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Conserved domains on  [gi|517731290|ref|WP_018901498|]
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MULTISPECIES: lipoprotein [Rhizobium/Agrobacterium group]

Protein Classification

lipoprotein( domain architecture ID 10613868)

lipoprotein similar to Pseudomonas aeruginosa lipopeptide LppL that contains a region that acts as an export signal

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LPAM_2 pfam13627
Prokaryotic lipoprotein-attachment site; In prokaryotes, membrane lipoproteins are synthesized ...
 13-34 6.70e-05

Prokaryotic lipoprotein-attachment site; In prokaryotes, membrane lipoproteins are synthesized with a precursor signal peptide, which is cleaved by a specific lipoprotein signal peptidase (signal peptidase II). The peptidase recognizes a conserved sequence and cuts upstream of a cysteine residue to which a glyceride-fatty acid lipid is attached.


:

Pssm-ID: 433360  Cd Length: 22  Bit Score: 35.43  E-value: 6.70e-05
                         10        20
                 ....*....|....*....|..
gi 517731290  13 VVFAVIGLAVAGCGRKGDLDPP 34
Cdd:pfam13627  1 LLLLALLLLLAGCGQKGPLYLP 22
 
Name Accession Description Interval E-value
LPAM_2 pfam13627
Prokaryotic lipoprotein-attachment site; In prokaryotes, membrane lipoproteins are synthesized ...
 13-34 6.70e-05

Prokaryotic lipoprotein-attachment site; In prokaryotes, membrane lipoproteins are synthesized with a precursor signal peptide, which is cleaved by a specific lipoprotein signal peptidase (signal peptidase II). The peptidase recognizes a conserved sequence and cuts upstream of a cysteine residue to which a glyceride-fatty acid lipid is attached.


Pssm-ID: 433360  Cd Length: 22  Bit Score: 35.43  E-value: 6.70e-05
                         10        20
                 ....*....|....*....|..
gi 517731290  13 VVFAVIGLAVAGCGRKGDLDPP 34
Cdd:pfam13627  1 LLLLALLLLLAGCGQKGPLYLP 22
YifL COG5567
Small periplasmic lipoprotein YifL (function unknown) [Function unknown];
9-54 5.86e-04

Small periplasmic lipoprotein YifL (function unknown) [Function unknown];


Pssm-ID: 444309  Cd Length: 43  Bit Score: 33.35  E-value: 5.86e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 517731290  9 IRLTVVFAVIGLAVAGCGRKGDLDPPsvqatkEGDSSKPTQQPGVK 54
Cdd:COG5567   4 LLRLLLLLLLLFTLAGCGLKGPLYLP------PAEKEKQPSQKQVE 43
 
Name Accession Description Interval E-value
LPAM_2 pfam13627
Prokaryotic lipoprotein-attachment site; In prokaryotes, membrane lipoproteins are synthesized ...
 13-34 6.70e-05

Prokaryotic lipoprotein-attachment site; In prokaryotes, membrane lipoproteins are synthesized with a precursor signal peptide, which is cleaved by a specific lipoprotein signal peptidase (signal peptidase II). The peptidase recognizes a conserved sequence and cuts upstream of a cysteine residue to which a glyceride-fatty acid lipid is attached.


Pssm-ID: 433360  Cd Length: 22  Bit Score: 35.43  E-value: 6.70e-05
                         10        20
                 ....*....|....*....|..
gi 517731290  13 VVFAVIGLAVAGCGRKGDLDPP 34
Cdd:pfam13627  1 LLLLALLLLLAGCGQKGPLYLP 22
YifL COG5567
Small periplasmic lipoprotein YifL (function unknown) [Function unknown];
9-54 5.86e-04

Small periplasmic lipoprotein YifL (function unknown) [Function unknown];


Pssm-ID: 444309  Cd Length: 43  Bit Score: 33.35  E-value: 5.86e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 517731290  9 IRLTVVFAVIGLAVAGCGRKGDLDPPsvqatkEGDSSKPTQQPGVK 54
Cdd:COG5567   4 LLRLLLLLLLLFTLAGCGLKGPLYLP------PAEKEKQPSQKQVE 43
 
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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