDEKLiktLNQVgLEA--LTTD-----EGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQ 511
Cdd:cd03250 91 PF--DEER---YEKV-IKAcaLEPDleilpDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1906086718 512 QIM-SVLNKHI-EHKTVVFITHRLVNLEQMDHICLMDHGE 549
Cdd:cd03250 165 HIFeNCILGLLlNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
337-555 |
2.58e-31 |
|
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: 120.59 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 337 GNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAM 416
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRVDILNGSLRDNLllaD--DTASDEKLiktlnqvgLEALTTDEglnawlgdGGRQLSGGERRRIGIARALLHDAP 494
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNL---DpfDEYSDEEI--------YGALRVSE--------GGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 495 IVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGT 555
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
339-552 |
5.99e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.16 E-value: 5.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGV---KLPKWKESSLRSA 415
Cdd:COG2884 2 IRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 416 MSVVSQrvD---ILNGSLRDNLLLA------DDTASDEKLIKTLNQVGLEalttdeglnawlgdgGR------QLSGGER 480
Cdd:COG2884 81 IGVVFQ--DfrlLPDRTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLS---------------DKakalphELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 481 RRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRLVNLEQMDH-ICLMDHGEIVE 552
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
339-555 |
2.71e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 121.34 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVD--YQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSA- 415
Cdd:COG1135 2 IELENLSktFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 416 --MSVVSQRVDILNG-SLRDN----LLLA--DDTASDEKLIKTLNQVGLEalttDEGlNAWLgdggRQLSGGERRRIGIA 486
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENvalpLEIAgvPKAEIRKRVAELLELVGLS----DKA-DAYP----SQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 487 RALLHDAPIVLLDEPTEGLDQKTEQQIMSVLnKHIEHK---TVVFITHrlvnleQMD---HIC----LMDHGEIVEQGT 555
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLL-KDINRElglTIVLITH------EMDvvrRICdrvaVLENGRIVEQGP 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
339-554 |
3.09e-30 |
|
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: 118.05 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADtnAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWD-----PKSGYIAIDGVKLPKWKES--S 411
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 412 LRSAMSVVSQRVDILNGSLRDNLLLADdTASDEKLIKTLNQVGLEALTTdeglnAWLGD------GGRQLSGGERRRIGI 485
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGL-RLHGIKLKEELDERVEEALRK-----AALWDevkdrlHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 486 ARALLHDAPIVLLDEPTEGLD----QKTEQQIMSvLNKHIehkTVVFITHrlvNLEQM----DHICLMDHGEIVEQG 554
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDpistAKIEELIAE-LKKEY---TIVIVTH---NMQQAarvaDRTAFLLNGRLVEFG 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
337-568 |
3.37e-30 |
|
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: 119.57 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 337 GNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKsGYIAIDGVKLPKWKESSLRSAM 416
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRVDILNGSLRDNLllaDDTA--SDEKLIKTLNQVGLEALTTD--EGLNAWLGDGGRQLSGGERRRIGIARALLHD 492
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNL---DPYGkwSDEEIWKVAEEVGLKSVIEQfpGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 493 APIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQ 568
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
339-567 |
7.49e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.50 E-value: 7.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKwkessLRSAMSV 418
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDI------------LNGSLRDNLLLADDTASDEKLI-KTLNQVGLEALttdegLNAWLGdggrQLSGGERRRIGI 485
Cdd:COG1121 80 VPQRAEVdwdfpitvrdvvLMGRYGRRGLFRRPSRADREAVdEALERVGLEDL-----ADRPIG----ELSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 486 ARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRLVNLEQM-DHICLMDHGeIVEQGTHDSLLS-- 561
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYfDRVLLLNRG-LVAHGPPEEVLTpe 229
|
....*..
gi 1906086718 562 -LKGAYH 567
Cdd:COG1121 230 nLSRAYG 236
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
359-560 |
1.32e-29 |
|
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: 117.00 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKES---SLRSAMSVVSQrvdilNGSLRDNLL 435
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRIGMLFQ-----GGALFDSLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 436 LADD--------TASDEKLIK-----TLNQVGLEalttdeglnawlGDGGR---QLSGGERRRIGIARALLHDAPIVLLD 499
Cdd:COG1127 99 VFENvafplrehTDLSEAEIRelvleKLELVGLP------------GAADKmpsELSGGMRKRVALARALALDPEILLYD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 500 EPTEGLD----QKTEQQIMSvLNKHIeHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLL 560
Cdd:COG1127 167 EPTAGLDpitsAVIDELIRE-LRDEL-GLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELL 230
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
339-569 |
2.00e-29 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 116.24 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSaMSV 418
Cdd:TIGR03864 2 LEVAGLSFRY--GARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALAR-LGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDI-LNGSLRDNLLLAddtASDEKLIKTLNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVL 497
Cdd:TIGR03864 79 VFQQPTLdLDLSVRQNLRYH---AALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 498 LDEPTEGLDQKTEQQIMSVLNKHIEHK--TVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLL------SLKGAYHQL 569
Cdd:TIGR03864 156 LDEPTVGLDPASRAAITAHVRALARDQglSVLWATHLVDEIEASDRLVVLHRGRVLADGAAAELRgatggaDLEAAFLAL 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
353-560 |
3.80e-29 |
|
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: 116.59 E-value: 3.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 353 TNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSL----RSAMSVVSQRVDIL-N 427
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 428 GSLRDN----LLLA--DDTASDEKLIKTLNQVGLEalttdeglnAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEP 501
Cdd:cd03294 117 RTVLENvafgLEVQgvPRAEREERAAEALELVGLE---------GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 502 TEGLDQ--KTEQQ--IMSVLNKHieHKTVVFITHRLVnlEQM---DHICLMDHGEIVEQGTHDSLL 560
Cdd:cd03294 188 FSALDPliRREMQdeLLRLQAEL--QKTIVFITHDLD--EALrlgDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
339-550 |
2.05e-28 |
|
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: 111.34 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKwKESSLRSAMSV 418
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNG-SLRDNLlladdtasdekliktlnqvglealttdeglnawlgdggrQLSGGERRRIGIARALLHDAPIVL 497
Cdd:cd03230 78 LPEEPSLYENlTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 498 LDEPTEGLDQKTEQQIMSVLNKHI-EHKTVVFITHRLVNLEQM-DHICLMDHGEI 550
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
339-551 |
2.99e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 113.23 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMS- 417
Cdd:COG3638 3 LELRNLSKRY-PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 418 ----------VVSQRV--DILNGSLRD--------NLLLADDTasdEKLIKTLNQVGLE--ALT-TDeglnawlgdggrQ 474
Cdd:COG3638 82 igmifqqfnlVPRLSVltNVLAGRLGRtstwrsllGLFPPEDR---ERALEALERVGLAdkAYQrAD------------Q 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 475 LSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHK-TVVfithrlVNLEQMDH-------ICLM 545
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRiAREDGiTVV------VNLHQVDLarryadrIIGL 220
|
....*.
gi 1906086718 546 DHGEIV 551
Cdd:COG3638 221 RDGRVV 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
294-532 |
3.24e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 118.76 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 294 LMPIAGAFQYLGQTLS--------------SARRL---NEIITAEPDTVFDENGVDQAIKGNLTISNVDYQymDADTNA- 355
Cdd:COG4178 301 LMQAASAFGQVQGALSwfvdnyqslaewraTVDRLagfEEALEAADALPEAASRIETSEDGALALEDLTLR--TPDGRPl 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAidgvkLPkwkesSLRSAMsVVSQRVDILNGSLRDNLL 435
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-----RP-----AGARVL-FLPQRPYLPLGTLREALL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 436 --LADDTASDEKLIKTLNQVGLEALTT--DEGLNaWlgdgGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQ 511
Cdd:COG4178 448 ypATAEAFSDAELREALEAVGLGHLAErlDEEAD-W----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA 522
|
250 260
....*....|....*....|.
gi 1906086718 512 QIMSVLNKHIEHKTVVFITHR 532
Cdd:COG4178 523 ALYQLLREELPGTTVISVGHR 543
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
359-559 |
3.47e-28 |
|
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: 112.60 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSA---MSVVSQrvdilNGSLRDNLL 435
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMGMLFQ-----SGALFDSLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 436 LADDTA-------------SDEKLIKTLNQVGLEAlttdeGLNAWLGdggrQLSGGERRRIGIARALLHDAPIVLLDEPT 502
Cdd:cd03261 94 VFENVAfplrehtrlseeeIREIVLEKLEAVGLRG-----AEDLYPA----ELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 503 EGLDQKT----EQQIMSvLNKHIeHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSL 559
Cdd:cd03261 165 AGLDPIAsgviDDLIRS-LKKEL-GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
341-548 |
1.16e-27 |
|
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: 110.70 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 341 ISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKwkessLRSAMSVVS 420
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 421 QRVDI------------LNGSLRDNLLLADDTASDEKLIKT-LNQVGLEALttdegLNAWLGdggrQLSGGERRRIGIAR 487
Cdd:cd03235 75 QRRSIdrdfpisvrdvvLMGLYGHKGLFRRLSKADKAKVDEaLERVGLSEL-----ADRQIG----ELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 488 ALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHrlvNLEQM----DHICLMDHG 548
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTH---DLGLVleyfDRVLLLNRT 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
339-559 |
6.56e-27 |
|
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: 109.19 E-value: 6.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDaDTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSA--- 415
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 416 -------------MSVVSqrvDILNGSL-RDNL---LLADDTASD-EKLIKTLNQVGLE--ALT-TDeglnawlgdggrQ 474
Cdd:cd03256 80 igmifqqfnlierLSVLE---NVLSGRLgRRSTwrsLFGLFPKEEkQRALAALERVGLLdkAYQrAD------------Q 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 475 LSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVL-NKHIEHKTVVFITHRLVNL--EQMDHICLMDHGEIV 551
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREEGITVIVSLHQVDLarEYADRIVGLKDGRIV 224
|
....*...
gi 1906086718 552 EQGTHDSL 559
Cdd:cd03256 225 FDGPPAEL 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
359-547 |
8.90e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 107.95 E-value: 8.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESsLRSAMSVVSQRVDILNG-SLRDNLL-- 435
Cdd:COG4133 21 LSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLAYLGHADGLKPElTVRENLRfw 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 436 --LADDTASDEKLIKTLNQVGLEALttdEGLNAwlgdggRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQI 513
Cdd:COG4133 100 aaLYGLRADREAIDEALEAVGLAGL---ADLPV------RQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1906086718 514 MSVLNKHIEH-KTVVFITHRLVNLEQMDHICLMDH 547
Cdd:COG4133 171 AELIAAHLARgGAVLLTTHQPLELAAARVLDLGDF 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
339-531 |
1.22e-26 |
|
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: 107.94 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDAD--TNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLpkwkeSSLRSAM 416
Cdd:cd03293 1 LEVRNVSKTYGGGGgaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQrvdilNGSL------RDNLLLA------DDTASDEKLIKTLNQVGLEALttdegLNAWlgdgGRQLSGGERRRIG 484
Cdd:cd03293 76 GYVFQ-----QDALlpwltvLDNVALGlelqgvPKAEARERAEELLELVGLSGF-----ENAY----PHQLSGGMRQRVA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1906086718 485 IARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEH--KTVVFITH 531
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtgKTVLLVTH 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
359-569 |
1.58e-26 |
|
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: 115.04 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLllaD 438
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---D 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 439 --DTASDEKLIKTLNQVGLEALTTD--EGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIM 514
Cdd:TIGR00957 1382 pfSQYSDEEVWWALELAHLKTFVSAlpDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 515 SVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAYHQL 569
Cdd:TIGR00957 1462 STIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
339-550 |
1.97e-26 |
|
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: 107.23 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKE--SSLRSAM 416
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRVDIL-NGSLRDNLLLA-------DDTASDEKLIKTLNQVGLEalttdEGLNAWlgdgGRQLSGGERRRIGIARA 488
Cdd:cd03262 79 GMVFQQFNLFpHLTVLENITLApikvkgmSKAEAEERALELLEKVGLA-----DKADAY----PAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 489 LLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHrlvnleQM-------DHICLMDHGEI 550
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTH------EMgfarevaDRVIFMDDGRI 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
335-568 |
3.42e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 113.97 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 335 IKGNLTISNVDYQYMDADTNAI-NAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPK-------------------- 393
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYISRPNVPIyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 394 ----------------------------------SGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLLLADD 439
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 440 TASDEKLIKTLNQVGL----EALTTDEGLNawLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMS 515
Cdd:PTZ00265 1322 DATREDVKRACKFAAIdefiESLPNKYDTN--VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 516 VLN--KHIEHKTVVFITHRLVNLEQMDHICLMDH----GEIVE-QGTHDSLLSLK-GAYHQ 568
Cdd:PTZ00265 1400 TIVdiKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQdGVYKK 1460
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
337-562 |
6.36e-26 |
|
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: 113.47 E-value: 6.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 337 GNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKsGYIAIDGVKlpkWKESSL---R 413
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVS---WNSVTLqtwR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 414 SAMSVVSQRVDILNGSLRDNLllaDDTA--SDEKLIKTLNQVGLEALTTD--EGLNAWLGDGGRQLSGGERRRIGIARAL 489
Cdd:TIGR01271 1292 KAFGVIPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQfpDKLDFVLVDGGYVLSNGHKQLMCLARSI 1368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 490 LHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHIcLMDHGEIVEQgtHDSLLSL 562
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQF-LVIEGSSVKQ--YDSIQKL 1438
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
341-563 |
7.38e-26 |
|
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: 107.13 E-value: 7.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 341 ISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDG--VKLPK--WKessLRSAM 416
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldTLDEEnlWE---IRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQrvdilNgslRDNLLLA----DDTA--------SDEKLIK----TLNQVGLEALTTDEGLNawlgdggrqLSGGER 480
Cdd:TIGR04520 80 GMVFQ-----N---PDNQFVGatveDDVAfglenlgvPREEMRKrvdeALKLVGMEDFRDREPHL---------LSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 481 RRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEH-KTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDS 558
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKlNKEEgITVISITHDMEEAVLADRVIVMNKGKIVAEGTPRE 222
|
....*
gi 1906086718 559 LLSLK 563
Cdd:TIGR04520 223 IFSQV 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
337-563 |
1.19e-25 |
|
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: 106.15 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 337 GNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAM 416
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRVDILNGSLRDNLLlADDTASDEKLIKTLN--QVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAP 494
Cdd:cd03288 98 SIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEiaQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 495 IVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLK 563
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
341-555 |
1.22e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.06 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 341 ISNVDYQYMDA---DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKL--PKWKESSLRSA 415
Cdd:PRK13637 5 IENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 416 MSVVSQ-----------RVDILNGSlrDNLLLADDTASdEKLIKTLNQVGLEalttdegLNAWLGDGGRQLSGGERRRIG 484
Cdd:PRK13637 85 VGLVFQypeyqlfeetiEKDIAFGP--INLGLSEEEIE-NRVKRAMNIVGLD-------YEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 485 IARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHK-TVVFITHRLVNLEQM-DHICLMDHGEIVEQGT 555
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElHKEYNmTIILVSHSMEDVAKLaDRIIVMNKGKCELQGT 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
339-531 |
2.17e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.56 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVD--YQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLpkwkeSSLRSAM 416
Cdd:COG1116 8 LELRGVSkrFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQrvdilNGSL------RDNLLLA------DDTASDEKLIKTLNQVGLEALttdegLNAWlgdgGRQLSGGERRRIG 484
Cdd:COG1116 83 GVVFQ-----EPALlpwltvLDNVALGlelrgvPKAERRERARELLELVGLAGF-----EDAY----PHQLSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 485 IARALLHDAPIVLLDEPTEGLDQKT----EQQIMSVLNKHieHKTVVFITH 531
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTrerlQDELLRLWQET--GKTVLFVTH 197
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
339-561 |
2.36e-25 |
|
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: 106.68 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISN--VDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPK---SGYIAIDGVKLPKWKESSLR 413
Cdd:COG0444 2 LEVRNlkVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 414 SA----MSVVSQ----------RV-DILNGSLRDNLLLaDDTASDEKLIKTLNQVGLEalttdeglnawlgDGGR----- 473
Cdd:COG0444 82 KIrgreIQMIFQdpmtslnpvmTVgDQIAEPLRIHGGL-SKAEARERAIELLERVGLP-------------DPERrldry 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 474 --QLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIE--HKTVVFITHRLVNLEQM-DHICLMDHG 548
Cdd:COG0444 148 phELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEIaDRVAVMYAG 227
|
250
....*....|...
gi 1906086718 549 EIVEQGTHDSLLS 561
Cdd:COG0444 228 RIVEEGPVEELFE 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
339-549 |
5.68e-25 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 101.88 E-value: 5.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESS--LRSAM 416
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRVDILNG-SLRDNLLLAddtasdekliktlnqvglealttdeglnawlgdggrqLSGGERRRIGIARALLHDAPI 495
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 496 VLLDEPTEGLDQKTEQQIMSVLNK-HIEH-KTVVFITHRLVNLEQM-DHICLMDHGE 549
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSlQAQLgITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
343-550 |
6.04e-25 |
|
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: 102.87 E-value: 6.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 343 NVDYQYmDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESS---LRSAMSVV 419
Cdd:cd03292 5 NVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 420 SQrvdilngslrDNLLLADDTASD-----------------EKLIKTLNQVGLEALTTDEGlnawlgdggRQLSGGERRR 482
Cdd:cd03292 84 FQ----------DFRLLPDRNVYEnvafalevtgvppreirKRVPAALELVGLSHKHRALP---------AELSGGEQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 483 IGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITH--RLVNleQMDH-ICLMDHGEI 550
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHakELVD--TTRHrVIALERGKL 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
332-560 |
9.07e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.92 E-value: 9.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 332 DQAIKgnltISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESS 411
Cdd:PRK13632 5 SVMIK----VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 412 LRSAMSVVSQRVDilN---GSlrdnlLLADDTA-------SDEKLIKTL-----NQVGLEALTTDEGLNawlgdggrqLS 476
Cdd:PRK13632 81 IRKKIGIIFQNPD--NqfiGA-----TVEDDIAfglenkkVPPKKMKDIiddlaKKVGMEDYLDKEPQN---------LS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 477 GGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLN--KHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQG 554
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
....*.
gi 1906086718 555 THDSLL 560
Cdd:PRK13632 225 KPKEIL 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
339-561 |
9.12e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.56 E-value: 9.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:PRK11231 3 LRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNG-SLRD---------NLLLADDTASDEKLIktlnQVGLEALTTDEGLNAWLGDggrqLSGGERRRIGIARA 488
Cdd:PRK11231 81 LPQHHLTPEGiTVRElvaygrspwLSLWGRLSAEDNARV----NQAMEQTRINHLADRRLTD----LSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 489 LLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHrlvNLEQM----DHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRElNTQGKTVVTVLH---DLNQAsrycDHLVVLANGHVMAQGTPEEVMT 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-555 |
9.70e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.94 E-value: 9.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVD--ILNGSLRDNLL--LADDTASDEKLIK----TLNQVGLEALTTDEglnawlgdgGRQLSGGERRRIGIARALL 490
Cdd:PRK13635 86 VFQNPDnqFVGATVQDDVAfgLENIGVPREEMVErvdqALRQVGMEDFLNRE---------PHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 491 HDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHK--TVVFITHRLVNLEQMDHICLMDHGEIVEQGT 555
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
281-566 |
1.07e-24 |
|
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: 109.65 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 281 AMVAFATMASFELL-MPI---AGAFQYLGQTLSSARRLNEIITAE---PDTVfDENGVDQAIKGNLTISNVDYQYMDADT 353
Cdd:TIGR00957 573 AEKAFVSLALFNILrFPLnilPMVISSIVQASVSLKRLRIFLSHEelePDSI-ERRTIKPGEGNSITVHNATFTWARDLP 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 354 NAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwkesslrsAMSVVSQRVDILNGSLRDN 433
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLREN 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 434 LLLAddTASDEKLIKTLNQV-----GLEALTTdeGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQK 508
Cdd:TIGR00957 719 ILFG--KALNEKYYQQVLEAcallpDLEILPS--GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 509 TEQQIM-SVLNKH--IEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGAY 566
Cdd:TIGR00957 795 VGKHIFeHVIGPEgvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
339-560 |
1.60e-24 |
|
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: 102.47 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGY-IAIDGVKLPKWKESSLRSAMS 417
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 418 VVSQRvdilngslrdnllLADDTASDEKLIKTL-----NQVGL--EALTTDEGL-NAWLGDGG---------RQLSGGER 480
Cdd:COG1119 82 LVSPA-------------LQLRFPRDETVLDVVlsgffDSIGLyrEPTDEQRERaRELLELLGlahladrpfGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 481 RRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEH--KTVVFITHRlvnLEQ----MDHICLMDHGEIVEQG 554
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHH---VEEippgITHVLLLKDGRVVAAG 225
|
....*.
gi 1906086718 555 THDSLL 560
Cdd:COG1119 226 PKEEVL 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
336-565 |
2.05e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 108.52 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 336 KGNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSA 415
Cdd:PLN03232 1232 RGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 416 MSVVSQRVDILNGSLRDNLlladDTAS---DEKLIKTLNQVGLEALTTDE--GLNAWLGDGGRQLSGGERRRIGIARALL 490
Cdd:PLN03232 1312 LSIIPQSPVLFSGTVRFNI----DPFSehnDADLWEALERAHIKDVIDRNpfGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 491 HDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLKGA 565
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
355-561 |
3.25e-24 |
|
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: 106.31 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTL----LQLLtrqwdPKSGYIAIDGVKLPKWKES---SLRSAMSVVSQ------ 421
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQdpfgsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 422 ----RV-DILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTTDeglnawlgdggR---QLSGGERRRIGIARALLHDA 493
Cdd:COG4172 376 sprmTVgQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARH-----------RyphEFSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 494 PIVLLDEPTEGLDQKTEQQIMSVLnKHIEHK---TVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:COG4172 445 KLLVLDEPTSALDVSVQAQILDLL-RDLQREhglAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
340-551 |
3.95e-24 |
|
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: 100.41 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 340 TISNVDYQYMDaDTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKessLRSAMSVV 419
Cdd:cd03226 1 RIENISFSYKK-GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 420 SQRVD--ILNGSLRDNLLLADDTASDEKLIKtlnqvglEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVL 497
Cdd:cd03226 77 MQDVDyqLFTDSVREELLLGLKELDAGNEQA-------ETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 498 LDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHrlvNLEQMDHIC----LMDHGEIV 551
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH---DYEFLAKVCdrvlLLANGAIV 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
339-561 |
4.92e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.17 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDA---DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLP-KWKESSLRS 414
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 415 amsvVSQRVDILNGSLRDNLLlaDDTASDEKLI------KTLNQVGLEA--LTTDEGLNA-WLGDGGRQLSGGERRRIGI 485
Cdd:PRK13646 83 ----VRKRIGMVFQFPESQLF--EDTVEREIIFgpknfkMNLDEVKNYAhrLLMDLGFSRdVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 486 ARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK--HIEHKTVVFITHRLVNLEQ-MDHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
339-555 |
9.13e-24 |
|
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: 99.50 E-value: 9.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwkeSSLRSAMSV 418
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--------YSIRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRV------DILNGSL--RDNLLL---------ADDTASDEKLIKTLnqvglealttdeGLNAWLGDGGRQLSGGERR 481
Cdd:cd03263 73 ARQSLgycpqfDALFDELtvREHLRFyarlkglpkSEIKEEVELLLRVL------------GLTDKANKRARTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 482 RIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHrlvNLEQM----DHICLMDHGEIVEQGT 555
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAealcDRIAIMSDGKLRCIGS 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
356-562 |
1.14e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 105.13 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTrQWDPK----SGYIAIDGVKLPKWKesslRSAMSVVSQRVDILNGSL- 430
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKE----MRAISAYVQQDDLFIPTLt 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 431 -RDNLL------LADDTASDEKLIKtlnqvgLEALTTDEGL----NAWLGDGGRQ--LSGGERRRIGIARALLHDAPIVL 497
Cdd:TIGR00955 116 vREHLMfqahlrMPRRVTKKEKRER------VDEVLQALGLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 498 LDEPTEGLDQKTEQQIMSVLnKHIEHK--TVVFITH----RLvnLEQMDHICLMDHGEIVEQGTHDSLLSL 562
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVL-KGLAQKgkTIICTIHqpssEL--FELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
339-552 |
1.49e-23 |
|
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: 99.43 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADT--NAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKE---SSLR 413
Cdd:COG4181 9 IELRGLTKTVGTGAGelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 414 SA-MSVVSQRVDILnGSL--RDN----LLLADDTASDEKLIKTLNQVGLEALttdeglnawLGDGGRQLSGGERRRIGIA 486
Cdd:COG4181 89 ARhVGFVFQSFQLL-PTLtaLENvmlpLELAGRRDARARARALLERVGLGHR---------LDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 487 RALLHDAPIVLLDEPTEGLDQKTEQQIMSVL---NKhiEHK-TVVFITHRLVNLEQMDHICLMDHGEIVE 552
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLfelNR--ERGtTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
337-555 |
3.02e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 104.86 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 337 GNLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAM 416
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRVDILNGSLRDNLlladD---TASDEKLIKTLNQVGL--EALTTDEGLNAWLGDGGRQLSGGERRRIGIARALL- 490
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNV----DpflEASSAEVWAALELVGLreRVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLk 1462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 491 HDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGT 555
Cdd:PTZ00243 1463 KGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
339-555 |
3.26e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.53 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKL--PKWKESSLRSAM 416
Cdd:COG1126 2 IEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQR--------VdilngslRDNLLLA-------DDTASDEKLIKTLNQVGLEalttdEGLNAWLGdggrQLSGGERR 481
Cdd:COG1126 80 GMVFQQfnlfphltV-------LENVTLApikvkkmSKAEAEERAMELLERVGLA-----DKADAYPA----QLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 482 RIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLnKHI--EHKTVVFITHrlvnleQM-------DHICLMDHGEIVE 552
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVM-RDLakEGMTMVVVTH------EMgfarevaDRVVFMDGGRIVE 216
|
...
gi 1906086718 553 QGT 555
Cdd:COG1126 217 EGP 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
356-554 |
4.36e-23 |
|
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: 96.85 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLT--RQWDPKSGYIAIDGVKLPKwkeSSLRSAMSVVSQrvdilngslrDN 433
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQ----------DD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 434 LLLADDTASdekliktlnqvglEALttdeGLNAWLgdggRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQI 513
Cdd:cd03213 92 ILHPTLTVR-------------ETL----MFAAKL----RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1906086718 514 MSVLnKHI--EHKTVVFITHRLVNL--EQMDHICLMDHGEIVEQG 554
Cdd:cd03213 151 MSLL-RRLadTGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
366-554 |
6.28e-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: 97.18 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 366 GQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPK-----------WKESSLRSAMSVvSQRVDI-LNGSLRdn 433
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAappadrpvsmlFQENNLFAHLTV-EQNVGLgLSPGLK-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 434 lLLADDTasdEKLIKTLNQVGLEalttdeGLNAWLGDggrQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQI 513
Cdd:cd03298 101 -LTAEDR---QAIEVALARVGLA------GLEKRLPG---ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1906086718 514 MSVLNK-HIEHK-TVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:cd03298 168 LDLVLDlHAETKmTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
346-555 |
7.83e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 99.88 E-value: 7.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 346 YQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSA---MSVVSQR 422
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrqIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 423 VDILngSLR---DNLLLADDTAS-DEKLIKT-----LNQVGLEALTtdeglNAWLGdggrQLSGGERRRIGIARALLHDa 493
Cdd:PRK11153 91 FNLL--SSRtvfDNVALPLELAGtPKAEIKArvtelLELVGLSDKA-----DRYPA----QLSGGQKQRVAIARALASN- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 494 PIVLL-DEPTEGLDQKTEQQIMSVLnKHIEHK---TVVFITHrlvnleQMD---HIC----LMDHGEIVEQGT 555
Cdd:PRK11153 159 PKVLLcDEATSALDPATTRSILELL-KDINRElglTIVLITH------EMDvvkRICdrvaVIDAGRLVEQGT 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
359-561 |
8.08e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 103.66 E-value: 8.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLllaD 438
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---D 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 439 --DTASDEKLIKTLNQVGLEALT--TDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIM 514
Cdd:PLN03130 1335 pfNEHNDADLWESLERAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ 1414
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1906086718 515 SVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:PLN03130 1415 KTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
339-561 |
1.04e-22 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 96.73 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWK-ESSLRSAMS 417
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 418 VVSQRVDILNG-SLRDNLLLADDTASDEKLIKTLNQVgLEALTTdegLNAWLGDGGRQLSGGERRRIGIARALLHDAPIV 496
Cdd:cd03224 79 YVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV-YELFPR---LKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 497 LLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFithrLVnlEQM--------DHICLMDHGEIVEQGTHDSLLS 561
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTIL----LV--EQNarfaleiaDRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
343-558 |
1.25e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.98 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 343 NVDYQYMDA---DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKL-PKWKESSLRSAMSV 418
Cdd:PRK13641 7 NVDYIYSPGtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNGSLRDNLLLAD-----------DTASDEKLIKTLNQVGLealttDEGLnawLGDGGRQLSGGERRRIGIAR 487
Cdd:PRK13641 87 VSLVFQFPEAQLFENTVLKDvefgpknfgfsEDEAKEKALKWLKKVGL-----SEDL---ISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 488 ALLHDAPIVLLDEPTEGLDQKTEQQIMSV-LNKHIEHKTVVFITHRLVNL-EQMDHICLMDHGEIVEqgtHDS 558
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIK---HAS 228
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
352-567 |
1.38e-22 |
|
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: 98.23 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 352 DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDG---VKLPKwkesSLRSAMSVVSQRV---DI 425
Cdd:TIGR01188 5 DFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvVREPR----KVRRSIGIVPQYAsvdED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 426 LNGslRDNLLLADD------TASDEKLIKTLNQVGL-EAltTDEGLnawlgdggRQLSGGERRRIGIARALLHDAPIVLL 498
Cdd:TIGR01188 81 LTG--RENLEMMGRlyglpkDEAEERAEELLELFELgEA--ADRPV--------GTYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 499 DEPTEGLDQKTEQQIMSVLNKHIEHKTVVFI-THRLVNLEQM-DHICLMDHGEIVEQGTHDSLLSLKGAYH 567
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRALKEEGVTILLtTHYMEEADKLcDRIAIIDHGRIIAEGTPEELKRRLGKDT 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
339-554 |
1.41e-22 |
|
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: 96.11 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQkMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESsLRSAMSV 418
Cdd:cd03264 1 LQLENLTKRY--GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDIL-NGSLRDNL-LLA-----DDTASDEKLIKTLNQVGLEALTTDEglnawLGdggrQLSGGERRRIGIARALLH 491
Cdd:cd03264 77 LPQEFGVYpNFTVREFLdYIAwlkgiPSKEVKARVDEVLELVNLGDRAKKK-----IG----SLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 492 DAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
339-554 |
1.42e-22 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 96.05 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGV---KLPKWKES----- 410
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtGVPPERRNigmvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 411 ---SLRSAMSVvsqrvdilngslRDNLLLA------DDTASDEKLIKTLNQVGLEALttdegLNAWLgdggRQLSGGERR 481
Cdd:cd03259 79 qdyALFPHLTV------------AENIAFGlklrgvPKAEIRARVRELLELVGLEGL-----LNRYP----HELSGGQQQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 482 RIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIE--HKTVVFITHRLVN-LEQMDHICLMDHGEIVEQG 554
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEaLALADRIAVMNEGRIVQVG 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
356-554 |
1.49e-22 |
|
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: 96.19 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDP---KSGYIAIDGVKLPK--WKESSlrsamSVVSQRVDILNG-S 429
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPdqFQKCV-----AYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 430 LRDNLLLAddtaSDEKLIKTLNQVGLEALTTDEGLNAwLGD---GG---RQLSGGERRRIGIARALLHDAPIVLLDEPTE 503
Cdd:cd03234 98 VRETLTYT----AILRLPRKSSDAIRKKRVEDVLLRD-LALtriGGnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 504 GLDQKTEQQIMSVLNKHIEHKTVVFIThrlvnLEQ--------MDHICLMDHGEIVEQG 554
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILT-----IHQprsdlfrlFDRILLLSSGEIVYSG 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
359-554 |
1.49e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 96.21 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLlSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKlpkWKESSLRSAMSVVSQRVDIL--------NGSL 430
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFDSRKKINLPPQQRKIGLVfqqyalfpHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 431 RDNLLLADDTASDEKLIKTLNQVgLEALTTDEGLNAWLGdggrQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTE 510
Cdd:cd03297 93 RENLAFGLKRKRNREDRISVDEL-LDLLGLDHLLNRYPA----QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1906086718 511 QQIMSVLNKHIE--HKTVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:cd03297 168 LQLLPELKQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
353-563 |
1.50e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 102.68 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 353 TNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwkesslrsAMSVVSQRVDILNGSLRD 432
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 433 NLLLAddTASDE-KLIKTLNQVGLEALTT--DEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKT 509
Cdd:TIGR01271 506 NIIFG--LSYDEyRYTSVIKACQLEEDIAlfPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 510 EQQIM-SVLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLK 563
Cdd:TIGR01271 584 EKEIFeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
359-563 |
1.62e-22 |
|
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: 97.62 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwkesslrsAMSVVSQRVDILNGSLRDNLL--L 436
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENIIfgV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 437 ADDTASDEKLIKTLnQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIM-S 515
Cdd:cd03291 123 SYDEYRYKSVVKAC-QLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFeS 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1906086718 516 VLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLSLK 563
Cdd:cd03291 202 CVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
340-555 |
4.12e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.92 E-value: 4.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 340 TISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVV 419
Cdd:COG4604 3 EIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 420 SQRVDIlngSLRdnlLLADD--------------TASDEKLI-KTLNQVGLEALTtDEGLNawlgdggrQLSGGERRRIG 484
Cdd:COG4604 81 RQENHI---NSR---LTVRElvafgrfpyskgrlTAEDREIIdEAIAYLDLEDLA-DRYLD--------ELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 485 IARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIE--HKTVVFITHRLvNleqM-----DHICLMDHGEIVEQGT 555
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIVLHDI-N---FascyaDHIVAMKDGRVVAQGT 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
352-559 |
5.10e-22 |
|
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: 94.74 E-value: 5.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 352 DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDG---VKLPKwkesSLRSAMSVVSQRV---DI 425
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvVREPR----EVRRRIGIVFQDLsvdDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 426 LNGslRDNLLL------ADDTASDEKLIKTLNQVGL-EAltTDEGLNAWlgdggrqlSGGERRRIGIARALLHDAPIVLL 498
Cdd:cd03265 88 LTG--WENLYIharlygVPGAERRERIDELLDFVGLlEA--ADRLVKTY--------SGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 499 DEPTEGLDQKTEQQIMSVLNKHIEHK--TVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSL 559
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
351-554 |
1.66e-21 |
|
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: 92.73 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 351 ADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVK-----------LPkwKESSLRSAMSVV 419
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiaarnrigyLP--EERGLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 420 SQRVDIlnGSLRdNLLLADDTASDEKLIKTLnqvglealttdeGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLD 499
Cdd:cd03269 89 DQLVYL--AQLK-GLKKEEARRRIDEWLERL------------ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 500 EPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
370-561 |
1.77e-21 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 95.94 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 370 AIVGQTGSGKSTLLQL---LTRqwdPKSGYIAIDG---------VKLPKWK--------ESSLRSAMSVvsqrvdilngs 429
Cdd:COG4148 29 ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGevlqdsargIFLPPHRrrigyvfqEARLFPHLSV----------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 430 lRDNLL-------LADDTASDEKLIKTLnqvGLEALttdeglnawLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPT 502
Cdd:COG4148 95 -RGNLLygrkrapRAERRISFDEVVELL---GIGHL---------LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 503 EGLDQKTEQQIMSVLNK-HIEHKT-VVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:COG4148 162 AALDLARKAEILPYLERlRDELDIpILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLS 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
360-561 |
2.56e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.26 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 360 SLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSA----MSVVSQRVDIL-NGSLRDNL 434
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMpHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 435 LLADDTAS------DEKLIKTLNQVGLEALT---TDEglnawlgdggrqLSGGERRRIGIARALLHDAPIVLLDEPTEGL 505
Cdd:PRK10070 128 AFGMELAGinaeerREKALDALRQVGLENYAhsyPDE------------LSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 506 DQ--KTEQQIMSVLNKHIEHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK10070 196 DPliRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILN 254
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
355-559 |
2.58e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 95.18 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSL---RSAMSVVSQ---------- 421
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQdpyaslnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 422 RV-DILNGSLRDNLLlADDTASDEKLIKTLNQVGLEAlttdEGLNawlgdggR---QLSGGERRRIGIARALLHDAPIVL 497
Cdd:COG4608 113 TVgDIIAEPLRIHGL-ASKAERRERVAELLELVGLRP----EHAD-------RyphEFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 498 LDEPTEGLDQKTEQQIMSVLNK-HIEHK-TVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSL 559
Cdd:COG4608 181 CDEPVSALDVSIQAQVLNLLEDlQDELGlTYLFISHDLSVVRHIsDRVAVMYLGKIVEIAPRDEL 245
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
339-561 |
3.34e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.62 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQY-MDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMS 417
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 418 VVSQRVD--ILNGSLRDNLL--LADDTASDEKLIKTLNqvglEALTTDEGLNAWLGDGGRqLSGGERRRIGIARALLHDA 493
Cdd:PRK13642 85 MVFQNPDnqFVGATVEDDVAfgMENQGIPREEMIKRVD----EALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 494 PIVLLDEPTEGLDQKTEQQIMSVLN--KHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
320-554 |
4.36e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.70 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 320 AEPDTVFDENGVDQAIKGNLTISNVDYQYmdadtnAINAISLDLLSGQKMAIVGQTGSGKST----LLQLLTRQwdpksG 395
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGILKRTVDHNV------VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----G 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 396 YIAIDGVKLPKWKESSL---RSAMSVVSQ--------RVDILN---GSLRDNLLLADDTASDEKLIKTLNQVGLEALTtd 461
Cdd:PRK15134 341 EIWFDGQPLHNLNRRQLlpvRHRIQVVFQdpnsslnpRLNVLQiieEGLRVHQPTLSAAQREQQVIAVMEEVGLDPET-- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 462 eglnawlgdggRQ-----LSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVL----NKHieHKTVVFITHR 532
Cdd:PRK15134 419 -----------RHrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLkslqQKH--QLAYLFISHD 485
|
250 260
....*....|....*....|...
gi 1906086718 533 LVNLEQMDH-ICLMDHGEIVEQG 554
Cdd:PRK15134 486 LHVVRALCHqVIVLRQGEVVEQG 508
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
338-561 |
4.57e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.13 E-value: 4.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 338 NLTISNVDYQY----MDADTnAINAisldllsGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLpkwkesslr 413
Cdd:COG3840 1 MLRLDDLTYRYgdfpLRFDL-TIAA-------GERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 414 sAMSVVSQR-VDIL---NG-----SLRDNLLLADD-----TASD-EKLIKTLNQVGLEALttdeglnawlgdGGR---QL 475
Cdd:COG3840 64 -TALPPAERpVSMLfqeNNlfphlTVAQNIGLGLRpglklTAEQrAQVEQALERVGLAGL------------LDRlpgQL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 476 SGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHK-TVVFITHrlvNLEQM----DHICLMDHGE 549
Cdd:COG3840 131 SGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDElCRERGlTVLMVTH---DPEDAariaDRVLLVADGR 207
|
250
....*....|..
gi 1906086718 550 IVEQGTHDSLLS 561
Cdd:COG3840 208 IAADGPTAALLD 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-555 |
5.75e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.63 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTL----LQLLtrqwDPKSGYIAIDGVKLPKWK------ 408
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTiriiLGIL----APDSGEVLWDGEPLDPEDrrrigy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 409 ---ESSLRSAMSVVSQRVDIlnGSLRDnllLADDTAsdEKLIKTLnqvgLEALttdeGLNAWLGDGGRQLSGGERRRIGI 485
Cdd:COG4152 76 lpeERGLYPKMKVGEQLVYL--ARLKG---LSKAEA--KRRADEW----LERL----GLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 486 ARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQM-DHICLMDHGEIVEQGT 555
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELcDRIVIINKGRKVLSGS 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
359-561 |
5.80e-21 |
|
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: 92.01 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGV---KLPKWKESslrsaMSVVSQRVDIL-NGSLRDNL 434
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEKRD-----ISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 435 ------LLADDTASDEKLIKTLNQVGLEALttdeglnawLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQK 508
Cdd:cd03299 93 ayglkkRKVDKKEIERKVLEIAEMLGIDHL---------LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 509 TEQQIMSVLnKHIEHK---TVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:cd03299 164 TKEKLREEL-KKIRKEfgvTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFK 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
339-555 |
9.15e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.78 E-value: 9.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmDADT----NAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAI-DGVKLPKWKES--- 410
Cdd:PRK13634 3 ITFQKVEHRY-QYKTpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 411 SLRSAMSVVSQ-----------RVDILNGSLrdNLLLADDTAsDEKLIKTLNQVGLealttDEGLnawLGDGGRQLSGGE 479
Cdd:PRK13634 82 PLRKKVGIVFQfpehqlfeetvEKDICFGPM--NFGVSEEDA-KQKAREMIELVGL-----PEEL---LARSPFELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 480 RRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHK-TVVFITHRLVNLEQ-MDHICLMDHGEIVEQGT 555
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlHKEKGlTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
346-552 |
2.37e-20 |
|
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: 89.72 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 346 YQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLpkwkesslrSAMSVvSQRVDI 425
Cdd:TIGR02211 11 YQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSL---------SKLSS-NERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 426 LNGSL----RDNLLLADDTA-----------------SDEKLIKTLNQVGLEalttdEGLNAWLGdggrQLSGGERRRIG 484
Cdd:TIGR02211 81 RNKKLgfiyQFHHLLPDFTAlenvamplligkksvkeAKERAYEMLEKVGLE-----HRINHRPS----ELSGGERQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 485 IARALLHDAPIVLLDEPTEGLDQKTEQQI---MSVLNKhiEHKT-VVFITHRLVNLEQMDHICLMDHGEIVE 552
Cdd:TIGR02211 152 IARALVNQPSLVLADEPTGNLDNNNAKIIfdlMLELNR--ELNTsFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
339-555 |
2.62e-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: 92.47 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVK---LPKWKesslRSa 415
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtgLPPEK----RN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 416 MSVVSQrvdilNGSL------RDN------LLLADDTASDEKLIKTLNQVGLEALttdeglnawlgdGGR---QLSGGER 480
Cdd:COG3842 79 VGMVFQ-----DYALfphltvAENvafglrMRGVPKAEIRARVAELLELVGLEGL------------ADRyphQLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 481 RRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLnKHIeHK----TVVFITHRLvnLEQM---DHICLMDHGEIVEQ 553
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREEL-RRL-QRelgiTFIYVTHDQ--EEALalaDRIAVMNDGRIEQV 217
|
..
gi 1906086718 554 GT 555
Cdd:COG3842 218 GT 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
339-561 |
2.71e-20 |
|
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: 94.37 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISN--VDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKS----TLLQLLTRQWDPKSGYIAIDGVKLPKWKESSL 412
Cdd:COG4172 7 LSVEDlsVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 413 RS------AM-------------SVVSQRVDILngSLRDNLllaDDTASDEKLIKTLNQVGLEAltTDEGLNAWlgdgGR 473
Cdd:COG4172 87 RRirgnriAMifqepmtslnplhTIGKQIAEVL--RLHRGL---SGAAARARALELLERVGIPD--PERRLDAY----PH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 474 QLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLN--KHIEHKTVVFITHRLVNLEQM-DHICLMDHGEI 550
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKdlQRELGMALLLITHDLGVVRRFaDRVAVMRQGEI 235
|
250
....*....|.
gi 1906086718 551 VEQGTHDSLLS 561
Cdd:COG4172 236 VEQGPTAELFA 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
355-561 |
3.14e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.95 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDG---VKLPKWKESSLRSAMSVVSQ---------- 421
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdlLKADPEAQKLLRQKIQIVFQnpygslnprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 422 RV-DILNGSLRDNlllADDTASD--EKLIKTLNQVGLEALTTDeglnawlgdggR---QLSGGERRRIGIARALLHDAPI 495
Cdd:PRK11308 110 KVgQILEEPLLIN---TSLSAAErrEKALAMMAKVGLRPEHYD-----------RyphMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 496 VLLDEPTEGLDQKTEQQimsVLNKHIE-----HKTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK11308 176 VVADEPVSALDVSVQAQ---VLNLMMDlqqelGLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIFN 244
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
339-554 |
5.72e-20 |
|
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: 88.43 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQrvdILNGSL--RDNLLLADDTA--SDEKLIKTLNQVGLEALTTDEGlnawlgdggRQLSGGERRRIGIARALLHDAP 494
Cdd:cd03268 79 EAP---GFYPNLtaRENLRLLARLLgiRKKRIDEVLDVVGLKDSAKKKV---------KGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 495 IVLLDEPTEGLDQ---KTEQQIMSVLNKhiEHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:cd03268 147 LLILDEPTNGLDPdgiKELRELILSLRD--QGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
356-563 |
6.32e-20 |
|
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: 89.86 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRS-----------AMSVVSQRV- 423
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvqlvfqdSPSAVNPRMt 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 424 --DILNGSLRdNLLLADDTASDEKLIKTLNQVGLEALTTDEGlnawlgdgGRQLSGGERRRIGIARALLHDAPIVLLDEP 501
Cdd:TIGR02769 107 vrQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKL--------PRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 502 TEGLDQKTEQQIMSVLNKHIEH--KTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLSLK 563
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
310-561 |
7.57e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 94.03 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 310 SARRLNEIITAEPDTVFDENGVDQAIKGnLTISNVDYQY-MDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTR 388
Cdd:PLN03130 587 SLKRLEELLLAEERVLLPNPPLEPGLPA-ISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 389 QWDPKSGYIAIdgvklpkwkessLRSAMSVVSQRVDILNGSLRDNLLLAD--DTASDEKLIK-TLNQVGLEALTTdeGLN 465
Cdd:PLN03130 666 ELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSpfDPERYERAIDvTALQHDLDLLPG--GDL 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 466 AWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIM-SVLNKHIEHKTVVFITHRLVNLEQMDHICL 544
Cdd:PLN03130 732 TEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDELRGKTRVLVTNQLHFLSQVDRIIL 811
|
250
....*....|....*..
gi 1906086718 545 MDHGEIVEQGTHDSLLS 561
Cdd:PLN03130 812 VHEGMIKEEGTYEELSN 828
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
355-555 |
8.47e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 90.68 E-value: 8.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGV------------------KLPKWKEssLRSAM 416
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknnhelitnpyskKIKNFKE--LRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQ-----------RVDILNGSLRdnlLLADDTASDEKLIKTLNQVGLEalttdeglNAWLGDGGRQLSGGERRRIGI 485
Cdd:PRK13631 119 SMVFQfpeyqlfkdtiEKDIMFGPVA---LGVKKSEAKKLAKFYLNKMGLD--------DSYLERSPFGLSGGQKRRVAI 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 486 ARALLHDAPIVLLDEPTEGLDQKTEQQIMS-VLNKHIEHKTVVFITHRLVN-LEQMDHICLMDHGEIVEQGT 555
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQlILDAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGT 259
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
356-555 |
8.98e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.06 E-value: 8.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWK--ESSLRSAM----SVVS-----QRVD 424
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaELARRRAVlpqhSSLSfpftvEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 425 ILNGSLRDNLLLADDTASDEKLiktlNQVGLEALttdeglnawlgdGGR---QLSGGERRRIGIARALL------HDAPI 495
Cdd:PRK13548 98 AMGRAPHGLSRAEDDALVAAAL----AQVDLAHL------------AGRdypQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 496 VLLDEPTEGLDQKTEQQIMSVLNK--HIEHKTVVFITHRLvNLEQM--DHICLMDHGEIVEQGT 555
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQlaHERGLAVIVVLHDL-NLAARyaDRIVLLHQGRLVADGT 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
339-555 |
1.16e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.52 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQL---LTrqwDPKSGYIAIDGV---KLPKWKessl 412
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMiagLE---DPTSGEILIGGRdvtDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 413 RS-AMsvVSQRvDIL--NGSLRDN----LLLADDTAS--DEKLIKTLNQVGLEALttdegLNawlgdggR---QLSGGER 480
Cdd:COG3839 75 RNiAM--VFQS-YALypHMTVYENiafpLKLRKVPKAeiDRRVREAAELLGLEDL-----LD-------RkpkQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 481 RRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHK-TVVFITHRLVnlEQM---DHICLMDHGEIVEQGT 555
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRlHRRLGtTTIYVTHDQV--EAMtlaDRIAVMNDGRIQQVGT 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
339-557 |
1.17e-19 |
|
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: 88.17 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDAdtNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPK-----------W 407
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvpvqernvgfvF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 408 KESSLRSAMSV---VSQRVDILNGSLRDNllladDTASDEKLIKTLNQVGLEalttdeglnaWLGDggR---QLSGGERR 481
Cdd:cd03296 81 QHYALFRHMTVfdnVAFGLRVKPRSERPP-----EAEIRAKVHELLKLVQLD----------WLAD--RypaQLSGGQRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 482 RIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIE-HKTVVFITH-RLVNLEQMDHICLMDHGEIVEQGTHD 557
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRlHDElHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPD 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
284-559 |
1.26e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 93.50 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 284 AFATMASFELL-MPIAGAFQYLGQTLS---SARRLNEIITAEpDTVFDENGVDQAIKGNLTISNVDYQYMDADTN-AINA 358
Cdd:PLN03232 557 AFTSLSLFAVLrSPLNMLPNLLSQVVNanvSLQRIEELLLSE-ERILAQNPPLQPGAPAISIKNGYFSWDSKTSKpTLSD 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQwdpksgyiaidgvkLPKWKESS--LRSAMSVVSQRVDILNGSLRDNLLL 436
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGE--------------LSHAETSSvvIRGSVAYVPQVSWIFNATVRENILF 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 437 ADDTASDekliKTLNQVGLEALTTDEGLNAW-----LGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQ 511
Cdd:PLN03232 702 GSDFESE----RYWRAIDVTALQHDLDLLPGrdlteIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1906086718 512 QIMSVLNKH-IEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSL 559
Cdd:PLN03232 778 QVFDSCMKDeLKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
359-554 |
2.17e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.92 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIaidgvklpkWKESSLrsamSVVSQRVDILNGSLRDNLLLAD 438
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERSI----AYVPQQAWIMNATVRGNILFFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 439 --DTASDEKLIKtLNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIM-S 515
Cdd:PTZ00243 746 eeDAARLADAVR-VSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeE 824
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906086718 516 VLNKHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQG 554
Cdd:PTZ00243 825 CFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
288-569 |
3.35e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 92.01 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 288 MASFELLMPIAGAFQYLgQTLSSARRLNEIITAEPDTVFDENGVDQAIKGNLTISNVDYQY-MDADTNAINAISLDLLSG 366
Cdd:PTZ00265 333 ISMFMLTIILPNITEYM-KSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYdTRKDVEIYKDLNFTLTEG 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 367 QKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDG------VKLPKWkesslRSAMSVVSQRVDILNGSLRDNLLLADDT 440
Cdd:PTZ00265 412 KTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdINLKWW-----RSKIGVVSQDPLLFSNSIKNNIKYSLYS 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 441 ASD-EKLIKTLNQVG------------------------LEALTTDEGLNA----------------------------- 466
Cdd:PTZ00265 487 LKDlEALSNYYNEDGndsqenknkrnscrakcagdlndmSNTTDSNELIEMrknyqtikdsevvdvskkvlihdfvsalp 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 467 -----WLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLN--KHIEHKTVVFITHRLVNLEQM 539
Cdd:PTZ00265 567 dkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYA 646
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 540 DHICLMDHGE-----------------------------------------------IVEQGTHDSLLSLK-GAYHQL 569
Cdd:PTZ00265 647 NTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYYTM 724
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
339-555 |
3.67e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.83 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDaDTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLpKWKESSL---RSA 415
Cdd:PRK13639 2 LETRDLKYSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 416 MSVVSQ---------RV--DILNGSLrdNLLLADDTAsDEKLIKTLNQVGLEALTTDEGlnawlgdggRQLSGGERRRIG 484
Cdd:PRK13639 80 VGIVFQnpddqlfapTVeeDVAFGPL--NLGLSKEEV-EKRVKEALKAVGMEGFENKPP---------HHLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 485 IARALLHDAPIVLLDEPTEGLDQKTEQQIMSV---LNKhiEHKTVVFITHRlVNLEQM--DHICLMDHGEIVEQGT 555
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLlydLNK--EGITIIISTHD-VDLVPVyaDKVYVMSDGKIIKEGT 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
359-561 |
3.76e-19 |
|
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: 89.02 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQL---LTRqwdPKSGYIAIDGVKlpkWKESSLRSAMSVVSQRVDIL--------N 427
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLiagLTR---PDEGEIVLNGRT---LFDSRKGIFLPPEKRRIGYVfqearlfpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 428 GSLRDNLLL-------ADDTASDEKLIKTLnqvGLEALttdeglnawLGDGGRQLSGGERRRIGIARALLHDAPIVLLDE 500
Cdd:TIGR02142 90 LSVRGNLRYgmkrarpSERRISFERVIELL---GIGHL---------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 501 PTEGLDQKTEQQIMSVLNK-HIEHKT-VVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERlHAEFGIpILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
352-554 |
3.77e-19 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 86.15 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 352 DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMsvVSQrvdilNGSLR 431
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAM--VFQ-----NYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 432 DNLLLADDTAS------------DEKLIKTLNQVGLEALttdeglnawLGDGGRQLSGGERRRIGIARALLHDAPIVLLD 499
Cdd:cd03301 85 PHMTVYDNIAFglklrkvpkdeiDERVREVAELLQIEHL---------LDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 500 EPTEGLDQKTEQQIMSVLNK-HIEHK-TVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRlQQRLGtTTIYVTHDQVEAMTMaDRIAVMNDGQIQQIG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
355-554 |
3.99e-19 |
|
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: 86.27 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESslrsamsvVSQRVDILNG------ 428
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE--------ARRRLGFVSDstglyd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 429 --SLRDNLL-------LADDTASD--EKLIKTLnqvglealttdeGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVL 497
Cdd:cd03266 92 rlTARENLEyfaglygLKGDELTArlEELADRL------------GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 498 LDEPTEGLDQKTEQQIMSVLnKHI--EHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:cd03266 160 LDEPTTGLDVMATRALREFI-RQLraLGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
339-555 |
4.42e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.50 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQ-----------RVDILNGsLRDNLLLADDTAsdEKLIKTLNQVGLEALTTDEglnawlgdgGRQLSGGERRRIGIAR 487
Cdd:PRK13648 88 VFQnpdnqfvgsivKYDVAFG-LENHAVPYDEMH--RRVSEALKQVDMLERADYE---------PNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 488 ALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHK--TVVFITHRLVNLEQMDHICLMDHGEIVEQGT 555
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
339-555 |
4.53e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.55 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQL----LTRQWDPKSgYIAIDGVKLPKWKESSLRS 414
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLinglLLPDDNPNS-KITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 415 AMSVVSQRVD--ILNGSLRDNLL--LADDTASDEKLIK----TLNQVGLEALTTDEGLNawlgdggrqLSGGERRRIGIA 486
Cdd:PRK13640 85 KVGIVFQNPDnqFVGATVGDDVAfgLENRAVPRPEMIKivrdVLADVGMLDYIDSEPAN---------LSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 487 RALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHK--TVVFITHRLVNLEQMDHICLMDHGEIVEQGT 555
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
338-557 |
4.99e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 338 NLTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKL-----PKWKES-S 411
Cdd:COG4161 2 SIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkPSEKAIrL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 412 LRSAMSVVSQRVDIL-NGSLRDNLLLA-------DDTASDEKLIKTLNQVGLealttDEGLNAWlgdgGRQLSGGERRRI 483
Cdd:COG4161 80 LRQKVGMVFQQYNLWpHLTVMENLIEApckvlglSKEQAREKAMKLLARLRL-----TDKADRF----PLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 484 GIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHK-TVVFITHRL-VNLEQMDHICLMDHGEIVEQGTHD 557
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVeFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
355-555 |
5.13e-19 |
|
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: 87.02 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKeSSLRSAMSVVS--QRVDILNG-SLR 431
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIARtfQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 432 DNLLLADDTASDEKLIKTLNQVGL----EALTTDE--------GLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLD 499
Cdd:COG0411 98 ENVLVAAHARLGRGLLAALLRLPRarreEREARERaeellervGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 500 EPTEGLDQKTEQQIMSVLNK--HIEHKTVVFITH--RLVnleqM---DHICLMDHGEIVEQGT 555
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRlrDERGITILLIEHdmDLV----MglaDRIVVLDFGRVIAEGT 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
309-557 |
5.45e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.35 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 309 SSARRLNEIITAEPDTVFDEngVDQAIKGNLT-----ISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLL 383
Cdd:PRK13536 9 EAPRRLELSPIERKHQGISE--AKASIPGSMStvaidLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 384 QLLTRQWDPKSGYIAIDGVKLPKwKESSLRSAMSVVSQ--RVDiLNGSLRDNLLLAD-----DTASDEKLIKTLnqvgLE 456
Cdd:PRK13536 85 RMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQfdNLD-LEFTVRENLLVFGryfgmSTREIEAVIPSL----LE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 457 ALTTDEGLNAWLGDggrqLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVN 535
Cdd:PRK13536 159 FARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTHFMEE 234
|
250 260
....*....|....*....|....
gi 1906086718 536 LEQM-DHICLMDHG-EIVEQGTHD 557
Cdd:PRK13536 235 AERLcDRLCVLEAGrKIAEGRPHA 258
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
339-555 |
8.30e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 87.89 E-value: 8.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQ----LLTrqwdPKSGYIAIDGVKLPKWKESSLRS 414
Cdd:COG1118 3 IEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRiiagLET----PDSGRIVLNGRDLFTNLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 415 A------------MSVvsqrvdilngslRDNL------LLADDTASDEKLIKTLNQVGLEalttdeglnaWLGDggR--- 473
Cdd:COG1118 77 VgfvfqhyalfphMTV------------AENIafglrvRPPSKAEIRARVEELLELVQLE----------GLAD--Ryps 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 474 QLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIE-HKTVVFITHRLvnLEQM---DHICLMDHG 548
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlHDElGGTTVFVTHDQ--EEALelaDRVVVMNQG 210
|
....*..
gi 1906086718 549 EIVEQGT 555
Cdd:COG1118 211 RIEQVGT 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
339-572 |
8.31e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 86.66 E-value: 8.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNA-------INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESS 411
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 412 LRS-----------AMSVVSQRVD---ILNGSLRdNLLLADDTASDEKLIKTLNQVGLEALTTDEgLNAwlgdggrQLSG 477
Cdd:PRK10419 84 RKAfrrdiqmvfqdSISAVNPRKTvreIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSVLDK-RPP-------QLSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 478 GERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLnKHIEHKT---VVFITHRLVNLEQMDHICL-MDHGEIVEQ 553
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLL-KKLQQQFgtaCLFITHDLRLVERFCQRVMvMDNGQIVET 233
|
250
....*....|....*....
gi 1906086718 554 GTHDSLLSLKGAYHQLWQR 572
Cdd:PRK10419 234 QPVGDKLTFSSPAGRVLQN 252
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
343-555 |
1.00e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 343 NVDYQYmDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQR 422
Cdd:PRK13652 8 DLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 423 VD--ILNGSLRDNL------LLADDTASDEKLIKTLNQVGLEALTTDeglnawlgdGGRQLSGGERRRIGIARALLHDAP 494
Cdd:PRK13652 87 PDdqIFSPTVEQDIafgpinLGLDEETVAHRVSSALHMLGLEELRDR---------VPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 495 IVLLDEPTEGLDQKTEQQIMSVLNKHIEH--KTVVFITHRLVNLEQM-DHICLMDHGEIVEQGT 555
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGT 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
339-531 |
1.14e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.07 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQY--MDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVklPKWKESSLRSam 416
Cdd:COG4525 4 LTVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV--PVTGPGADRG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 sVVSQRVDILNG-SLRDNLLLA------DDTASDEKLIKTLNQVGLEALttdEGLNAWlgdggrQLSGGERRRIGIARAL 489
Cdd:COG4525 80 -VVFQKDALLPWlNVLDNVAFGlrlrgvPKAERRARAEELLALVGLADF---ARRRIW------QLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1906086718 490 LHDAPIVLLDEPTEGLDQKTEQQIMSVLNK--HIEHKTVVFITH 531
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
355-555 |
1.17e-18 |
|
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: 85.18 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESsLRSAMSVVS--QRVDILNG-SLR 431
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 432 DNLLLA----------------DDTASDEKLIKTLNQVGLEALttdeglnawLGDGGRQLSGGERRRIGIARALLHDAPI 495
Cdd:cd03219 94 ENVMVAaqartgsglllararrEEREARERAEELLERVGLADL---------ADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 496 VLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRL-VNLEQMDHICLMDHGEIVEQGT 555
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMdVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
339-555 |
1.27e-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: 84.98 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGV---KLPKWKESslrsa 415
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditNLPPHKRP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 416 MSVVSQrvdilNGSLRDNLLLADDTA-------SDEKLIK-----TLNQVGLEALttdeglnawlgdGGR---QLSGGER 480
Cdd:cd03300 74 VNTVFQ-----NYALFPHLTVFENIAfglrlkkLPKAEIKervaeALDLVQLEGY------------ANRkpsQLSGGQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 481 RRIGIARALLHDAPIVLLDEPTEGLDQKTEQQiMSVLNKHIEHK---TVVFITHRlvNLEQM---DHICLMDHGEIVEQG 554
Cdd:cd03300 137 QRVAIARALVNEPKVLLLDEPLGALDLKLRKD-MQLELKRLQKElgiTFVFVTHD--QEEALtmsDRIAVMNKGKIQQIG 213
|
.
gi 1906086718 555 T 555
Cdd:cd03300 214 T 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
355-545 |
1.36e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.82 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKW--KESSLRSAMSV-VSQRVDIlnGSLR 431
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYvpQRSEVPDSLPLtVRDLVAM--GRWA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 432 DNLLLADDTASDEKLI-KTLNQVGLEALttdeglnawlgdGGRQ---LSGGERRRIGIARALLHDAPIVLLDEPTEGLDQ 507
Cdd:NF040873 85 RRGLWRRLTRDDRAAVdDALERVGLADL------------AGRQlgeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906086718 508 KTEQQIMSVLNK-HIEHKTVVFITHRLVNLEQMDHICLM 545
Cdd:NF040873 153 ESRERIIALLAEeHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
354-561 |
1.58e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.61 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 354 NAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLP----KWKESSLRSAMSVVS------QRV 423
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQRIRMIFQDPStslnprQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 424 -DILNGSLRDNLLLaDDTASDEKLIKTLNQVGLealttdegLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPT 502
Cdd:PRK15112 107 sQILDFPLRLNTDL-EPEQREKQIIETLRQVGL--------LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 503 EGLDQKTEQQIMSVLNKHIEHKTVVFItHRLVNLEQMDHIC----LMDHGEIVEQG-THDSLLS 561
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYI-YVTQHLGMMKHISdqvlVMHQGEVVERGsTADVLAS 240
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
352-531 |
2.56e-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: 83.24 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 352 DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLpKWKESSLRSamsvVSQRVDILNGSLR 431
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLE----RRQRVGLVFQDPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 432 DNLLLADdtaSDEKLIKTLNQVGLEA----LTTDEGLNAWLGDGGR-----QLSGGERRRIGIARALLHDAPIVLLDEPT 502
Cdd:TIGR01166 79 DQLFAAD---VDQDVAFGPLNLGLSEaeveRRVREALTAVGASGLRerpthCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 1906086718 503 EGLDQKTEQQIMSVLNKHIEH-KTVVFITH 531
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEgMTVVISTH 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
339-555 |
4.01e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.80 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDA---DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKL---PKWKE-SS 411
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 412 LRSAMSVVSQrvdILNGSLRDNLLLaDDTA--------SDEKLIKT----LNQVGLealttDEGLnawLGDGGRQLSGGE 479
Cdd:PRK13649 83 IRKKVGLVFQ---FPESQLFEETVL-KDVAfgpqnfgvSQEEAEALarekLALVGI-----SESL---FEKNPFELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 480 RRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRLVNL-EQMDHICLMDHGEIVEQGT 555
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
346-565 |
4.08e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.71 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 346 YQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLpkwkeSSLRSAmsvvsQRVDI 425
Cdd:PRK11629 15 YQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM-----SKLSSA-----AKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 426 LNGSL----RDNLLLADDTA-----------------SDEKLIKTLNQVGLEALTTDEGlnawlgdggRQLSGGERRRIG 484
Cdd:PRK11629 85 RNQKLgfiyQFHHLLPDFTAlenvamplligkkkpaeINSRALEMLAAVGLEHRANHRP---------SELSGGERQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 485 IARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVF--ITHRLVNLEQMDHICLMDHGEIVEQgthdslLSL 562
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFlvVTHDLQLAKRMSRQLEMRDGRLTAE------LSL 229
|
...
gi 1906086718 563 KGA 565
Cdd:PRK11629 230 MGA 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
352-551 |
4.18e-18 |
|
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: 81.71 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 352 DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWkesSLRSAmsvvsqrvdilngslr 431
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA---SPRDA---------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 432 dnllladdtasdekliktlNQVGLEALTtdeglnawlgdggrQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQ 511
Cdd:cd03216 73 -------------------RRAGIAMVY--------------QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906086718 512 QIMSVLNK-HIEHKTVVFITHRLVNLEQM-DHICLMDHGEIV 551
Cdd:cd03216 120 RLFKVIRRlRAQGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
341-558 |
4.78e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.53 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 341 ISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKL-----PKWKE-SSLRS 414
Cdd:PRK11124 5 LNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktPSDKAiRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 415 AMSVVSQRVDIL-NGSLRDNLLLA-------DDTASDEKLIKTLNQVGLEALTtdeglNAWlgdgGRQLSGGERRRIGIA 486
Cdd:PRK11124 83 NVGMVFQQYNLWpHLTVQQNLIEApcrvlglSKDQALARAEKLLERLRLKPYA-----DRF----PLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 487 RALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIE-HKTVVFITHRlVNLEQ--MDHICLMDHGEIVEQGTHDS 558
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHE-VEVARktASRVVYMENGHIVEQGDASC 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
339-557 |
4.93e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQymdADTNAI-NAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMS 417
Cdd:PRK10247 8 LQLQNVGYL---AGDAKIlNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 418 VVSQRVDILNGSLRDNLL----LADDTASDEKLIKTLNQVGLEALTTDEGLNAwlgdggrqLSGGERRRIGIARALLHDA 493
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIfpwqIRNQQPDPAIFLDDLERFALPDTILTKNIAE--------LSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 494 PIVLLDEPTEGLDQKTEQQIMSVLNKHIEHK--TVVFITHRLVNLEQMDH-ICLMDHGEIVEQGTHD 557
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKvITLQPHAGEMQEARYE 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
356-547 |
5.45e-18 |
|
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: 81.43 E-value: 5.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIaidgvklpkwkESSLRSAMSVVSQRVDILNGSLRDNLL 435
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFLPQRPYLPLGTLREQLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 436 LAddtasdekliktlnqvglealttdeglnaWlgdgGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMS 515
Cdd:cd03223 86 YP-----------------------------W----DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ 132
|
170 180 190
....*....|....*....|....*....|..
gi 1906086718 516 VLNKHieHKTVVFITHRLVNLEQMDHICLMDH 547
Cdd:cd03223 133 LLKEL--GITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
356-561 |
9.80e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.88 E-value: 9.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYI-----AIDGVKLPKWKESSLRSamsvVSQRVdilnGSL 430
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGLIRQ----LRQHV----GFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 431 RDNLLLADDTASDEKLIKTLNQVGLE----ALTTDEGLNAWLGDGG------RQLSGGERRRIGIARALLHDAPIVLLDE 500
Cdd:PRK11264 91 FQNFNLFPHRTVLENIIEGPVIVKGEpkeeATARARELLAKVGLAGketsypRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 501 PTEGLDQKTEQQIMSVLNKHIEHK-TVVFITHRL-VNLEQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMsFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
339-531 |
1.02e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.21 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLpkwkeSSLRSAMSV 418
Cdd:PRK11248 2 LQISHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILN-GSLRDN----LLLA--DDTASDEKLIKTLNQVGLEalttdeglnawlGDGGR---QLSGGERRRIGIARA 488
Cdd:PRK11248 75 VFQNEGLLPwRNVQDNvafgLQLAgvEKMQRLEIAHQMLKKVGLE------------GAEKRyiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1906086718 489 LLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK--HIEHKTVVFITH 531
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
339-554 |
1.10e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 83.16 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWD--PK---SGYIAIDGVKL--PKWKESS 411
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 412 LRSAMSVVSQRVDILNGSLRDNLLLA-------DDTASDEKLIKTLNQVGLealttdeglnaW------LGDGGRQLSGG 478
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgikSKSELDEIVEESLRKAAL-----------WdevkdrLKKSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 479 ERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQI---MSVLNKHIehkTVVFITHrlvNLEQM----DHICLMDHGEIV 551
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIeelILELKKDY---TIVIVTH---NMQQAarvsDYTAFFYLGELV 232
|
...
gi 1906086718 552 EQG 554
Cdd:COG1117 233 EFG 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
341-561 |
1.69e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.73 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 341 ISNVDYQYMDAdTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKW-KESSLRSAMSVV 419
Cdd:PRK13644 4 LENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 420 SQ--RVDILNGSLRDNLLLADD------TASDEKLIKTLNQVGLEAlttdeglnaWLGDGGRQLSGGERRRIGIARALLH 491
Cdd:PRK13644 83 FQnpETQFVGRTVEEDLAFGPEnlclppIEIRKRVDRALAEIGLEK---------YRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 492 DAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
341-554 |
2.69e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.09 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 341 ISNVDYQYMDaDTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVS 420
Cdd:PRK13647 7 VEDLHFRYKD-GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 421 QRVD--ILNGSLRD-------NLLLADDTAsDEKLIKTLNQVGLEALTTdeglnawlgDGGRQLSGGERRRIGIARALLH 491
Cdd:PRK13647 86 QDPDdqVFSSTVWDdvafgpvNMGLDKDEV-ERRVEEALKAVRMWDFRD---------KPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 492 DAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRL-VNLEQMDHICLMDHGEIVEQG 554
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVdLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
359-538 |
3.14e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 80.23 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQrvDILNGSL--RDNLLL 436
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHA--PGIKTTLsvLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 437 ADDTASDEKLIKTLNQVGLEALttdEGLNAwlgdggRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSV 516
Cdd:cd03231 97 WHADHSDEQVEEALARVGLNGF---EDRPV------AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170 180
....*....|....*....|...
gi 1906086718 517 LNKHIEH-KTVVFITHRLVNLEQ 538
Cdd:cd03231 168 MAGHCARgGMVVLTTHQDLGLSE 190
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
356-561 |
3.34e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.55 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDG--VKLPKWKES-----------SLRSAMSVVSQR 422
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtINLVRDKDGqlkvadknqlrLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 423 VDILNG-SLRDNLLLA-------DDTASDEKLIKTLNQVGLEALTTdeglnawlGDGGRQLSGGERRRIGIARALLHDAP 494
Cdd:PRK10619 101 FNLWSHmTVLENVMEApiqvlglSKQEARERAVKYLAKVGIDERAQ--------GKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 495 IVLLDEPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
343-561 |
3.59e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.29 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 343 NVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDG--VKLPKWKESSLRSAMSVVS 420
Cdd:PRK09493 6 NVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 421 QRV----------DILNGSLRdnlLLADDTASDEKLIKTL-NQVGLEalttdEGLNAWLGdggrQLSGGERRRIGIARAL 489
Cdd:PRK09493 84 QQFylfphltaleNVMFGPLR---VRGASKEEAEKQARELlAKVGLA-----ERAHHYPS----ELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 490 LHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
353-557 |
3.76e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.21 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 353 TNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPK-----------WKESSLRSAMSV--- 418
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhardrkvgfvFQHYALFRHMTVfdn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNGSLRDNLlladdTASDEKLIKTLNQVGLEALTTdeglnawlgdggR---QLSGGERRRIGIARALLHDAPI 495
Cdd:PRK10851 95 IAFGLTVLPRRERPNA-----AAIKAKVTQLLEMVQLAHLAD------------RypaQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 496 VLLDEPTEGLDQKTEQQIMSVLNK-HIEHK-TVVFITH-RLVNLEQMDHICLMDHGEIVEQGTHD 557
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQlHEELKfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
354-559 |
4.80e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.06 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 354 NAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAI--------------------DGVKLPKWKE---- 409
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekekvlekLVIQKTRFKKikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 410 SSLRSAMSVVSQ-----------RVDILNGSLRdnlLLADDTASDEKLIKTLNQVGLealttDEglnAWLGDGGRQLSGG 478
Cdd:PRK13651 101 KEIRRRVGVVFQfaeyqlfeqtiEKDIIFGPVS---MGVSKEEAKKRAAKYIELVGL-----DE---SYLQRSPFELSGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 479 ERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRLVN-LEQMDHICLMDHGEIVEQG-T 555
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNvLEWTKRTIFFKDGKIIKDGdT 249
|
....
gi 1906086718 556 HDSL 559
Cdd:PRK13651 250 YDIL 253
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
343-555 |
5.06e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.67 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 343 NVDYQYMDADTN----AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPK----WKessLRS 414
Cdd:PRK13633 9 NVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeenlWD---IRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 415 AMSVVSQRvdilngslRDNLLLA----DDTA-SDEKL------IKTLNQVGLEALttdeGLNAWLGDGGRQLSGGERRRI 483
Cdd:PRK13633 86 KAGMVFQN--------PDNQIVAtiveEDVAfGPENLgippeeIRERVDESLKKV----GMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 484 GIARALLHDAPIVLLDEPTEGLDQKTEQQIMSV---LNKhIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGT 555
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTikeLNK-KYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
337-555 |
5.09e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.59 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 337 GNLTISNVDYQYMDA---DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLP----KWKE 409
Cdd:PRK13645 5 KDIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 410 -SSLRSAMSVVSQ-----------RVDILNGSLRdnlLLADDTASDEKLIKTLNQVGLEalttdeglNAWLGDGGRQLSG 477
Cdd:PRK13645 85 vKRLRKEIGLVFQfpeyqlfqetiEKDIAFGPVN---LGENKQEAYKKVPELLKLVQLP--------EDYVKRSPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 478 GERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSV---LNKHiEHKTVVFITHrlvNLEQM----DHICLMDHGEI 550
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLferLNKE-YKKRIIMVTH---NMDQVlriaDEVIVMHEGKV 229
|
....*
gi 1906086718 551 VEQGT 555
Cdd:PRK13645 230 ISIGS 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
339-560 |
7.08e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.78 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKwKESSLRSAMSV 418
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQrVDILNG--SLRDNLLL-----ADDTASDEKLIKTLnqvgLEALTTDEGLNAWLGDggrqLSGGERRRIGIARALLH 491
Cdd:PRK13537 85 VPQ-FDNLDPdfTVRENLLVfgryfGLSAAAARALVPPL----LEFAKLENKADAKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 492 DAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLL 560
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALI 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
339-559 |
7.13e-17 |
|
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: 79.88 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWK-ESSLRSAMS 417
Cdd:TIGR03410 1 LEVSNLNVYY--GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 418 VVSQRVDILNG-SLRDNLLL-ADDTASDEKLIKTlnqvglEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPI 495
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLLTgLAALPRRSRKIPD------EIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 496 VLLDEPTEGLDQKTEQQIMSVLNKHIEHK--TVVFITHRL-VNLEQMDHICLMDHGEIVEQGTHDSL 559
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLdFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
355-551 |
7.35e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.52 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSlRSAMsvVSqRV--DILNG---- 428
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKY--IG-RVfqDPMMGtaps 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 429 -SLRDNLLLAD---------------DTASDEKLIKTLNQvGLEA-LTTDEGLnawlgdggrqLSGGERRRIGIARALLH 491
Cdd:COG1101 97 mTIEENLALAYrrgkrrglrrgltkkRRELFRELLATLGL-GLENrLDTKVGL----------LSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 492 DAPIVLLDEPTEGLDQKTEQQIMSVLNKHI-EHK-TVVFITHrlvNLEQ-MDH---ICLMDHGEIV 551
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIVeENNlTTLMVTH---NMEQaLDYgnrLIMMHEGRII 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
359-550 |
9.58e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 9.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDgvklPKWKesslrsaMSVVSQRVDIL-NGSLRDNLLLA 437
Cdd:COG0488 17 VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGLR-------IGYLPQEPPLDdDLTVLDTVLDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 438 DDTASDekLIKTLNQVGLEALTTD-------------EGLNAW------------LG----DGGRQ---LSGGERRRIGI 485
Cdd:COG0488 86 DAELRA--LEAELEELEAKLAEPDedlerlaelqeefEALGGWeaearaeeilsgLGfpeeDLDRPvseLSGGWRRRVAL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 486 ARALLHDAPIVLLDEPTEGLDqkteqqIMSV------LNKHieHKTVVFITH------RLVNleqmdHICLMDHGEI 550
Cdd:COG0488 164 ARALLSEPDLLLLDEPTNHLD------LESIewleefLKNY--PGTVLVVSHdryfldRVAT-----RILELDRGKL 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
355-555 |
1.24e-16 |
|
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: 83.91 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwkeSSLRSAMSVVSQRvdiLNGSLRDNL 434
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG--------KDIETNLDAVRQS---LGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 435 LLADDTASDEKLIKTL--------NQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLD 506
Cdd:TIGR01257 1014 LFHHLTVAEHILFYAQlkgrsweeAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1906086718 507 QKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQGT 555
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
339-555 |
1.35e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.55 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDAD---TNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAI-DGVKLPKWKESSLRS 414
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 415 AMSVVSQRVDILNGSLRDNLLLADDTASDEKL---IKTLNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLH 491
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPQNFgipKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 492 DAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRLVNL-EQMDHICLMDHGEIVEQGT 555
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGT 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
355-554 |
1.41e-16 |
|
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: 79.30 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVkLPkWKESS-LRSAMSVV-SQRVD-ILNGSLR 431
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VP-WKRRKkFLRRIGVVfGQKTQlWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 432 DNLLLADDT--ASDEKLIKTLNQVGlEALTTDEGLNAWLgdggRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLD--- 506
Cdd:cd03267 114 DSFYLLAAIydLPPARFKKRLDELS-ELLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDvva 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1906086718 507 QKTEQQIMSVLNKhiEHKTVVFIT-HRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:cd03267 189 QENIRNFLKEYNR--ERGTTVLLTsHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
339-566 |
1.97e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 78.87 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWK-ESSLRSAMS 417
Cdd:COG0410 4 LEVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 418 VVSQRVDILnGSL--RDNLLLADDTASDEKLIK-TLNQVG-----LEALttdeglnawLGDGGRQLSGGERRRIGIARAL 489
Cdd:COG0410 82 YVPEGRRIF-PSLtvEENLLLGAYARRDRAEVRaDLERVYelfprLKER---------RRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 490 LHDAPIVLLDEPTEGLDQKTEQQIMSVLnKHI--EHKTVVfithrLVnlEQM--------DHICLMDHGEIVEQGTHDSL 559
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEII-RRLnrEGVTIL-----LV--EQNarfaleiaDRAYVLERGRIVLEGTAAEL 223
|
250
....*....|
gi 1906086718 560 LS---LKGAY 566
Cdd:COG0410 224 LAdpeVREAY 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-561 |
2.34e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.37 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 351 ADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGY-----IAIDGVKLPKWKES-SLRSAMSVVSQRVD 424
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVlEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 425 ILNGSLRDNLL--LADDTASDEKLIKTLNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPT 502
Cdd:PRK14271 112 PFPMSIMDNVLagVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 503 EGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
339-531 |
2.45e-16 |
|
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: 75.95 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIaidgvklpkwkesslrsamsv 418
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 vsqrvdilngslrdnllladdtasdeKLIKTLNQVGLEalttdeglnawlgdggrQLSGGERRRIGIARALLHDAPIVLL 498
Cdd:cd03221 58 --------------------------TWGSTVKIGYFE-----------------QLSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|...
gi 1906086718 499 DEPTEGLDQKTEQQIMSVLNKHieHKTVVFITH 531
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-561 |
2.72e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.94 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 346 YQYMDaDTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKES------SLRSAMSVV 419
Cdd:PRK14246 17 YLYIN-DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfqidaiKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 420 SQRVDIL-NGSLRDNLL--LADDTASDEKLIKTLNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIV 496
Cdd:PRK14246 96 FQQPNPFpHLSIYDNIAypLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 497 LLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFT 241
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
10-500 |
2.81e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 81.77 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 10 LYKKHWFGLTLGMLLSFATLFASIGLLtisgWFISASAIAGLTIARETFnyMLPAGAVRGFSIGRTAGRWGERVVSHNAT 89
Cdd:COG4615 7 LLRESRWLLLLALLLGLLSGLANAGLI----ALINQALNATGAALARLL--LLFAGLLVLLLLSRLASQLLLTRLGQHAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 90 FKLltelRIFFFKKLI--PLIpgRFSKLRDADLLNRLVADVDAMDHVYLRLvSPIIVGTLGIIGLTAFLAWFDITI-GLT 166
Cdd:COG4615 81 ARL----RLRLSRRILaaPLE--RLERIGAARLLAALTEDVRTISQAFVRL-PELLQSVALVLGCLAYLAWLSPPLfLLT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 167 LGAILLSLLLIWpTLFYKLGKH-NGSELTQNKATLRIKTLdwLQGNAELRIfgaEAQYRQRILD---AQTALLANQHRMA 242
Cdd:COG4615 154 LVLLGLGVAGYR-LLVRRARRHlRRAREAEDRLFKHFRAL--LEGFKELKL---NRRRRRAFFDedlQPTAERYRDLRIR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 243 ALTGLANGLLLLANGWTLL--LMLWIAgdgiAGMTPDPMVAMVAFATMASFeLLMPIAGAFQYLgQTLSSA----RRLNE 316
Cdd:COG4615 228 ADTIFALANNWGNLLFFALigLILFLL----PALGWADPAVLSGFVLVLLF-LRGPLSQLVGAL-PTLSRAnvalRKIEE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 317 IiTAEPDTVFDENGVDQAIKGN-----LTISNVDYQYMDADTN---AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTR 388
Cdd:COG4615 302 L-ELALAAAEPAAADAAAPPAPadfqtLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 389 QWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQrvdilNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTTDEglnawl 468
Cdd:COG4615 381 LYRPESGEILLDGQPVTADNREAYRQLFSAVFS-----DFHLFDRLLGLDGEADPARARELLERLELDHKVSVE------ 449
|
490 500 510
....*....|....*....|....*....|....*
gi 1906086718 469 gDGG---RQLSGGERRRIGIARALLHDAPIVLLDE 500
Cdd:COG4615 450 -DGRfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
339-555 |
4.65e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.74 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDAdTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKES--SLRSAM 416
Cdd:PRK13636 6 LKVEELNYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRVD--ILNGSLRD-------NLLLADDTASdEKLIKTLNQVGLEALtTDEGLNAwlgdggrqLSGGERRRIGIAR 487
Cdd:PRK13636 85 GMVFQDPDnqLFSASVYQdvsfgavNLKLPEDEVR-KRVDNALKRTGIEHL-KDKPTHC--------LSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 488 ALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHK--TVVFITHRL--VNLeQMDHICLMDHGEIVEQGT 555
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIdiVPL-YCDNVFVMKEGRVILQGN 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
339-561 |
5.80e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.90 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISN--VDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKS-TLLQLLTRQWDPK----SGYIAIDGVKLPKWKESS 411
Cdd:PRK15134 6 LAIENlsVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 412 LRS------AMSVVSQRVDI-----LNGSLRDNLLL----ADDTASDEkLIKTLNQVGLEALTTDeglnawLGDGGRQLS 476
Cdd:PRK15134 86 LRGvrgnkiAMIFQEPMVSLnplhtLEKQLYEVLSLhrgmRREAARGE-ILNCLDRVGIRQAAKR------LTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 477 GGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLN--KHIEHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQ 553
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQ 238
|
....*...
gi 1906086718 554 GTHDSLLS 561
Cdd:PRK15134 239 NRAATLFS 246
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-573 |
6.09e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 77.65 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTR--QWDPK---SGYIAIDGVKLPKWKESSLR 413
Cdd:PRK14247 4 IEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEarvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 414 SAMSVVSQRVD-ILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALttdEGLNAW------LGDGGRQLSGGERRRIGIA 486
Cdd:PRK14247 82 RRVQMVFQIPNpIPNLSIFENVALGLKLNRLVKSKKELQERVRWAL---EKAQLWdevkdrLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 487 RALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQG-THDSLLSLKg 564
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGpTREVFTNPR- 237
|
....*....
gi 1906086718 565 ayHQLWQRF 573
Cdd:PRK14247 238 --HELTEKY 244
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
360-561 |
7.29e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.93 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 360 SLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGV--------KLPK---WKESSLRSAMSVvSQRVDI-LN 427
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsRRPVsmlFQENNLFSHLTV-AQNIGLgLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 428 GSLRDNllladdTASDEKLIKTLNQVGLEALTtdEGLNAwlgdggrQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQ 507
Cdd:PRK10771 98 PGLKLN------AAQREKLHAIARQMGIEDLL--ARLPG-------QLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 508 KTEQQIMSVLNK--HIEHKTVVFITHrlvNLEQMDHIC----LMDHGEIVEQGTHDSLLS 561
Cdd:PRK10771 163 ALRQEMLTLVSQvcQERQLTLLMVSH---SLEDAARIAprslVVADGRIAWDGPTDELLS 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
349-554 |
7.47e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.43 E-value: 7.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 349 MDADTNAINAISLDLLSGQKMAIVGQTGSGKS----TLLQLL---TRQwdpKSGYIAIDGVKLpkwKESSLRSAM-SVVS 420
Cdd:PRK10418 12 LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpagVRQ---TAGRVLLDGKPV---APCALRGRKiATIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 421 QR-------VDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTTDEGLNAWlgdggrQLSGGERRRIGIARALLHDA 493
Cdd:PRK10418 86 QNprsafnpLHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPF------EMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 494 PIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKT--VVFITHRL-VNLEQMDHICLMDHGEIVEQG 554
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMgVVARLADDVAVMSHGRIVEQG 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
339-550 |
8.43e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.41 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYI---------AIDGVKLpKWKE 409
Cdd:PRK11247 13 LLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplaeAREDTRL-MFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 410 SSLRSAMSVVSQRVDILNGSLRDNLLLAddtasdekliktLNQVGLEALTTDeglnaWLGdggrQLSGGERRRIGIARAL 489
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLKGQWRDAALQA------------LAAVGLADRANE-----WPA----ALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 490 LHDAPIVLLDEPTEGLDQKT----EQQIMSVLNKHieHKTVVFITHRLVNLEQM-DHICLMDHGEI 550
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTriemQDLIESLWQQH--GFTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
356-560 |
8.45e-16 |
|
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: 76.81 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGV---KLPKWKESslRSAMSVVSQRVDILNG-SLR 431
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditKLPMHKRA--RLGIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 432 DNLLLADDTASDEKLIKTLNqvgLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQ 511
Cdd:cd03218 94 ENILAVLEIRGLSKKEREEK---LEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 512 QIMSVLNKHIEHKTVVFITHRLVN--LEQMDHICLMDHGEIVEQGTHDSLL 560
Cdd:cd03218 171 DIQKIIKILKDRGIGVLITDHNVRetLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
339-554 |
1.14e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.12 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWD--PK---SGYIAIDGVKL--PKWKESS 411
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 412 LRSAMSVVSQRVDILNGSLRDNLL-------LADDTASDEKLIKTLNQVGLEALTTDEglnawLGDGGRQLSGGERRRIG 484
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVyglrlkgIKDKQVLDEAVEKSLKGASIWDEVKDR-----LHDSALGLSGGQQQRVC 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 485 IARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHrlvNLEQMDHIC----LMDHGEIVEQG 554
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRISdrtgFFLDGDLIEYN 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
358-530 |
1.25e-15 |
|
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: 75.47 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 358 AISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSaMSVVSQRvDILNGSL--RDNL- 434
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN-ILYLGHL-PGLKPELsaLENLh 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 435 LLADDTASDEKLIKT-LNQVGLEALttdEGLNAwlgdggRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQI 513
Cdd:TIGR01189 96 FWAAIHGGAQRTIEDaLAAVGLTGF---EDLPA------AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170
....*....|....*..
gi 1906086718 514 MSVLNKHIEHKTVVFIT 530
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLT 183
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
355-543 |
1.49e-15 |
|
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: 75.93 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYI-------AIDGVKLPKWKESSLR-SAMSVVSQ----- 421
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggWVDLAQASPREILALRrRTIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 422 -RV---DILNGSLRDnLLLADDTASDEKliKTLnqvgLEALTTDEGLnaWlgdggrQL-----SGGERRRIGIARALLHD 492
Cdd:COG4778 106 pRVsalDVVAEPLLE-RGVDREEARARA--REL----LARLNLPERL--W------DLppatfSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 493 APIVLLDEPTEGLDQKTEQQIMSVLNkhiEHK----TVVFITHrlvNLEQMDHIC 543
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIE---EAKargtAIIGIFH---DEEVREAVA 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
352-555 |
1.88e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.07 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 352 DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGV---KLPKWKesslRSAMSVVSQRVDILNG 428
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQditHVPAEN----RHVNTVFQSYALFPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 429 SLRDNL---LLADDTASDEklIKT-----LNQVGLEALttdeglnawlgdGGR---QLSGGERRRIGIARALLHDAPIVL 497
Cdd:PRK09452 102 TVFENVafgLRMQKTPAAE--ITPrvmeaLRMVQLEEF------------AQRkphQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 498 LDEPTEGLDQKTEQQIMSVLnKHIEHK---TVVFITH-RLVNLEQMDHICLMDHGEIVEQGT 555
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNEL-KALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
346-573 |
2.94e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.00 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 346 YQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSL----RSAMSVVSQ 421
Cdd:PRK10535 14 YPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 422 RVDILNG-SLRDNLLLADDTASDEKlikTLNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDE 500
Cdd:PRK10535 94 RYHLLSHlTAAQNVEVPAVYAGLER---KQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 501 PTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQMDHICLMDHGEIV----------EQGTHDSLLSLKGAYHQL 569
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIVrnppaqekvnVAGGTEPVVNTASGWRQF 250
|
....
gi 1906086718 570 WQRF 573
Cdd:PRK10535 251 VSGF 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
355-554 |
4.32e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKES-SLRSAMSVVSQRVDILNG-SLRD 432
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDElTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 433 NLLLADDTAS--------DEKLIKTLNQVGLEALTTDEGLNAWLGDggrqLSGGERRRIGIARALLHDAPIVLLDEPTEG 504
Cdd:PRK09700 100 NLYIGRHLTKkvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 505 LDQKTEQQIMSVLNK-HIEHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:PRK09700 176 LTNKEVDYLFLIMNQlRKEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSG 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
359-560 |
6.58e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.96 E-value: 6.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSG---YIAIDGVKLPKWKESS------LRSAMSVVSQ------RV 423
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGevhYRMRDGQLRDLYALSEaerrrlLRTEWGFVHQhprdglRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 424 DILNGSLRDNLLLA---------DDTASDeklikTLNQVGLEALTTDeglnawlgDGGRQLSGGERRRIGIARALLHDAP 494
Cdd:PRK11701 105 QVSAGGNIGERLMAvgarhygdiRATAGD-----WLERVEIDAARID--------DLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 495 IVLLDEPTEGLDQKTEQQIMSVLNKHIE--HKTVVFITH-----RLVNleqmDHICLMDHGEIVEQGTHDSLL 560
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHdlavaRLLA----HRLLVMKQGRVVESGLTDQVL 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
339-566 |
8.58e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.42 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSV 418
Cdd:PRK09536 4 IDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDI-LNGSLR--------------DNLLLADDTASDEklikTLNQVGLEALTtDEGLNAwlgdggrqLSGGERRRI 483
Cdd:PRK09536 82 VPQDTSLsFEFDVRqvvemgrtphrsrfDTWTETDRAAVER----AMERTGVAQFA-DRPVTS--------LSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 484 GIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLvNLEQM--DHICLMDHGEIVEQGTHDSLL 560
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDL-DLAARycDELVLLADGRVRAAGPPADVL 227
|
....*....
gi 1906086718 561 S---LKGAY 566
Cdd:PRK09536 228 TadtLRAAF 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
359-559 |
9.21e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.80 E-value: 9.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSL---RSAMSVVSQrvdilNGSLRDNLL 435
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQ-----SGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 436 LADD--------TASDEKLIKTLNQVGLEALttdeGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQ 507
Cdd:PRK11831 101 VFDNvayplrehTQLPAPLLHSTVMMKLEAV----GLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 508 KTeqqiMSVLNKHIEH------KTVVFITHRLVN-LEQMDHICLMDHGEIVEQGTHDSL 559
Cdd:PRK11831 177 IT----MGVLVKLISElnsalgVTCVVVSHDVPEvLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
355-561 |
1.41e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwKESSLRSAMSVVSQRVDILNGSLR--- 431
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG------QEMRFASTTAALAAGVAIIYQELHlvp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 432 -----DNLLLADDTAS----DEKLIKTLNQVGLEALTTDEGLNAWLGDggrqLSGGERRRIGIARALLHDAPIVLLDEPT 502
Cdd:PRK11288 93 emtvaENLYLGQLPHKggivNRRLLNYEAREQLEHLGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 503 EGLDQKTEQQIMSVLNK-HIEHKTVVFITHRlvnLEQMDHIC----------LMDHGEIVEQGTHDSLLS 561
Cdd:PRK11288 169 SSLSAREIEQLFRVIRElRAEGRVILYVSHR---MEEIFALCdaitvfkdgrYVATFDDMAQVDRDQLVQ 235
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-554 |
1.74e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTnaINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKES--SLRSAM 416
Cdd:PRK13638 2 LATSDLWFRYQDEPV--LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVSQRvdilngslRDNLLLADDTASDekLIKTLNQVGLE----ALTTDEGLNAWLGDGGRQ-----LSGGERRRIGIAR 487
Cdd:PRK13638 80 ATVFQD--------PEQQIFYTDIDSD--IAFSLRNLGVPeaeiTRRVDEALTLVDAQHFRHqpiqcLSHGQKKRVAIAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 488 ALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNL--EQMDHICLMDHGEIVEQG 554
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLiyEISDAVYVLRQGQILTHG 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
339-541 |
2.14e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.90 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTnaINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKwKESSLRSAMSV 418
Cdd:PRK13540 2 LDVIELDFDYHDQPL--LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDI-LNGSLRDNLLLADDTASdekliktlNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVL 497
Cdd:PRK13540 79 VGHRSGInPYLTLRENCLYDIHFSP--------GAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1906086718 498 LDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFIT-HRLVNLEQMDH 541
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTsHQDLPLNKADY 195
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
359-550 |
2.30e-14 |
|
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: 71.31 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSA-MSVVSQ-RVD---ILNGSLRDN 433
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEdRKReglVLDLSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 434 LLLaddtasdekliktlnqvglealttdeglnawlgdgGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQI 513
Cdd:cd03215 99 IAL-----------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906086718 514 MSVLNKHIEH-KTVVFITHRLVNLEQM-DHICLMDHGEI 550
Cdd:cd03215 144 YRLIRELADAgKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
351-548 |
3.52e-14 |
|
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: 71.98 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 351 ADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGV--KLPKWKESSLRSAMSV--VSQRVDIL 426
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKneSEPSFEATRSRNRYSVayAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 427 NGSLRDNLLLADDTASDE-KLIKTLNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGL 505
Cdd:cd03290 92 NATVEENITFGSPFNKQRyKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1906086718 506 -----DQKTEQQIMSVLNKhiEHKTVVFITHRLVNLEQMDHICLMDHG 548
Cdd:cd03290 172 dihlsDHLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
339-562 |
3.79e-14 |
|
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: 75.22 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDAD---TNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIA-------IDGVKLPKWK 408
Cdd:TIGR03269 280 IKVRNVSKRYISVDrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 409 ESSLRSAMSVVSQRVDIL-NGSLRDNLLLA-----DDTASDEKLIKTLNQVGLEALTTDEGLNAWlgdgGRQLSGGERRR 482
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYpHRTVLDNLTEAiglelPDELARMKAVITLKMVGFDEEKAEEILDKY----PDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 483 IGIARALLHDAPIVLLDEPTEGLDQKTEQQIM-SVLNKHIE-HKTVVFITHRL-VNLEQMDHICLMDHGEIVEQGTHDSL 559
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEmEQTFIIVSHDMdFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
...
gi 1906086718 560 LSL 562
Cdd:TIGR03269 516 VEE 518
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
339-552 |
3.79e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIdGVKLpkwkesslrsAMSV 418
Cdd:COG0488 316 LELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVDILNG--SLRDNLLLADDTASDEKLIktlnqvglealttdeglnAWLGD----GGRQ------LSGGERRRIGIA 486
Cdd:COG0488 383 FDQHQEELDPdkTVLDELRDGAPGGTEQEVR------------------GYLGRflfsGDDAfkpvgvLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 487 RALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNkhiEHK-TVVFITH------RLVnleqmDHICLMDHGEIVE 552
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALD---DFPgTVLLVSHdryfldRVA-----TRILEFEDGGVRE 509
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
339-561 |
5.38e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.46 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTN-AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMS 417
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 418 VVSQRVD--ILNGSLRDNLLLA------DDTASDEKLIKTLNQVGLEALTTDEglnawlgdgGRQLSGGERRRIGIARAL 489
Cdd:PRK13650 85 MVFQNPDnqFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKERE---------PARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 490 LHDAPIVLLDEPTEGLDQKTEQQIMSVLnKHIEHK---TVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTI-KGIRDDyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
359-560 |
6.39e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRDNLL--- 435
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVaig 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 436 -------LADDTASD-EKLIKTLNQVGLEALTTDeglnawLGDggrQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQ 507
Cdd:PRK10575 110 rypwhgaLGRFGAADrEKVEEAISLVGLKPLAHR------LVD---SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 508 KTEQQIMSVLNKHIEHK--TVVFITHRL-VNLEQMDHICLMDHGEIVEQGTHDSLL 560
Cdd:PRK10575 181 AHQVDVLALVHRLSQERglTVIAVLHDInMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
354-561 |
7.24e-14 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 71.54 E-value: 7.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 354 NAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDG---VKLPKWKESslRSAMSVVSQRVDILNG-S 429
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGqdiTHLPMHERA--RLGIGYLPQEASIFRKlT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 430 LRDNLLLADDTAsdEKLIKTLNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKT 509
Cdd:TIGR04406 93 VEENIMAVLEIR--KDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 510 EQQIMSVLnKHIEHKTV-VFITHRLV--NLEQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:TIGR04406 171 VGDIKKII-KHLKERGIgVLITDHNVreTLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
352-554 |
9.60e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.12 E-value: 9.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 352 DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVK---LPKWKESSLRSAMSVVSQ----RVD 424
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidtLSPGKLQALRRDIQFIFQdpyaSLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 425 ---ILNGSLRDNLL---LADDTASDEKLIKTLNQVGLEAlttdegLNAWLGDggRQLSGGERRRIGIARALLHDAPIVLL 498
Cdd:PRK10261 416 prqTVGDSIMEPLRvhgLLPGKAAAARVAWLLERVGLLP------EHAWRYP--HEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 499 DEPTEGLDQKTEQQIMSVLNKHIEHKTV--VFITHRLVNLEQMDH-ICLMDHGEIVEQG 554
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHrVAVMYLGQIVEIG 546
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
359-522 |
1.24e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPkwkESSLRSAMSVVSQRvDILNGSL--RDNLLL 436
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYLGHR-NAMKPALtvAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 437 ADDT--ASDEKLIKTLNQVGLEALTTdegLNAwlgdggRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIM 514
Cdd:PRK13539 97 WAAFlgGEELDIAAALEAVGLAPLAH---LPF------GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
....*...
gi 1906086718 515 SVLNKHIE 522
Cdd:PRK13539 168 ELIRAHLA 175
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
352-561 |
1.65e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.91 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 352 DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLL--TRQWDPKSG-------------YIAI---DGVKLPKWKESslr 413
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGriiyhvalcekcgYVERpskVGEPCPVCGGT--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 414 samsVVSQRVDILNGS--LRDNL-------------LLADDTASDeKLIKTLNQVGLEA---------LTTDEGLNAWLG 469
Cdd:TIGR03269 89 ----LEPEEVDFWNLSdkLRRRIrkriaimlqrtfaLYGDDTVLD-NVLEALEEIGYEGkeavgravdLIEMVQLSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 470 DGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHK--TVVFITHRLVNLEQM-DHICLMD 546
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDLsDKAIWLE 243
|
250
....*....|....*
gi 1906086718 547 HGEIVEQGTHDSLLS 561
Cdd:TIGR03269 244 NGEIKEEGTPDEVVA 258
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
358-536 |
2.04e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 358 AISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIaidgvklpKWKESSLRsamsvvSQRVDI---------LNG 428
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV--------LWQGEPIR------RQRDEYhqdllylghQPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 429 ---------SLRDNLLLADDtASDEKLIKTLNQVGLEALttdEGLNAwlgdggRQLSGGERRRIGIARALLHDAPIVLLD 499
Cdd:PRK13538 85 ikteltaleNLRFYQRLHGP-GDDEALWEALAQVGLAGF---EDVPV------RQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1906086718 500 EPTEGLDQKTEQQIMSVLNKHIEHK-TVVFITHRLVNL 536
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQGgMVILTTHQDLPV 192
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
355-533 |
2.42e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.36 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKwkeSSLRSAM----SVVSQRVDILNG-S 429
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF---RSPRDAQaagiAIIHQELNLVPNlS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 430 LRDNLLLA---------DDTASDEKLIKTLNQVGLealttDEGLNAWLGDggrqLSGGERRRIGIARALLHDAPIVLLDE 500
Cdd:COG1129 96 VAENIFLGreprrggliDWRAMRRRARELLARLGL-----DIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1906086718 501 PTEGLDQK-TEQ--QIMSVLNKhiEHKTVVFITHRL 533
Cdd:COG1129 167 PTASLTEReVERlfRIIRRLKA--QGVAIIYISHRL 200
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-569 |
2.84e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 354 NAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvKLPkWK-ESSLRSAMSVVS-QRV----DIln 427
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-YVP-FKrRKEFARRIGVVFgQRSqlwwDL-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 428 gSLRDNL-LLAD----DTASDEKLIKTLNQV-GLEALttdeglnawLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEP 501
Cdd:COG4586 112 -PAIDSFrLLKAiyriPDAEYKKRLDELVELlDLGEL---------LDTPVRQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 502 TEGLDQKTEQQIMSVL---NKhiEHKTVVFIT-HRLVNLEQM-DHICLMDHGEIVEQGTHDSLLSLKGAYHQL 569
Cdd:COG4586 182 TIGLDVVSKEAIREFLkeyNR--ERGTTILLTsHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERFGPYKTI 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
354-554 |
3.82e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.02 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 354 NAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKL---PKWKES--------SLRSAMSVvsqR 422
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvPPYQRPinmmfqsyALFPHMTV---E 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 423 VDILNGSLRDNLLLADDTASDEKLIKTLNqvglealttdegLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPT 502
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEIASRVNEMLGLVH------------MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 503 EGLDQKTEQQIMSVLNKHIEH--KTVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMaGRIAIMNRGKFVQIG 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
355-538 |
3.86e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.81 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWD-----PKSGYIAIDGVKL--PKWKESSLRSAMSVVSQRVDILN 427
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 428 GSLRDNL-----LLADDTASDEKLIKTLNQVGLEALTTDEglnawLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPT 502
Cdd:PRK14243 105 KSIYDNIaygarINGYKGDMDELVERSLRQAALWDEVKDK-----LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1906086718 503 EGLDQKTEQQIMSVLNKHIEHKTVVFITHrlvNLEQ 538
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQYTIIIVTH---NMQQ 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
355-514 |
4.55e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.75 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESS---LRSAMSVVSQRVDIL-NGSL 430
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLmDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 431 RDN----LLLADDTASD--EKLIKTLNQVGLealtTDEGLNAWLgdggrQLSGGERRRIGIARALLHDAPIVLLDEPTEG 504
Cdd:PRK10908 97 YDNvaipLIIAGASGDDirRRVSAALDKVGL----LDKAKNFPI-----QLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170
....*....|
gi 1906086718 505 LDQKTEQQIM 514
Cdd:PRK10908 168 LDDALSEGIL 177
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
362-531 |
5.00e-13 |
|
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: 68.97 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 362 DLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLP-KWKESSLRSAMSVVSQRVDILNGSLRDNLLLADdt 440
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQYIKADYEGTVRDLLSSITKDFYTHPYFKTE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 441 asdeklikTLNQVGLEALtTDEGLNawlgdggrQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDqkTEQQIM--SVLN 518
Cdd:cd03237 99 --------IAKPLQIEQI-LDREVP--------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMasKVIR 159
|
170
....*....|....*
gi 1906086718 519 KHIEH--KTVVFITH 531
Cdd:cd03237 160 RFAENneKTAFVVEH 174
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-561 |
7.13e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.91 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdaDTNAI-NAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQwDPKSGYIAIDGvKLPKWKES------- 410
Cdd:PRK14258 8 IKVNNLSFYY---DTQKIlEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEG-RVEFFNQNiyerrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 411 --SLRSAMSVVSQRVDILNGSLRDNLlladdtASDEKLIKTLNQVGLEALTTDEGLNAWLGD--------GGRQLSGGER 480
Cdd:PRK14258 83 lnRLRRQVSMVHPKPNLFPMSVYDNV------AYGVKIVGWRPKLEIDDIVESALKDADLWDeikhkihkSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 481 RRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHI--EHKTVVFITHRLVNLEQMDHICLMDHG------EIVE 552
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVE 236
|
....*....
gi 1906086718 553 QGTHDSLLS 561
Cdd:PRK14258 237 FGLTKKIFN 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
356-531 |
9.17e-13 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 67.88 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLrsamsVVSQRVDILNG-SLRDNL 434
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 435 LLADDTAsdeklIKTLNQVGLEALTTDE----GLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKT- 509
Cdd:TIGR01184 76 ALAVDRV-----LPDLSKSERRAIVEEHialvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTr 150
|
170 180
....*....|....*....|....*
gi 1906086718 510 ---EQQIMSVLNKHieHKTVVFITH 531
Cdd:TIGR01184 151 gnlQEELMQIWEEH--RVTVLMVTH 173
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
359-531 |
1.97e-12 |
|
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: 69.58 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLL-----------TRQWDPKSGYIAIDgvklPKWKESS--LRSAMSVVSQRVDI 425
Cdd:TIGR03719 24 ISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfngeaRPQPGIKVGYLPQE----PQLDPTKtvRENVEEGVAEIKDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 426 LNGSLRDNLLLADDTASDEKLIKTlnQVGLEALTtdEGLNAWlgDGGRQ-------------------LSGGERRRIGIA 486
Cdd:TIGR03719 100 LDRFNEISAKYAEPDADFDKLAAE--QAELQEII--DAADAW--DLDSQleiamdalrcppwdadvtkLSGGERRRVALC 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1906086718 487 RALLHDAPIVLLDEPTEGLDQKTeqqiMSVLNKHIEH--KTVVFITH 531
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEypGTVVAVTH 216
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
339-566 |
2.13e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESS-LRSAMS 417
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 418 VVSQ-RVDILNGSLRDNLLLADDTASDEKLIKTLNQVglealttdEGLNAWLGDGGRQ----LSGGERRRIGIARALLHD 492
Cdd:PRK11614 84 IVPEgRRVFSRMTVEENLAMGGFFAERDQFQERIKWV--------YELFPRLHERRIQragtMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 493 APIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVN--LEQMDHICLMDHGEIVEQGTHDSLLS---LKGAY 566
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqaLKLADRGYVLENGHVVLEDTGDALLAneaVRSAY 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
358-554 |
2.25e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 358 AISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDIlNGSLRDNLLLA 437
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT-PGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 438 DDTASDEKLIKTLNQVGLEALTT---DEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLD---QKTEQ 511
Cdd:PRK10253 104 RGRYPHQPLFTRWRKEDEEAVTKamqATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDishQIDLL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1906086718 512 QIMSVLNKHiEHKTVVFITHRLVN-LEQMDHICLMDHGEIVEQG 554
Cdd:PRK10253 184 ELLSELNRE-KGYTLAAVLHDLNQaCRYASHLIALREGKIVAQG 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
356-532 |
2.39e-12 |
|
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: 69.78 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwkesslRSAMSVVSQRVDILNGSLRDNLL 435
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 436 LADDTA-------SDEKLIKTLNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQK 508
Cdd:TIGR00954 537 YPDSSEdmkrrglSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
170 180
....*....|....*....|....*
gi 1906086718 509 TEQQIMSVL-NKHIehkTVVFITHR 532
Cdd:TIGR00954 617 VEGYMYRLCrEFGI---TLFSVSHR 638
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
365-545 |
2.52e-12 |
|
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: 67.01 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 365 SGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYI-----------AIDGVKLPKWKESSLRSAMSVV--SQRVDIL----N 427
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLLEGDVKVIvkPQYVDLIpkavK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 428 GSLRDNLLLADDTASDEKLIKTLnqvglealttdeGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQ 507
Cdd:cd03236 105 GKVGELLKKKDERGKLDELVDQL------------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1906086718 508 KTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQM-DHICLM 545
Cdd:cd03236 173 KQRLNAARLIRELAEDdNYVLVVEHDLAVLDYLsDYIHCL 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
339-555 |
3.79e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMD--ADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDG----------VKLPK 406
Cdd:PRK10261 13 LAVENLNIAFMQeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 407 WKESSLRSA----MSVVSQR-------VDILNGSLRDNLLLADDTASDEKLI---KTLNQVGL-EAlttdeglNAWLGDG 471
Cdd:PRK10261 93 QSAAQMRHVrgadMAMIFQEpmtslnpVFTVGEQIAESIRLHQGASREEAMVeakRMLDQVRIpEA-------QTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 472 GRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIM---SVLNKHIEhKTVVFITHRL-VNLEQMDHICLMDH 547
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILqliKVLQKEMS-MGVIFITHDMgVVAEIADRVLVMYQ 244
|
....*...
gi 1906086718 548 GEIVEQGT 555
Cdd:PRK10261 245 GEAVETGS 252
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
346-554 |
4.16e-12 |
|
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: 64.65 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 346 YQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQlltrqwdpksgyiaidgvklpkwkesslrsamsvvsqrvDI 425
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------------------------------EG 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 426 LNGSLRDNLLLADDTASDEKLI-----KTLNQVGLEALTTDEGLNAwlgdggrqLSGGERRRIGIARAL-LHDAPIV-LL 498
Cdd:cd03238 42 LYASGKARLISFLPKFSRNKLIfidqlQFLIDVGLGYLTLGQKLST--------LSGGELQRVKLASELfSEPPGTLfIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 499 DEPTEGLDQKTEQQIMSVLNKHIEHK-TVVFITHRLVNLEQMDHICLMDH------GEIVEQG 554
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGnTVILIEHNLDVLSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
343-555 |
5.43e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 343 NVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKS----TLLQLLTRQwDPKSGYIAIDG---VKLPKWKESSLRS- 414
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAAN-GRIGGSATFNGreiLNLPEKELNKLRAe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 415 AMSVVSQR-VDILNGSLR--DNLL--------LADDTASDEKlIKTLNQVGL-EALTTdeglnawLGDGGRQLSGGERRR 482
Cdd:PRK09473 98 QISMIFQDpMTSLNPYMRvgEQLMevlmlhkgMSKAEAFEES-VRMLDAVKMpEARKR-------MKMYPHEFSGGMRQR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 483 IGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLN--KHIEHKTVVFITHRL-VNLEQMDHICLMDHGEIVEQGT 555
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDLgVVAGICDKVLVMYAGRTMEYGN 245
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
339-558 |
6.30e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.44 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTnAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLrSAMSV 418
Cdd:PRK15056 7 IVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 VSQRVD----------ILNGSLRDNLLLADDTASDEKLIKTlnqvGLEALTTDEGLNAWLGdggrQLSGGERRRIGIARA 488
Cdd:PRK15056 85 QSEEVDwsfpvlvedvVMMGRYGHMGWLRRAKKRDRQIVTA----ALARVDMVEFRHRQIG----ELSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 489 LLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRLVNLEQMDHICLMDHGEIVEQGTHDS 558
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTET 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-557 |
6.52e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.78 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVK---LPkwkeSSLRSAMSVVS--QRVDILNG- 428
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLP----GHQIARMGVVRtfQHVRLFREm 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 429 SLRDNLLLADDTASDEK----LIKT-----------------LNQVGLEALTTDEGLNawlgdggrqLSGGERRRIGIAR 487
Cdd:PRK11300 96 TVIENLLVAQHQQLKTGlfsgLLKTpafrraesealdraatwLERVGLLEHANRQAGN---------LAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 488 ALLHDAPIVLLDEPTEGLD-QKTE--QQIMSVLNKhiEHK-TVVFITH--RLVnLEQMDHICLMDHGEIVEQGTHD 557
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNpKETKelDELIAELRN--EHNvTVLLIEHdmKLV-MGISDRIYVVNQGTPLANGTPE 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
358-559 |
1.60e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 358 AISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRS-AMSVVSQRVDIL-NGSLRDNLL 435
Cdd:PRK15439 29 GIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFpNLSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 436 L-----ADDTASDEKLIKTLN-QVGLEALTTdeglnawlgdggrQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQ-K 508
Cdd:PRK15439 109 FglpkrQASMQKMKQLLAALGcQLDLDSSAG-------------SLEVADRQIVEILRGLMRDSRILILDEPTASLTPaE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 509 TE---QQIMSVLNKHIehkTVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSL 559
Cdd:PRK15439 176 TErlfSRIRELLAQGV---GIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
355-559 |
1.66e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.88 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPK-----WKE-------------SSLRSAM 416
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddeWRAvrsdiqmifqdplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SVVsqrvDILNGSLRDNLLLADDTASDEKLIKTLNQVGLealttdegLNAWLGDGGRQLSGGERRRIGIARALLHDAPIV 496
Cdd:PRK15079 116 TIG----EIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGL--------LPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 497 LLDEPTEGLDQKTEQQIMSVLnKHIEHK---TVVFITHRLVNLEQM-DHICLMDHGEIVEQGTHDSL 559
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLL-QQLQREmglSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
338-554 |
1.73e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.82 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 338 NLTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKwKESSLRSaMS 417
Cdd:PRK11000 3 SVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND-VPPAERG-VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 418 VVSQRVdilngSLRDNLLLADDTASDEKLIKT--------LNQVGlEALTTDEGLNawlgdggRQ---LSGGERRRIGIA 486
Cdd:PRK11000 79 MVFQSY-----ALYPHLSVAENMSFGLKLAGAkkeeinqrVNQVA-EVLQLAHLLD-------RKpkaLSGGQRQRVAIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 487 RALLHDAPIVLLDEPTEGLDQKTEQQI---MSVLNKHIEhKTVVFITHRLVnlEQM---DHICLMDHGEIVEQG 554
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAALRVQMrieISRLHKRLG-RTMIYVTHDQV--EAMtlaDKIVVLDAGRVAQVG 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
354-531 |
2.79e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.64 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 354 NAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSlRSAMSvvSQRVDILNGSLrdn 433
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA-RAKLR--AKHVGFVFQSF--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 434 llladdtasdeKLIKTLN---QVGLEALTTDEG----------LNAWLGDGGR------QLSGGERRRIGIARALLHDAP 494
Cdd:PRK10584 98 -----------MLIPTLNaleNVELPALLRGESsrqsrngakaLLEQLGLGKRldhlpaQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1906086718 495 IVLLDEPTEGLDQKTEQQIMSVL---NKhiEH-KTVVFITH 531
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLfslNR--EHgTTLILVTH 205
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
358-561 |
3.13e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 63.71 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 358 AISLDLLSGQKMAIVGQTGSGKSTLLQ----LLtrqwdPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGS---- 429
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLArmagLL-----PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMpvfq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 430 -LRdnlLLADDTASDEKLIKTLNQVgLEALttdeGLNAWLGDGGRQLSGGERRRIGIARALLH-------DAPIVLLDEP 501
Cdd:COG4138 89 yLA---LHQPAGASSEAVEQLLAQL-AEAL----GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 502 TEGLDqkTEQQimSVLNKHIEH-----KTVVFITHRLvN--LEQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:COG4138 161 MNSLD--VAQQ--AALDRLLRElcqqgITVVMSSHDL-NhtLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
355-541 |
3.20e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.88 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQ----LLTRQWDPKS-----GYIAIDGVKLPKWKESSlRSAMSVVSQRVDI 425
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellGRTVQREGRLARDIRKS-RANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 426 LNG-SLRDNLLLADDTASD------EKLIKTLNQVGLEALTTdEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLL 498
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTR-VGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1906086718 499 DEPTEGLDQKTEQQIMSVLNKHIEHKTVVFIthrlVNLEQMDH 541
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDGITVV----VTLHQVDY 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
333-552 |
3.58e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.76 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 333 QAIKGNLTIS--NVDYQYMDaDTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKES 410
Cdd:PRK10522 315 QAFPDWQTLElrNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 411 SLRSAMSVVSQRVdilngSLRDNLLLADDTASDEKLIKT-LNQVGLEALTTDEglnawlgdGGR----QLSGGERRRIGI 485
Cdd:PRK10522 394 DYRKLFSAVFTDF-----HLFDQLLGPEGKPANPALVEKwLERLKMAHKLELE--------DGRisnlKLSKGQKKRLAL 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 486 ARALLHDAPIVLLDEptEGLDQKTE------QQIMSVLnkHIEHKTVVFITHRLVNLEQMDHICLMDHGEIVE 552
Cdd:PRK10522 461 LLALAEERDILLLDE--WAADQDPHfrrefyQVLLPLL--QEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
355-533 |
3.74e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwKESSLRS---------AMsvVSQR--- 422
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG------KPVRIRSprdaialgiGM--VHQHfml 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 423 VDILngSLRDNLLLADDTASDEKL-IKTLNQVgLEALTTDEGL----NAWLGDggrqLSGGERRRIGIARALLHDAPIVL 497
Cdd:COG3845 92 VPNL--TVAENIVLGLEPTKGGRLdRKAARAR-IRELSERYGLdvdpDAKVED----LSVGEQQRVEILKALYRGARILI 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906086718 498 LDEPTEGL-DQKTEQ--QIMSVLNKhiEHKTVVFITHRL 533
Cdd:COG3845 165 LDEPTAVLtPQEADElfEILRRLAA--EGKSIIFITHKL 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
355-554 |
2.43e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 60.62 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwKESSLrsamsvvsqrVDI---LNGSL- 430
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSL----------LGLgggFNPELt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 431 -RDNLLL------ADDTASDEKL--IKTLNQVGlEALttDEGLnawlgdggRQLSGGERRRIGIARALLHDAPIVLLDEP 501
Cdd:cd03220 101 gRENIYLngrllgLSRKEIDEKIdeIIEFSELG-DFI--DLPV--------KTYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 502 TEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
351-554 |
3.14e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 60.74 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 351 ADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRqwDPK----SGYIAIDGVKLPKWK-ESSLRSAMSVVSQR-VD 424
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEpDERARAGLFLAFQYpEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 425 ILNGSLRDNL---LLADDTASDEKLIKTLN-----QVGLEALTTDEG-LNAWLGDGgrqLSGGERRRIGIARALLHDAPI 495
Cdd:TIGR01978 89 IPGVSNLEFLrsaLNARRSARGEEPLDLLDfekllKEKLALLDMDEEfLNRSVNEG---FSGGEKKRNEILQMALLEPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 496 VLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITH--RLVNLEQMDHICLMDHGEIVEQG 554
Cdd:TIGR01978 166 AILDEIDSGLDIDALKIVAEGINRlREPDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-554 |
3.31e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 60.63 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 338 NLTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPK-----SGYIAIDGVKL--PKWKES 410
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 411 SLRSAMSVVSQR---------VDILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTTDEglnawLGDGGRQLSGGERR 481
Cdd:PRK14267 82 EVRREVGMVFQYpnpfphltiYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDR-----LNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 482 RIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHKTVVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVG 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
356-554 |
3.70e-10 |
|
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: 59.58 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPK---SGYIAIDGVKLPKWKESSLRSAMSVVSQRVDILNGSLRD 432
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 433 NLLLADDTASDEKLiktlnqvglealttdeglnawlgdggRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQ 512
Cdd:cd03233 103 TLDFALRCKGNEFV--------------------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1906086718 513 IMSVLNK--HIEHKTVVFITHRLVN--LEQMDHICLMDHGEIVEQG 554
Cdd:cd03233 157 ILKCIRTmaDVLKTTTFVSLYQASDeiYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
359-561 |
3.79e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAID--GVKLPKWKESSLRsAMSVVSQRVDILNG-SLRDNLL 435
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLHARARR-GIGYLPQEASIFRRlSVYDNLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 436 LADDTASDekLIKTLNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMS 515
Cdd:PRK10895 101 AVLQIRDD--LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1906086718 516 VLNKHIEHKTVVFITHRlvNLEQMDHIC----LMDHGEIVEQGTHDSLLS 561
Cdd:PRK10895 179 IIEHLRDSGLGVLITDH--NVRETLAVCerayIVSQGHLIAHGTPTEILQ 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
339-548 |
4.17e-10 |
|
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: 59.18 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADTNA--INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPK--SGYIAIDGVKLPKwkesSLRS 414
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK----NFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 415 AMSVVSQrVDILNGSLrdnllladdtasdeklikTLNqvglEALTtdegLNAWLgdggRQLSGGERRRIGIARALLHDAP 494
Cdd:cd03232 80 STGYVEQ-QDVHSPNL------------------TVR----EALR----FSALL----RGLSVEQRKRLTIGVELAAKPS 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 495 IVLLDEPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHR--LVNLEQMDHICLMDHG 548
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIVRFLKKLADSgQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
359-554 |
5.68e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.08 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTrqwdPKSGYIAIDGvklpkwkesslrsamSVVSQRVDILNgslrdnlLLAD 438
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIM----GHPKYEVTEG---------------EILFKGEDITD-------LPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 439 DTAsdeKLIKTL---NQVGLEALTTDEGLNAwLGDGgrqLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMS 515
Cdd:cd03217 73 ERA---RLGIFLafqYPPEIPGVKNADFLRY-VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1906086718 516 VLNK-HIEHKTVVFITH--RLVNLEQMDHICLMDHGEIVEQG 554
Cdd:cd03217 146 VINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
355-533 |
9.55e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDG----VKLPKwkeSSLRSAMSVVSQRVDIL-NGS 429
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevtFNGPK---SSQEAGIGIIHQELNLIpQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 430 LRDNLLLADD-------------TASDEKLIKTLNqvglealttdeglnawLGDGGRQLSG----GERRRIGIARALLHD 492
Cdd:PRK10762 96 IAENIFLGREfvnrfgridwkkmYAEADKLLARLN----------------LRFSSDKLVGelsiGEQQMVEIAKVLSFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1906086718 493 APIVLLDEPTEGL-DQKTEqQIMSVLNK-HIEHKTVVFITHRL 533
Cdd:PRK10762 160 SKVIIMDEPTDALtDTETE-SLFRVIRElKSQGRGIVYISHRL 201
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
356-561 |
1.21e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.89 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQkmaIV---GQTGSGKSTLLQLLTRQWDPKSGYIAIDGV---KLPKWK-----------ESSLRSAMSV 418
Cdd:COG1137 19 VKDVSLEVNQGE---IVgllGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEditHLPMHKrarlgigylpqEASIFRKLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 419 vsqrvdilngslRDNLLLA------DDTASDEKLIKTLNQVGLEALTTDEGLnawlgdggrQLSGGERRRIGIARALLHD 492
Cdd:COG1137 96 ------------EDNILAVlelrklSKKEREERLEELLEEFGITHLRKSKAY---------SLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 493 APIVLLDEPTEGLDQKTEQQIMSVLnKHIEHKTV-VFIThrlvnleqmDH-------IC----LMDHGEIVEQGTHDSLL 560
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKII-RHLKERGIgVLIT---------DHnvretlgICdrayIISEGKVLAEGTPEEIL 224
|
.
gi 1906086718 561 S 561
Cdd:COG1137 225 N 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
356-555 |
1.24e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.93 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLT--RQWDPKSGYIAIDGVKLPKWK--EsslRSAMSV------------V 419
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSpdE---RARAGIflafqypveipgV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 420 SQRvDILNGSLRDNLLLADDTASDEKLIKT-LNQVGLEalttDEGLNAWLGDGgrqLSGGERRRIGIARALLHDAPIVLL 498
Cdd:COG0396 93 SVS-NFLRTALNARRGEELSAREFLKLLKEkMKELGLD----EDFLDRYVNEG---FSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 499 DEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITH--RLVNLEQMDHICLMDHGEIVEQGT 555
Cdd:COG0396 165 DETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
424-555 |
1.32e-09 |
|
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: 59.17 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 424 DILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTtdeglnawLGDGGRQLSGGERRRIGIARALLHDAP---IVLLDE 500
Cdd:cd03271 127 DVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIK--------LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDE 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 501 PTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQMDHICLM-----DH-GEIVEQGT 555
Cdd:cd03271 199 PTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNLDVIKCADWIIDLgpeggDGgGQVVASGT 260
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
352-557 |
1.32e-09 |
|
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: 60.61 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 352 DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTR-----QWDpksGYIAIDGVKLpkwKESSLR----SAMSVVSQR 422
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgTWD---GEIYWSGSPL---KASNIRdterAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 423 VDIL-NGSLRDNLLLA----------DDTASDEKLIKTLNQVGLEALTTDEGLNawlgdggrQLSGGERRRIGIARALLH 491
Cdd:TIGR02633 87 LTLVpELSVAENIFLGneitlpggrmAYNAMYLRAKNLLRELQLDADNVTRPVG--------DYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 492 DAPIVLLDEPTEGLDQKtEQQIMSVLNKHIEHKTV--VFITHRLVNLEQM-DHICLMDHGEIVeqGTHD 557
Cdd:TIGR02633 159 QARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVacVYISHKLNEVKAVcDTICVIRDGQHV--ATKD 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
351-561 |
1.55e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 351 ADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVSQRvdilngsl 430
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQR-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 431 RDNLLLADD------TASDEKLIKTLNQVGLEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEG 504
Cdd:PRK10938 86 NNTDMLSPGeddtgrTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 505 LDQKTEQQIMSVLNK-HIEHKTVVFITHRLVNL-EQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK10938 166 LDVASRQQLAELLASlHQSGITLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
316-543 |
1.99e-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: 60.80 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 316 EIITAEPDTVFDENgvDQAIKGN-----LTISNVDYQYMDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQW 390
Cdd:TIGR01257 1912 EPIFDEDDDVAEER--QRIISGGnktdiLRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDT 1989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 391 DPKSGYIAIDGvklpkwkeSSLRSAMSVVSQRV----------DILNGslRDNLLL-ADDTASDEKLIKTLNQVGLEALt 459
Cdd:TIGR01257 1990 TVTSGDATVAG--------KSILTNISDVHQNMgycpqfdaidDLLTG--REHLYLyARLRGVPAEEIEKVANWSIQSL- 2058
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 460 tdeGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHI-EHKTVVFITHrlvNLEQ 538
Cdd:TIGR01257 2059 ---GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSH---SMEE 2132
|
....*
gi 1906086718 539 MDHIC 543
Cdd:TIGR01257 2133 CEALC 2137
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
352-555 |
3.22e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 352 DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQ--WDPKSGYIAIDGVKLPKwKESSLRSAMSVV---SQRVDIL 426
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILD-LEPEERAHLGIFlafQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 427 NGSLRDNLLLA-------------DDTASDEKLIKTLNQVGLEALTtdegLNAWLGDGgrqLSGGERRRIGIARALLHDA 493
Cdd:CHL00131 98 GVSNADFLRLAynskrkfqglpelDPLEFLEIINEKLKLVGMDPSF----LSRNVNEG---FSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 494 PIVLLDEPTEGLDQKTEQQIMSVLNKHI-EHKTVVFITH--RLVNLEQMDHICLMDHGEIVEQGT 555
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
366-532 |
3.43e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 366 GQKMAIVGQTGSGKSTLLQLLTR--QWDPKSGYIAIDGVKLPKwkesSLRSAMSVVSQRvDILNGSL--RDNLLLADDTA 441
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTK----QILKRTGFVTQD-DILYPHLtvRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 442 SDEKLIKTLNQVGLEALTTDEGL----NAWLGDGG-RQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSV 516
Cdd:PLN03211 169 LPKSLTKQEKILVAESVISELGLtkceNTIIGNSFiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170
....*....|....*..
gi 1906086718 517 LNKHIEH-KTVVFITHR 532
Cdd:PLN03211 249 LGSLAQKgKTIVTSMHQ 265
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
371-531 |
4.41e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 371 IVGQTGSGKSTLLQLLTRQWDPKSGYIAIDgVKLpKWKESSLRSAMSVvsqRVDILNGSLRDNLllaDDTASDEKLIKTL 450
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKI-SYKPQYIKPDYDG---TVEDLLRSITDDL---GSSYYKSEIIKPL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 451 NqvgLEALttdegLNAWLGDggrqLSGGERRRIGIARALLHDAPIVLLDEPTEGLDqkTEQQIM--SVLNKHIEH--KTV 526
Cdd:PRK13409 442 Q---LERL-----LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAvaKAIRRIAEEreATA 507
|
....*
gi 1906086718 527 VFITH 531
Cdd:PRK13409 508 LVVDH 512
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
355-551 |
6.19e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLP-KWKESSLRSAMSVVSQRVD-ILNGSLRD 432
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNlVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 433 NLLLADDTAS----DEKliKTLNQVglEALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQK 508
Cdd:PRK10982 93 NMWLGRYPTKgmfvDQD--KMYRDT--KAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1906086718 509 TEQQIMSVLNKHIEHKT-VVFITHRLVNLEQM-DHICLMDHGEIV 551
Cdd:PRK10982 169 EVNHLFTIIRKLKERGCgIVYISHKMEEIFQLcDEITILRDGQWI 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
359-531 |
6.32e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSG-YIAIDGVK---LPKwkESSLRSAMSV-------VSQRVDILN 427
Cdd:PRK11819 26 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIKvgyLPQ--EPQLDPEKTVrenveegVAEVKAALD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 428 GSLRDNLLLADDTASDEKLIKtlNQVGLEALTtdEGLNAWlgDGGRQ-------------------LSGGERRRIGIARA 488
Cdd:PRK11819 104 RFNEIYAAYAEPDADFDALAA--EQGELQEII--DAADAW--DLDSQleiamdalrcppwdakvtkLSGGERRRVALCRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1906086718 489 LLHDAPIVLLDEPTEGLDQKteqqimSV--LNKHIE--HKTVVFITH 531
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLDAE------SVawLEQFLHdyPGTVVAVTH 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
339-555 |
9.98e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.06 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDADT--NAINAISLDLLSGQKMAIVGQTGSGKS----TLLQLLTRQWDPKSGYIAIDGVKLPKWKE--- 409
Cdd:PRK11022 4 LNVDKLSVHFGDESApfRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEker 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 410 ----------------SSLRSAMSVVSQRVDILN----GSLRdnllladdtASDEKLIKTLNQVGLEALTTDegLNAWlg 469
Cdd:PRK11022 84 rnlvgaevamifqdpmTSLNPCYTVGFQIMEAIKvhqgGNKK---------TRRQRAIDLLNQVGIPDPASR--LDVY-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 470 dgGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLN--KHIEHKTVVFITHRLVNL-EQMDHICLMD 546
Cdd:PRK11022 151 --PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLelQQKENMALVLITHDLALVaEAAHKIIVMY 228
|
....*....
gi 1906086718 547 HGEIVEQGT 555
Cdd:PRK11022 229 AGQVVETGK 237
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
353-552 |
1.11e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 353 TNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQ--WDPKSGYIAIDGVKLPKwkesslrsamsvvsqrvdilNGSL 430
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPDNQFGR--------------------EASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 431 RDNLLLADDTASdekLIKTLNQVGL-EALTtdeglnaWLGDgGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKT 509
Cdd:COG2401 103 IDAIGRKGDFKD---AVELLNAVGLsDAVL-------WLRR-FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1906086718 510 EQQIMSVLNKHI-EH-KTVVFITHR--LVNLEQMDHICLMDHGEIVE 552
Cdd:COG2401 172 AKRVARNLQKLArRAgITLVVATHHydVIDDLQPDLLIFVGYGGVPE 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
366-533 |
1.22e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 366 GQKMAIVGQTGSGKSTLLQLLTRQWDPKSGyiaiDGVKLPKWKE--------------SSLRS-AMSVV--SQRVDI--- 425
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLG----DYEEEPSWDEvlkrfrgtelqnyfKKLYNgEIKVVhkPQYVDLipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 426 -LNGSLRDNLLLADDTASDEKLIKTLNqvglealttdegLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEG 504
Cdd:PRK13409 175 vFKGKVRELLKKVDERGKLDEVVERLG------------LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180
....*....|....*....|....*....
gi 1906086718 505 LDQKTEQQIMSVLNKHIEHKTVVFITHRL 533
Cdd:PRK13409 243 LDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
356-513 |
1.27e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 55.18 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPK---SGYIAIDGVKLpkwkesslrSAMSVVSQRVDIL------ 426
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRL---------TALPAEQRRIGILfqddll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 427 --NGSLRDNLLLA-----DDTASDEKLIKTLNQVGLEALttdeglnawlgdGGR---QLSGGERRRIGIARALLHDAPIV 496
Cdd:COG4136 88 fpHLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGF------------ADRdpaTLSGGQRARVALLRALLAEPRAL 155
|
170
....*....|....*..
gi 1906086718 497 LLDEPTEGLDQKTEQQI 513
Cdd:COG4136 156 LLDEPFSKLDAALRAQF 172
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
341-509 |
1.88e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 341 ISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIdGVKL-------------PKw 407
Cdd:PRK11147 322 MENVNYQI--DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLevayfdqhraeldPE- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 408 kesslRSAMSVVS---QRVDIlNGSLRDNLLLADDTASDEKliktlnqvglEALTTdeglnawlgdgGRQLSGGERRRIG 484
Cdd:PRK11147 398 -----KTVMDNLAegkQEVMV-NGRPRHVLGYLQDFLFHPK----------RAMTP-----------VKALSGGERNRLL 450
|
170 180
....*....|....*....|....*
gi 1906086718 485 IARALLHDAPIVLLDEPTEGLDQKT 509
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDVET 475
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
370-554 |
1.97e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.42 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 370 AIVGQTGSGKSTLLQL---LTRqwdPKSGYIAID---------GVKLPKWK--------ESSLRSAMSVvsqrvdilngs 429
Cdd:PRK11144 28 AIFGRSGAGKTSLINAisgLTR---PQKGRIVLNgrvlfdaekGICLPPEKrrigyvfqDARLFPHYKV----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 430 lRDNLLL---ADDTASDEKLIKTLnqvGLEALttdeglnawLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLD 506
Cdd:PRK11144 94 -RGNLRYgmaKSMVAQFDKIVALL---GIEPL---------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 507 QKTEQQIMSVLNKHIEH-KT-VVFITHRLVNLEQM-DHICLMDHGEIVEQG 554
Cdd:PRK11144 161 LPRKRELLPYLERLAREiNIpILYVSHSLDEILRLaDRVVVLEQGKVKAFG 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
338-555 |
2.12e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.39 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 338 NLTISNVDYQYmDADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvKLPKWKESSLRS-AM 416
Cdd:PRK11650 3 GLKLQAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG-RVVNELEPADRDiAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 svVSQrvdilNGSL------RDNL---LLADDTASDEkliktLNQVGLEALTTDEgLNAWLGDGGRQLSGGERRRIGIAR 487
Cdd:PRK11650 81 --VFQ-----NYALyphmsvRENMaygLKIRGMPKAE-----IEERVAEAARILE-LEPLLDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 488 ALLHDAPIVLLDEPTEGLDQKTEQQiMSVLNKHIeHK----TVVFITHRLVnlEQM---DHICLMDHGEIvEQ-GT 555
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVQ-MRLEIQRL-HRrlktTSLYVTHDQV--EAMtlaDRVVVMNGGVA-EQiGT 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
356-509 |
3.56e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.10 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAI-DGVKLpkwkesslrsamSVVSQRVDILNGSlrdnl 434
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKL------------AYVDQSRDALDPN----- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 435 lladdtasdekliKTLNQV---GLEALT---TDEGLNAWLG----DGGRQ------LSGGERRRIGIARALLHDAPIVLL 498
Cdd:TIGR03719 401 -------------KTVWEEisgGLDIIKlgkREIPSRAYVGrfnfKGSDQqkkvgqLSGGERNRVHLAKTLKSGGNVLLL 467
|
170
....*....|.
gi 1906086718 499 DEPTEGLDQKT 509
Cdd:TIGR03719 468 DEPTNDLDVET 478
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
424-555 |
4.34e-08 |
|
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: 56.17 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 424 DILNGSLRDNLLLADDTASDEKLIKTLNQVGLEALTtdeglnawLGDGGRQLSGGERRRIGIARALLHDA---PIVLLDE 500
Cdd:TIGR00630 787 DVLDMTVEEAYEFFEAVPSISRKLQTLCDVGLGYIR--------LGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDE 858
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 501 PTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQMDHICLM-----DH-GEIVEQGT 555
Cdd:TIGR00630 859 PTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEHNLDVIKTADYIIDLgpeggDGgGTVVASGT 920
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
365-539 |
5.04e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.38 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 365 SGQKMAIVGQTGSGKSTLLQLLTRQWDPKS-GYIAIDGVKLPkwkesslrsamsvvsqrvdilngslrdnllladdtasd 443
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDIL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 444 ekliktlnqvgleALTTDEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMS-------V 516
Cdd:smart00382 43 -------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrllL 109
|
170 180
....*....|....*....|...
gi 1906086718 517 LNKHIEHKTVVFITHRLVNLEQM 539
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPA 132
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
355-555 |
5.94e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.93 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwKESSLrsamsvvsqrVDI---LNGSL- 430
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSAL----------LELgagFHPELt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 431 -RDNLLL--------ADDTasDEKL--IKTLNQVGlEALttDEGLnawlgdggRQLSGGERRRIGIARALLHDAPIVLLD 499
Cdd:COG1134 105 gRENIYLngrllglsRKEI--DEKFdeIVEFAELG-DFI--DQPV--------KTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 500 EPTEGLD----QKTEQQIMSVLNkhiEHKTVVFITHrlvNLEQMDHIC----LMDHGEIVEQGT 555
Cdd:COG1134 172 EVLAVGDaafqKKCLARIRELRE---SGRTVIFVSH---SMGAVRRLCdraiWLEKGRLVMDGD 229
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
469-559 |
7.98e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 469 GDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHI-EHKTVVFITHRLVNLEQMDH-ICLMD 546
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQLAHeLTVID 218
|
90
....*....|...
gi 1906086718 547 HGEIVEQGTHDSL 559
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
355-549 |
8.47e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTR-----QWDpksGYIAIDGVKLpkwKESSLR----SAMSVVSQRVDI 425
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgTYE---GEIIFEGEEL---QASNIRdterAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 426 L-NGSLRDNLLLA---------DDTASDEKLIKTLNQVGLealttdeGLNAWLGDGgrQLSGGERRRIGIARALLHDAPI 495
Cdd:PRK13549 94 VkELSVLENIFLGneitpggimDYDAMYLRAQKLLAQLKL-------DINPATPVG--NLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 496 VLLDEPTEGLdqkTEQQIMSVLN--KHIEHKTV--VFITHRLVNLEQM-DHICLMDHGE 549
Cdd:PRK13549 165 LILDEPTASL---TESETAVLLDiiRDLKAHGIacIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
366-531 |
8.93e-08 |
|
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: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 366 GQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIaidgvklpkwkESSLRsaMSVVSQRVDI-LNGSLRDNLLLADDTASDE 444
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLK--ISYKPQYISPdYDGTVEEFLRSANTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 445 KLIKT--LNQVGLEALttdegLNAWLGDggrqLSGGERRRIGIARALLHDAPIVLLDEPTEGLDqkTEQQIM--SVLNKH 520
Cdd:COG1245 433 SYYKTeiIKPLGLEKL-----LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAvaKAIRRF 501
|
170
....*....|...
gi 1906086718 521 IE--HKTVVFITH 531
Cdd:COG1245 502 AEnrGKTAMVVDH 514
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
366-557 |
1.23e-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: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 366 GQKMAIVGQTGSGKSTLLQLLTRQWD----PKSGYIAIDGVKLPKWKESslRSAMSVVSQRVDILNGSL--RDNLLLAD- 438
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKH--YRGDVVYNAETDVHFPHLtvGETLDFAAr 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 439 --------DTASDEKLIKTLNQVGLEALTTDEGLNAWLG-DGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKT 509
Cdd:TIGR00956 165 cktpqnrpDGVSREEYAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 510 EQQIMSVLnkhiehKTVVFITHR--LVNLEQ--------MDHICLMDHGEIVEQGTHD 557
Cdd:TIGR00956 245 ALEFIRAL------KTSANILDTtpLVAIYQcsqdayelFDKVIVLYEGYQIYFGPAD 296
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
356-559 |
1.81e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 53.18 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKwkesslrsamSVVSQRvDIL--------- 426
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH----------RSIQQR-DICmvfqsyalf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 427 -NGSLRDNL---LLADDTASDEklIKTLNQVGLEaLTTDEGLNAWLGDggrQLSGGERRRIGIARALLHDAPIVLLDEPT 502
Cdd:PRK11432 91 pHMSLGENVgygLKMLGVPKEE--RKQRVKEALE-LVDLAGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 503 EGLDQKTEQqimSVLNKHIEHKTVVFITHRLVNLEQM------DHICLMDHGEIVEQGTHDSL 559
Cdd:PRK11432 165 SNLDANLRR---SMREKIRELQQQFNITSLYVTHDQSeafavsDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
22-314 |
1.94e-07 |
|
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: 52.94 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 22 MLLSFATLFASIGLLTISGWFISAsAIAGLTIARETFNYMLPAGAVRGFSIGRTAGRWGERVVSHNATFKLLTELRIFFF 101
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKL-LIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 102 KKLIPLIPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPIIVGTLGIIGLTAFLAWFDITigLTLGAILLSLLLIWPTL 181
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWK--LTLVALLLLPLYVLILR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 182 FYKLGKHNGSELTQNKATLRIKTL-DWLQGNAELRIFGAEAQYRQRILDAQTALLANQHRMAALTGLANGLLLLANGWTL 260
Cdd:cd07346 158 YFRRRIRKASREVRESLAELSAFLqESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906086718 261 LLMLWIAGDGIAG--MTPDPMVAMVAFATMASFEL--LMPIAGAFQylgQTLSSARRL 314
Cdd:cd07346 238 ALVLLYGGYLVLQgsLTIGELVAFLAYLGMLFGPIqrLANLYNQLQ---QALASLERI 292
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
474-533 |
3.26e-07 |
|
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: 50.44 E-value: 3.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 474 QLSGGERRRIGIARAL----LHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHK-TVVFITHRL 533
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLP 141
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
302-506 |
3.83e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 302 QYLGQTLSSARRLNEIITAEPDtvfdENGVDQAIKGN---LTISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSG 378
Cdd:PRK10938 225 QALVAQLAHSEQLEGVQLPEPD----EPSARHALPANeprIVLNNGVVSY--NDRPILHNLSWQVNPGEHWQIVGPNGAG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 379 KSTLLQLLT---------------RQ-------WDPKS--GYIAidgvklpkwkeSSLRSAMSV-VSQRVDILNGSLrDN 433
Cdd:PRK10938 299 KSTLLSLITgdhpqgysndltlfgRRrgsgetiWDIKKhiGYVS-----------SSLHLDYRVsTSVRNVILSGFF-DS 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 434 LLLADdTASDEKliKTLNQVGLEALttdeGLNAWLGDGG-RQLSGGERRRIGIARALLHDAPIVLLDEPTEGLD 506
Cdd:PRK10938 367 IGIYQ-AVSDRQ--QKLAQQWLDIL----GIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
370-548 |
4.37e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 370 AIVGQTGSGKSTLLQLLTRQwdPKSGYIAIDgVKL---PKWKESSLRsaMSVVSQRVDILNG--SLRDNLL------LAD 438
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAGR--KTGGYIEGD-IRIsgfPKKQETFAR--ISGYCEQNDIHSPqvTVRESLIysaflrLPK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 439 DTASDEKLIkTLNQVgLEALTTDEGLNAWLG-DGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIM-SV 516
Cdd:PLN03140 985 EVSKEEKMM-FVDEV-MELVELDNLKDAIVGlPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMrTV 1062
|
170 180 190
....*....|....*....|....*....|....
gi 1906086718 517 LNKHIEHKTVVFITHR--LVNLEQMDHICLMDHG 548
Cdd:PLN03140 1063 RNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
356-517 |
5.50e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAI-DGVKLPKWKESSLRsamsvvsqrvdilngSLRdnl 434
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLE---------------FLR--- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 435 lladdtaSDEKLIKTLNQVGLEAltTDEGLNAWLGDGG----------RQLSGGERRRIGIARALLHDAPIVLLDEPTEG 504
Cdd:PRK10636 390 -------ADESPLQHLARLAPQE--LEQKLRDYLGGFGfqgdkvteetRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170
....*....|...
gi 1906086718 505 LDQKTEQQIMSVL 517
Cdd:PRK10636 461 LDLDMRQALTEAL 473
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
356-506 |
5.83e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.88 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAidgvklpkwKESSLRsaMSVVSQRVDI---LNGSLRD 432
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IGYVPQKLYLdttLPLTVNR 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906086718 433 NLLLADDTASDEkLIKTLNQVGLEALttdegLNAWLgdggRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLD 506
Cdd:PRK09544 89 FLRLRPGTKKED-ILPALKRVQAGHL-----IDAPM----QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
362-549 |
6.39e-07 |
|
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: 49.88 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 362 DLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLpkwkesslrsamSVVSQRVDilngslrdnllladdta 441
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP------------VYKPQYID----------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 442 sdekliktlnqvglealttdeglnawlgdggrqLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHI 521
Cdd:cd03222 72 ---------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180 190
....*....|....*....|....*....|
gi 1906086718 522 EH--KTVVFITHRLVNLEQMDHICLMDHGE 549
Cdd:cd03222 119 EEgkKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
366-531 |
7.40e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 366 GQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDG-VKLPKWKESSLR----SAMSVVSQRVDILNGSLRDNLLLADDT 440
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdLIVARLQQDPPRnvegTVYDFVAEGIEEQAEYLKRYHDISHLV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 441 ASD--EKLIKTLNQVgLEALttdEGLNAW------------LG-DGGRQL---SGGERRRIGIARALLHDAPIVLLDEPT 502
Cdd:PRK11147 109 ETDpsEKNLNELAKL-QEQL---DHHNLWqlenrinevlaqLGlDPDAALsslSGGWLRKAALGRALVSNPDVLLLDEPT 184
|
170 180 190
....*....|....*....|....*....|...
gi 1906086718 503 EGLDQKT----EQQIMSVlnkhieHKTVVFITH 531
Cdd:PRK11147 185 NHLDIETiewlEGFLKTF------QGSIIFISH 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
365-549 |
9.55e-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: 51.71 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 365 SGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGyiaiDGVKLPKWKE-------SSLRSAMSVVS----------QRVD--- 424
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG----DYDEEPSWDEvlkrfrgTELQDYFKKLAngeikvahkpQYVDlip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 425 -ILNGSLRDNLLLADDTASDEKLIKTLNqvglealttdegLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTE 503
Cdd:COG1245 174 kVFKGTVRELLEKVDERGKLDELAEKLG------------LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 504 GLDQKteqQIMSVlNKHI-----EHKTVVFITHRLVNLEQM-DHICLMdHGE 549
Cdd:COG1245 242 YLDIY---QRLNV-ARLIrelaeEGKYVLVVEHDLAILDYLaDYVHIL-YGE 288
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
359-551 |
2.36e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.40 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwKESSLRSAMSVVSQRV-----D------ILN 427
Cdd:COG1129 271 VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG------KPVRIRSPRDAIRAGIayvpeDrkgeglVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 428 GSLRDNLLLA-----------DDTASD---EKLIKTLNqV---GLEALTtdeglnawlgdggRQLSGGERRRIGIARALL 490
Cdd:COG1129 345 LSIRENITLAsldrlsrggllDRRRERalaEEYIKRLR-IktpSPEQPV-------------GNLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 491 HDAPIVLLDEPTEGLD--QKTE-QQIMSVLNKhiEHKTVVFITHRLVNLEQM-DHICLMDHGEIV 551
Cdd:COG1129 411 TDPKVLILDEPTRGIDvgAKAEiYRLIRELAA--EGKAVIVISSELPELLGLsDRILVMREGRIV 473
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
356-531 |
2.83e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIaidgvklpKWKESslrSAMSVVSQrvdilngslrDNll 435
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSEN---ANIGYYAQ----------DH-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 436 lADDTASDEKLIKTLNQVGLEAlTTDEGLNAWLG-------DGGRQ---LSGGERRRIGIARALLHDAPIVLLDEPTEGL 505
Cdd:PRK15064 392 -AYDFENDLTLFDWMSQWRQEG-DDEQAVRGTLGrllfsqdDIKKSvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
170 180
....*....|....*....|....*...
gi 1906086718 506 DQKTeqqIMSvLNKHIEH--KTVVFITH 531
Cdd:PRK15064 470 DMES---IES-LNMALEKyeGTLIFVSH 493
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
366-548 |
3.43e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 366 GQKMAIVGQTGSGKSTLLQLLTRQWDpkSGYIAiDGVKL---PKWKESSLRSAMSVVSQRVDILNGSLRDNLLLA----- 437
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVT--TGVIT-GGDRLvngRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSaylrq 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 438 ----DDTASDEKLIKTLNQVGLEALTtdeglNAWLGDGGRQLSGGERRRIGIARALL-HDAPIVLLDEPTEGLDQKTEQQ 512
Cdd:TIGR00956 866 pksvSKSEKMEYVEEVIKLLEMESYA-----DAVVGVPGEGLNVEQRKRLTIGVELVaKPKLLLFLDEPTSGLDSQTAWS 940
|
170 180 190
....*....|....*....|....*....|....*....
gi 1906086718 513 IMSVLNKHIEH-KTVVFITHR--LVNLEQMDHICLMDHG 548
Cdd:TIGR00956 941 ICKLMRKLADHgQAILCTIHQpsAILFEEFDRLLLLQKG 979
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
450-566 |
4.10e-06 |
|
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: 50.01 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 450 LNQVGLEALTtdeglnawLGDGGRQLSGGERRRIGIARALLHDAPIVL--LDEPTEGLDQKTEQQIMSVLnKHIEHK--T 525
Cdd:TIGR00630 472 LIDVGLDYLS--------LSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTL-KRLRDLgnT 542
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 526 VVFITHRLVNLEQMDHICLM-----DH-GEIVEQGTHDSLL----SLKGAY 566
Cdd:TIGR00630 543 LIVVEHDEDTIRAADYVIDIgpgagEHgGEVVASGTPEEILanpdSLTGQY 593
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
359-561 |
4.95e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.01 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 359 ISLDLLSGQKMAIVGQTGSGKSTLLQ----LLtrqwdPKSGYIAIDGVKLPKWKESSL-----------RSAMSV-VSQR 422
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELarhraylsqqqTPPFAMpVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 423 VDilngslrdnLLLADDTASDEkLIKTLNQVgLEALTTDEGLNAWLGdggrQLSGGERRRIGIARALLHDAP-------I 495
Cdd:PRK03695 90 LT---------LHQPDKTRTEA-VASALNEV-AEALGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQVWPdinpagqL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906086718 496 VLLDEPTEGLDqkTEQQimSVLNKHIEH-----KTVVFITHRLvN--LEQMDHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK03695 155 LLLDEPMNSLD--VAQQ--AALDRLLSElcqqgIAVVMSSHDL-NhtLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
371-509 |
5.22e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 371 IVGQTGSGKSTLLQLLTRQWDPKSGYIAI-DGVKLpkwkesslrsamSVVSQRvdilngslRDNLllaDDTasdekliKT 449
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKL------------AYVDQS--------RDAL---DPN-------KT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 450 LNQV---GLEALTtdeglnawLGD---------------GGRQ------LSGGERRRIGIARALLHDAPIVLLDEPTEGL 505
Cdd:PRK11819 405 VWEEisgGLDIIK--------VGNreipsrayvgrfnfkGGDQqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
....
gi 1906086718 506 DQKT 509
Cdd:PRK11819 477 DVET 480
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
341-560 |
5.61e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 341 ISNVDYQYmdADTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLltrqwdpksgyiaIDGVKlpkwkesslrsamsVVS 420
Cdd:NF033858 4 LEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSL-------------IAGAR--------------KIQ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 421 Q-RVDILNGSLRD--------------------NL---------------LLADDTASDEKLIktlnqvglEALTTDEGL 464
Cdd:NF033858 55 QgRVEVLGGDMADarhrravcpriaympqglgkNLyptlsvfenldffgrLFGQDAAERRRRI--------DELLRATGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 465 NAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLD-----Q--------KTEQQIMSVL--NKHIEHKtvvfi 529
Cdd:NF033858 127 APFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplsrrQfwelidriRAERPGMSVLvaTAYMEEA----- 201
|
250 260 270
....*....|....*....|....*....|.
gi 1906086718 530 thrlvnlEQMDHICLMDHGEIVEQGTHDSLL 560
Cdd:NF033858 202 -------ERFDWLVAMDAGRVLATGTPAELL 225
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
370-543 |
6.14e-06 |
|
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: 47.22 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 370 AIVGQTGSGKSTLLQLLTrqwdpksgyIAIDGVKLPKWKE-SSLRSAMSVVSQRVDIlngslrdNLLLADDTASDEKLIK 448
Cdd:cd03240 26 LIVGQNGAGKTTIIEALK---------YALTGELPPNSKGgAHDPKLIREGEVRAQV-------KLAFENANGKKYTITR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 449 TLNQVGLEALTTDEGLNAWLGDGGRQLSGGERR------RIGIARALLHDAPIVLLDEPTEGLD-QKTEQQIMSVLN--K 519
Cdd:cd03240 90 SLAILENVIFCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeENIEESLAEIIEerK 169
|
170 180
....*....|....*....|....*.
gi 1906086718 520 HIEHKTVVFITH--RLVNLeqMDHIC 543
Cdd:cd03240 170 SQKNFQLIVITHdeELVDA--ADHIY 193
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
361-506 |
6.55e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 361 LDLLSgqKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIaidgvklpkwkessLRSA---MSVVSQR-VDILNGSLRDNLLL 436
Cdd:PLN03073 532 IDLDS--RIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAkvrMAVFSQHhVDGLDLSSNPLLYM 595
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 437 AD--DTASDEKLIKTLNQVGLealTTDEGLNAWLgdggrQLSGGERRRIGIARALLHDAPIVLLDEPTEGLD 506
Cdd:PLN03073 596 MRcfPGVPEQKLRAHLGSFGV---TGNLALQPMY-----TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
365-530 |
7.01e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.15 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 365 SGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKLPKWKESSLRSAMSVVsqrvdilnGSLRDNLlladDTASDE 444
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHL--------PGLKADL----STLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 445 KLIKTLN-----QVGLEALTTdEGLNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK 519
Cdd:PRK13543 104 HFLCGLHgrrakQMPGSALAI-VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISA 182
|
170
....*....|.
gi 1906086718 520 HIEHKTVVFIT 530
Cdd:PRK13543 183 HLRGGGAALVT 193
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
356-555 |
8.03e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQL----LTRQWDPK----SGYIAIDG---VKLPKWKESSLRSAMSVVSQRVd 424
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRgarvTGDVTLNGeplAAIDAPRLARLRAVLPQAAQPA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 425 iLNGSLRDNLLLA---DDTASDEKLIKTlNQVGLEALTTdEGLNAWLGDGGRQLSGGERRRIGIARALL-----HDAPI- 495
Cdd:PRK13547 96 -FAFSAREIVLLGrypHARRAGALTHRD-GEIAWQALAL-AGATALVGRDVTTLSGGELARVQFARVLAqlwppHDAAQp 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906086718 496 ---VLLDEPTEGLDQKTEQQIMSVLNKHIE--HKTVVFITHRlVNL--EQMDHICLMDHGEIVEQGT 555
Cdd:PRK13547 173 pryLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHD-PNLaaRHADRIAMLADGAIVAHGA 238
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
339-561 |
8.52e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 339 LTISNVDYQYMDAD--TNAINAISLDLLSGQKMAIVGQTGSGKSTLLQlltrqwdpksgyiAIDGVKLPKWKESSLRSAM 416
Cdd:PRK15093 4 LDIRNLTIEFKTSDgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAK-------------AICGVTKDNWRVTADRMRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 417 SvvsqRVDILNGSLRDNLLLADDTAS----------------------------------------DEKLIKTLNQVGLE 456
Cdd:PRK15093 71 D----DIDLLRLSPRERRKLVGHNVSmifqepqscldpservgrqlmqnipgwtykgrwwqrfgwrKRRAIELLHRVGIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 457 ALttdeglNAWLGDGGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQI---MSVLNKHiEHKTVVFITHRL 533
Cdd:PRK15093 147 DH------KDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIfrlLTRLNQN-NNTTILLISHDL 219
|
250 260
....*....|....*....|....*....
gi 1906086718 534 VNLEQM-DHICLMDHGEIVEQGTHDSLLS 561
Cdd:PRK15093 220 QMLSQWaDKINVLYCGQTVETAPSKELVT 248
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
447-555 |
3.23e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.94 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 447 IKTLNQVGLEALTtdeglnawLGdggrQ----LSGGERRRIGIARALLHDAP---IVLLDEPTEGL---DqktEQQIMSV 516
Cdd:COG0178 807 LQTLQDVGLGYIK--------LG----QpattLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhD---IRKLLEV 871
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 517 LNKHIEHK-TVVFITHrlvNLEQM---DHIclMD--------HGEIVEQGT 555
Cdd:COG0178 872 LHRLVDKGnTVVVIEH---NLDVIktaDWI--IDlgpeggdgGGEIVAEGT 917
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
444-555 |
3.71e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.60 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 444 EKLiKTLNQVGLEALTtdeglnawLGDGGRQLSGGERRRIGIARALLHDA---PIVLLDEPTEGL---DQKteqQIMSVL 517
Cdd:PRK00349 809 RKL-QTLVDVGLGYIK--------LGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIR---KLLEVL 876
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1906086718 518 NKHIEH-KTVVFITHrlvNLE---QMDHICLM-----DH-GEIVEQGT 555
Cdd:PRK00349 877 HRLVDKgNTVVVIEH---NLDvikTADWIIDLgpeggDGgGEIVATGT 921
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
371-560 |
6.10e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 371 IVGQTGSGKSTLLQLLTRQWDPK---SGYIAIDGVKLPKW---KESSLRS-------AMSV------------VSQRVDI 425
Cdd:PLN03140 196 LLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFvprKTSAYISqndvhvgVMTVketldfsarcqgVGTRYDL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 426 LNGSLR-----------DNLLLADDTAS---DEKLIK--TLNQVGLE----ALTTDEGLnawlgdggRQLSGGERRRIGI 485
Cdd:PLN03140 276 LSELARrekdagifpeaEVDLFMKATAMegvKSSLITdyTLKILGLDickdTIVGDEMI--------RGISGGQKKRVTT 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 486 ARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLnKHIEHKTVVFIthrLVNLEQ--------MDHICLMDHGEIVEQGTHD 557
Cdd:PLN03140 348 GEMIVGPTKTLFMDEISTGLDSSTTYQIVKCL-QQIVHLTEATV---LMSLLQpapetfdlFDDIILLSEGQIVYQGPRD 423
|
...
gi 1906086718 558 SLL 560
Cdd:PLN03140 424 HIL 426
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
473-550 |
8.35e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.43 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 473 RQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLnKHI--EHKTVVFITHRLVNLEQM-DHICLMDHGE 549
Cdd:PRK15439 402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLI-RSIaaQNVAVLFISSDLEEIEQMaDRVLVMHQGE 480
|
.
gi 1906086718 550 I 550
Cdd:PRK15439 481 I 481
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
34-244 |
1.21e-04 |
|
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: 44.32 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 34 GLLTISGWFISASAIAGLTIARETFNYMLPA-GAVRGFSIGRTAGRWGERVVSHNATFKLLTELRIFFFKKLIPLIPGRF 112
Cdd:cd18584 9 ALLIIAQAWLLARIIAGVFLEGAGLAALLPLlLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 113 SKLRDADLLNRLVADVDAMDhVYLRLVSPIIVGTLGI-IGLTAFLAWFDITIGLTLGAillsllliwpT-----LFYKL- 185
Cdd:cd18584 89 RRQSSGELATLLTEGVDALD-GYFARYLPQLVLAAIVpLLILVAVFPLDWVSALILLV----------TaplipLFMILi 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 186 GKHngselTQNKATLRIKT--------LDWLQGNAELRIFGAEAQYRQRIldaqtALLANQHR---MAAL 244
Cdd:cd18584 158 GKA-----AQAASRRQWAAlsrlsghfLDRLRGLPTLKLFGRARAQAARI-----ARASEDYRrrtMKVL 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
356-531 |
1.50e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQwdpksgyiAIDGvkLPKW-------------KESSLRSAMSVVSQR 422
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMH--------AIDG--IPKNcqilhveqevvgdDTTALQCVLNTDIER 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 423 VDIL--------------------NGSLRDNLLLADDTASD--EKLIKTLNQVglEALTTDEGLNAWLG----------D 470
Cdd:PLN03073 263 TQLLeeeaqlvaqqrelefetetgKGKGANKDGVDKDAVSQrlEEIYKRLELI--DAYTAEARAASILAglsftpemqvK 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906086718 471 GGRQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHieHKTVVFITH 531
Cdd:PLN03073 341 ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSH 399
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-314 |
1.57e-04 |
|
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: 43.95 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 18 LTLGMLLSFATLFASIGLLTISGWFISASAIAGltiaRETFNYMLPAGAVrGFSIGRTAGRWGERVVSHNATFKLLTELR 97
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEK----DLEALLLVPLAII-GLFLLRGLASYLQTYLMAYVGQRVVRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 98 IFFFKKLIPLIPGRFSKLRDADLLNRLVADVDAMDHVYLRLVSPIIVGTLGIIGLTAFLAWFDITigLTLGAILLSLLLI 177
Cdd:cd18552 76 NDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWK--LTLIALVVLPLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 178 WPTlfYKLGK--HNGSELTQNKATLRIKTLD-WLQGNAELRIFGAEAQYRQRILDAQTALLANQHRMAALTGLANGLLLL 254
Cdd:cd18552 154 LPI--RRIGKrlRKISRRSQESMGDLTSVLQeTLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMEL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906086718 255 ANGWTLLLMLWIAGDGIA--GMTPDpmvAMVAFATMASFeLLMPI---AGAFQYLGQTLSSARRL 314
Cdd:cd18552 232 LGAIAIALVLWYGGYQVIsgELTPG---EFISFITALLL-LYQPIkrlSNVNANLQRGLAAAERI 292
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
352-552 |
2.56e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.62 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 352 DTNAINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKL-PKWKESSLRSAMSVVSQrvdilngSL 430
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsPRSPLDAVKKGMAYITE-------SR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 431 RDNLLLAD-DTASDEKLIKTLNQVGLEAL--TTDEGLNAWLGDGGR---------------QLSGGERRRIGIARALLHD 492
Cdd:PRK09700 348 RDNGFFPNfSIAQNMAISRSLKDGGYKGAmgLFHEVDEQRTAENQRellalkchsvnqnitELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906086718 493 APIVLLDEPTEGLDQKTEQQIMSVLNKHIEH-KTVVFITHRLVNLEQM-DHICLMDHGEIVE 552
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
473-562 |
3.58e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.36 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 473 RQLSGGERRRIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHIEHK-TVVFITHRLVnlEQM---DHICLMDHG 548
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGvAVLFVSSDLP--EVLgvaDRIVVMREG 472
|
90
....*....|....*....
gi 1906086718 549 EIV-----EQGTHDSLLSL 562
Cdd:PRK11288 473 RIAgelarEQATERQALSL 491
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
450-566 |
3.93e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 450 LNQVGLEALTtdegLNawlgdggRQ---LSGGERRRIGIARAL---LHDapiVL--LDEPTEGLDQKTEQQIMSVLnkhi 521
Cdd:COG0178 469 LVDVGLDYLT----LD-------RSagtLSGGEAQRIRLATQIgsgLVG---VLyvLDEPSIGLHQRDNDRLIETL---- 530
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906086718 522 ehktvvfitHRLVNL----------EQM----DHICLM-----DH-GEIVEQGTHDSLL----SLKGAY 566
Cdd:COG0178 531 ---------KRLRDLgntvivvehdEDTiraaDYIIDIgpgagEHgGEVVAQGTPEEILknpdSLTGQY 590
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
356-518 |
5.47e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.89 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPK-SGYIAIDGvklpkwKESSLRSAMSVVSQRVDIL------NG 428
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFING------KPVDIRNPAQAIRAGIAMVpedrkrHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 429 SLRD-----NLLLA-----------DDTASDEKLIKTLNQVGLEALTTDeglnawLGDGGrqLSGGERRRIGIARALLHD 492
Cdd:TIGR02633 350 IVPIlgvgkNITLSvlksfcfkmriDAAAELQIIGSAIQRLKVKTASPF------LPIGR--LSGGNQQKAVLAKMLLTN 421
|
170 180
....*....|....*....|....*.
gi 1906086718 493 APIVLLDEPTEGLDQKTEQQIMSVLN 518
Cdd:TIGR02633 422 PRVLILDEPTRGVDVGAKYEIYKLIN 447
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
439-542 |
9.27e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 439 DTASDEKLIKTLNQVGLEALTtdeglnawLGDGGRQLSGGERRRIGIARALLHDAP---IVLLDEPTEGLDQKTEQQIMS 515
Cdd:PRK00635 782 DEPSIHEKIHALCSLGLDYLP--------LGRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIY 853
|
90 100
....*....|....*....|....*....
gi 1906086718 516 VLNK--HIEHkTVVFITHRLVNLEQMDHI 542
Cdd:PRK00635 854 VLQSltHQGH-TVVIIEHNMHVVKVADYV 881
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
355-566 |
1.04e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 355 AINAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGvklpkwKESSLRSAMSVVSQRVDILNGSLRDNL 434
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG------KKINNHNANEAINHGFALVTEERRSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 435 LLADDTASDEKLI----KTLNQVGLEALTTDEGLNAWLGDGGR-----------QLSGGERRRIGIARALLHDAPIVLLD 499
Cdd:PRK10982 337 IYAYLDIGFNSLIsnirNYKNKVGLLDNSRMKSDTQWVIDSMRvktpghrtqigSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906086718 500 EPTEGLD--QKTE-QQIMSVLNKhiEHKTVVFITHRLVNLEQM-DHICLMDHGE---IVE--QGTHDSLLSLKGAY 566
Cdd:PRK10982 417 EPTRGIDvgAKFEiYQLIAELAK--KDKGIIIISSEMPELLGItDRILVMSNGLvagIVDtkTTTQNEILRLASLH 490
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
356-560 |
1.89e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 356 INAISLDLLSGQKMAIVGQTGSGKSTLLQLLTRQWDPKSGYIAIDGVKL-PKWKESSLRSAMSVVSQ--RVD--ILNGSL 430
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEdrKRDglVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 431 RDNLLLaddTA-------------SDEKL----------IKTLN---QVGLealttdeglnawlgdggrqLSGGERRRIG 484
Cdd:PRK10762 348 KENMSL---TAlryfsraggslkhADEQQavsdfirlfnIKTPSmeqAIGL-------------------LSGGNQQKVA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 485 IARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNK-HIEHKTVVFITHRLVNLEQM-DHICLMDHGEI-----VEQGTHD 557
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQfKAEGLSIILVSSEMPEVLGMsDRILVMHEGRIsgeftREQATQE 485
|
...
gi 1906086718 558 SLL 560
Cdd:PRK10762 486 KLM 488
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
482-550 |
3.42e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 3.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906086718 482 RIGIARALLHDAPIVLLDEPTEGLDQKTEQQIMSVLNKHieHKTVVFITHRLVNLEQM-DHICLMDHGEI 550
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNER--NSTMIIISHDRHFLNSVcTHMADLDYGEL 230
|
|
| |
