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Conserved domains on  [gi|981585856|ref|WP_059786839|]
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lipase secretion chaperone [Burkholderia multivorans]

Protein Classification

lipase secretion chaperone( domain architecture ID 11479520)

lipase secretion chaperone may be involved in the folding of the extracellular lipase during its passage through the periplasm

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK01294 PRK01294
lipase secretion chaperone;
9-338 3.73e-84

lipase secretion chaperone;


:

Pssm-ID: 234937 [Multi-domain]  Cd Length: 336  Bit Score: 258.45  E-value: 3.73e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856   9 PPMRRVAVYAIAGCAAVAAVVLWRGAPPPRGIEVAHAGLQAGERNAIAL-PSPATPPAGASVPAPLAGSSAPRLPLDPGG 87
Cdd:PRK01294   1 MKKKRALSLGLVGLVAIGAVWLWPGDPANSSAGAASAAAAAAAAALSAAaAPAAADAAVAALPASLAGTSVPGLPLDAQG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856  88 HLAKSRAVRDFFDYCLTAQSELDAAALDALVAREIAAQLDgTVAQAEALDVWHRYRAYRDALAKLPDAGAvtDKSDLGAL 167
Cdd:PRK01294  81 HLADTRALRDFFDYFLSALGELDLAAIDALVEREIAAQLP-EPADSQALDLWLRYKAYLSALAQLEDDGP--GKLDLQAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856 168 QLALDRRASIAYRTLGDWS-EPFFGAEQWRQRYDLARLRIMQDRTLTDAQKAERLAALDQQMPADERAAQQRANAQQAAI 246
Cdd:PRK01294 158 QQLLDARLALRARFFSDWEiQAFFGEENQYQRYALERLRIAQDPSLSDAQKAARLAALEAQLPEDLRAALQESQRQQALL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856 247 DRIAQWQKSGAAPDATRAALAQTLGADVAARVAQLQQDDAAWQSRYADYAAQRAQIE-AAGLSPQDRDAQIAALRQRMFt 325
Cdd:PRK01294 238 QQLAQLQASGASPQELRLMRAQLVGPEAAQRLEQLDQQRAAWQQRYDDYLAQRAQILnAAGLSPQDRQAQIAQLRQQRF- 316
                        330
                 ....*....|...
gi 981585856 326 KPGEAVRAASLDR 338
Cdd:PRK01294 317 SPQEALRLAALER 329
 
Name Accession Description Interval E-value
PRK01294 PRK01294
lipase secretion chaperone;
9-338 3.73e-84

lipase secretion chaperone;


Pssm-ID: 234937 [Multi-domain]  Cd Length: 336  Bit Score: 258.45  E-value: 3.73e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856   9 PPMRRVAVYAIAGCAAVAAVVLWRGAPPPRGIEVAHAGLQAGERNAIAL-PSPATPPAGASVPAPLAGSSAPRLPLDPGG 87
Cdd:PRK01294   1 MKKKRALSLGLVGLVAIGAVWLWPGDPANSSAGAASAAAAAAAAALSAAaAPAAADAAVAALPASLAGTSVPGLPLDAQG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856  88 HLAKSRAVRDFFDYCLTAQSELDAAALDALVAREIAAQLDgTVAQAEALDVWHRYRAYRDALAKLPDAGAvtDKSDLGAL 167
Cdd:PRK01294  81 HLADTRALRDFFDYFLSALGELDLAAIDALVEREIAAQLP-EPADSQALDLWLRYKAYLSALAQLEDDGP--GKLDLQAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856 168 QLALDRRASIAYRTLGDWS-EPFFGAEQWRQRYDLARLRIMQDRTLTDAQKAERLAALDQQMPADERAAQQRANAQQAAI 246
Cdd:PRK01294 158 QQLLDARLALRARFFSDWEiQAFFGEENQYQRYALERLRIAQDPSLSDAQKAARLAALEAQLPEDLRAALQESQRQQALL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856 247 DRIAQWQKSGAAPDATRAALAQTLGADVAARVAQLQQDDAAWQSRYADYAAQRAQIE-AAGLSPQDRDAQIAALRQRMFt 325
Cdd:PRK01294 238 QQLAQLQASGASPQELRLMRAQLVGPEAAQRLEQLDQQRAAWQQRYDDYLAQRAQILnAAGLSPQDRQAQIAQLRQQRF- 316
                        330
                 ....*....|...
gi 981585856 326 KPGEAVRAASLDR 338
Cdd:PRK01294 317 SPQEALRLAALER 329
LimK COG5380
Lipase chaperone LimK [Posttranslational modification, protein turnover, chaperones];
61-338 3.85e-61

Lipase chaperone LimK [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444145 [Multi-domain]  Cd Length: 304  Bit Score: 197.92  E-value: 3.85e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856  61 ATPPAGASVPAPLAGSSAP-RLPLDPGGHLAKSRAVRDFFDYCLTAQSELDAAALDALVAREIAAQLdGTVAQAEALDVW 139
Cdd:COG5380   23 QAASTGPSLPPSLAGTDVDgALKVDANGNLILDREVRDLFDYFLSALGEESLAAIRARIQAYIRRQL-PEPAAAQALALL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856 140 HRYRAYRDALAKLPDAGAVtDKSDLGALQLALDRRASIAYRTLG-DWSEPFFGAEQWRQRYDLARLRIMQDRTLTDAQKA 218
Cdd:COG5380  102 DRYLAYKEALAELEAQAGP-ASADLEDLRQRLEELQALRRQYLGpDEADAFFGDEEAYDDYTLARLEILQDPALSAEEKA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856 219 ERLAALDQQMPADERAAQQRANAQQAAIDRIAQWQKSGAAPDATRAALAQTLGADVAARVAQLQQDDAAWQSRYADYAAQ 298
Cdd:COG5380  181 AQLAALEAQLPEEVREARQAALRLAELAAQEAELRAQGASAAELRQLRAALVGPEAADRLAALDQQRAQWQQRLDAYLAE 260
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 981585856 299 RAQIEAAGLSPQDRDAQIAALRQRMFTkPGEAVRAASLDR 338
Cdd:COG5380  261 RAQILDSGLSPADRQAALEQLRQQHFS-PQERLRVEALER 299
Lipase_chap pfam03280
Proteobacterial lipase chaperone protein;
138-322 5.54e-39

Proteobacterial lipase chaperone protein;


Pssm-ID: 427230 [Multi-domain]  Cd Length: 185  Bit Score: 136.67  E-value: 5.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856  138 VWHRYRAYRDALAKLPDAGAVTDKsDLGALQLALDRRASIAYRTLG-DWSEPFFGAEQWRQRYDLARLRIMQDRTLTDAQ 216
Cdd:pfam03280   1 LFQRYLAYKEALAELDAPAPALGD-SLAALRARLEQLQALRRRYFSpEEADALFGEEEAYDRYALERLAIAQDSALSAEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856  217 KAERLAALDQQMPADERAAQQRANAQQAAIDRIAQWQKSGAAPDATRAALAQTLGADVAARVAQLQQDDAAWQSRYADYA 296
Cdd:pfam03280  80 KQQRLAALRAQLPEDLRAAREAQQRLQELAARTAQLQKAGASPQQLRQARAQLVGPEAAQRLAALDQQRAAWQQRLDDYL 159
                         170       180
                  ....*....|....*....|....*.
gi 981585856  297 AQRAQIEAAGLSPQDRDAQIAALRQR 322
Cdd:pfam03280 160 AERQQINAAGLSEQERQAAIAQLRQQ 185
 
Name Accession Description Interval E-value
PRK01294 PRK01294
lipase secretion chaperone;
9-338 3.73e-84

lipase secretion chaperone;


Pssm-ID: 234937 [Multi-domain]  Cd Length: 336  Bit Score: 258.45  E-value: 3.73e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856   9 PPMRRVAVYAIAGCAAVAAVVLWRGAPPPRGIEVAHAGLQAGERNAIAL-PSPATPPAGASVPAPLAGSSAPRLPLDPGG 87
Cdd:PRK01294   1 MKKKRALSLGLVGLVAIGAVWLWPGDPANSSAGAASAAAAAAAAALSAAaAPAAADAAVAALPASLAGTSVPGLPLDAQG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856  88 HLAKSRAVRDFFDYCLTAQSELDAAALDALVAREIAAQLDgTVAQAEALDVWHRYRAYRDALAKLPDAGAvtDKSDLGAL 167
Cdd:PRK01294  81 HLADTRALRDFFDYFLSALGELDLAAIDALVEREIAAQLP-EPADSQALDLWLRYKAYLSALAQLEDDGP--GKLDLQAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856 168 QLALDRRASIAYRTLGDWS-EPFFGAEQWRQRYDLARLRIMQDRTLTDAQKAERLAALDQQMPADERAAQQRANAQQAAI 246
Cdd:PRK01294 158 QQLLDARLALRARFFSDWEiQAFFGEENQYQRYALERLRIAQDPSLSDAQKAARLAALEAQLPEDLRAALQESQRQQALL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856 247 DRIAQWQKSGAAPDATRAALAQTLGADVAARVAQLQQDDAAWQSRYADYAAQRAQIE-AAGLSPQDRDAQIAALRQRMFt 325
Cdd:PRK01294 238 QQLAQLQASGASPQELRLMRAQLVGPEAAQRLEQLDQQRAAWQQRYDDYLAQRAQILnAAGLSPQDRQAQIAQLRQQRF- 316
                        330
                 ....*....|...
gi 981585856 326 KPGEAVRAASLDR 338
Cdd:PRK01294 317 SPQEALRLAALER 329
LimK COG5380
Lipase chaperone LimK [Posttranslational modification, protein turnover, chaperones];
61-338 3.85e-61

Lipase chaperone LimK [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444145 [Multi-domain]  Cd Length: 304  Bit Score: 197.92  E-value: 3.85e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856  61 ATPPAGASVPAPLAGSSAP-RLPLDPGGHLAKSRAVRDFFDYCLTAQSELDAAALDALVAREIAAQLdGTVAQAEALDVW 139
Cdd:COG5380   23 QAASTGPSLPPSLAGTDVDgALKVDANGNLILDREVRDLFDYFLSALGEESLAAIRARIQAYIRRQL-PEPAAAQALALL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856 140 HRYRAYRDALAKLPDAGAVtDKSDLGALQLALDRRASIAYRTLG-DWSEPFFGAEQWRQRYDLARLRIMQDRTLTDAQKA 218
Cdd:COG5380  102 DRYLAYKEALAELEAQAGP-ASADLEDLRQRLEELQALRRQYLGpDEADAFFGDEEAYDDYTLARLEILQDPALSAEEKA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856 219 ERLAALDQQMPADERAAQQRANAQQAAIDRIAQWQKSGAAPDATRAALAQTLGADVAARVAQLQQDDAAWQSRYADYAAQ 298
Cdd:COG5380  181 AQLAALEAQLPEEVREARQAALRLAELAAQEAELRAQGASAAELRQLRAALVGPEAADRLAALDQQRAQWQQRLDAYLAE 260
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 981585856 299 RAQIEAAGLSPQDRDAQIAALRQRMFTkPGEAVRAASLDR 338
Cdd:COG5380  261 RAQILDSGLSPADRQAALEQLRQQHFS-PQERLRVEALER 299
Lipase_chap pfam03280
Proteobacterial lipase chaperone protein;
138-322 5.54e-39

Proteobacterial lipase chaperone protein;


Pssm-ID: 427230 [Multi-domain]  Cd Length: 185  Bit Score: 136.67  E-value: 5.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856  138 VWHRYRAYRDALAKLPDAGAVTDKsDLGALQLALDRRASIAYRTLG-DWSEPFFGAEQWRQRYDLARLRIMQDRTLTDAQ 216
Cdd:pfam03280   1 LFQRYLAYKEALAELDAPAPALGD-SLAALRARLEQLQALRRRYFSpEEADALFGEEEAYDRYALERLAIAQDSALSAEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981585856  217 KAERLAALDQQMPADERAAQQRANAQQAAIDRIAQWQKSGAAPDATRAALAQTLGADVAARVAQLQQDDAAWQSRYADYA 296
Cdd:pfam03280  80 KQQRLAALRAQLPEDLRAAREAQQRLQELAARTAQLQKAGASPQQLRQARAQLVGPEAAQRLAALDQQRAAWQQRLDDYL 159
                         170       180
                  ....*....|....*....|....*.
gi 981585856  297 AQRAQIEAAGLSPQDRDAQIAALRQR 322
Cdd:pfam03280 160 AERQQINAAGLSEQERQAAIAQLRQQ 185
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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