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Conserved domains on  [gi|81539798|sp|Q9HVD1|]
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RecName: Full=Lipid A deacylase PagL; AltName: Full=LPS 3-O-deacylase PagL; AltName: Full=Outer membrane enzyme PagL; AltName: Full=PhoP/PhoQ-activated gene product L; Flags: Precursor

Protein Classification

acyloxyacyl hydrolase( domain architecture ID 10559446)

acyloxyacyl hydrolase has lipid A 3-O-deacylase activity; it hydrolyzes the ester bond at the 3 position of lipid A, a bioactive component of lipopolysaccharide (LPS), thereby releasing the primary fatty acyl moiety

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PagL pfam09411
Lipid A 3-O-deacylase (PagL); PagL is an outer membrane protein with lipid A 3-O-deacylase ...
 38-169 4.47e-37

Lipid A 3-O-deacylase (PagL); PagL is an outer membrane protein with lipid A 3-O-deacylase activity. It forms an 8 stranded beta barrel structure.


:

Pssm-ID: 462791  Cd Length: 129  Bit Score: 124.51  E-value: 4.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81539798    38 MTYRLG--LSWDWDKSWWQTSTGRLTGYWDAGYTYWeggdegagkHSLSFAPVFVYEFAGDSIKPFIEAGIGVAAFSGTR 115
Cdd:pfam09411   1 AYYGLSyqLFWDWGERWYNSPDWGLSLYWDAGYNAW---------LGLGVTPVFRFFFWSGKRGPYLEAGIGVAYLSRTN 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 81539798   116 VGDQNLGSSLNFEDRIGAGLKFANGQ-SVGVRAIHYSNAGLKQPNDGIESYSLFY 169
Cdd:pfam09411  72 FGDNDLGTRFQFRDQAGLGYRFGEGNlSLGLRFQHYSNAGIKDPNPGLNSLGLNL 126
 
Name Accession Description Interval E-value
PagL pfam09411
Lipid A 3-O-deacylase (PagL); PagL is an outer membrane protein with lipid A 3-O-deacylase ...
 38-169 4.47e-37

Lipid A 3-O-deacylase (PagL); PagL is an outer membrane protein with lipid A 3-O-deacylase activity. It forms an 8 stranded beta barrel structure.


Pssm-ID: 462791  Cd Length: 129  Bit Score: 124.51  E-value: 4.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81539798    38 MTYRLG--LSWDWDKSWWQTSTGRLTGYWDAGYTYWeggdegagkHSLSFAPVFVYEFAGDSIKPFIEAGIGVAAFSGTR 115
Cdd:pfam09411   1 AYYGLSyqLFWDWGERWYNSPDWGLSLYWDAGYNAW---------LGLGVTPVFRFFFWSGKRGPYLEAGIGVAYLSRTN 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 81539798   116 VGDQNLGSSLNFEDRIGAGLKFANGQ-SVGVRAIHYSNAGLKQPNDGIESYSLFY 169
Cdd:pfam09411  72 FGDNDLGTRFQFRDQAGLGYRFGEGNlSLGLRFQHYSNAGIKDPNPGLNSLGLNL 126
 
Name Accession Description Interval E-value
PagL pfam09411
Lipid A 3-O-deacylase (PagL); PagL is an outer membrane protein with lipid A 3-O-deacylase ...
 38-169 4.47e-37

Lipid A 3-O-deacylase (PagL); PagL is an outer membrane protein with lipid A 3-O-deacylase activity. It forms an 8 stranded beta barrel structure.


Pssm-ID: 462791  Cd Length: 129  Bit Score: 124.51  E-value: 4.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81539798    38 MTYRLG--LSWDWDKSWWQTSTGRLTGYWDAGYTYWeggdegagkHSLSFAPVFVYEFAGDSIKPFIEAGIGVAAFSGTR 115
Cdd:pfam09411   1 AYYGLSyqLFWDWGERWYNSPDWGLSLYWDAGYNAW---------LGLGVTPVFRFFFWSGKRGPYLEAGIGVAYLSRTN 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 81539798   116 VGDQNLGSSLNFEDRIGAGLKFANGQ-SVGVRAIHYSNAGLKQPNDGIESYSLFY 169
Cdd:pfam09411  72 FGDNDLGTRFQFRDQAGLGYRFGEGNlSLGLRFQHYSNAGIKDPNPGLNSLGLNL 126
 
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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