Q5B428 · X325_EMENI

Function

function

Lytic polysaccharide monooxygenase-like protein that has diverged to biological functions other than polysaccharide degradation since it does not perform oxidative cleavage of polysaccharides (PubMed:37452022).
Acts as a cell surface-bound protein that functions in the copper-accumulation pathway (By similarity).
May also act as the major cell wall sensor that regulates MAP kinase-dependent hyphal anastomosis, the fusion of hyphal cells (By similarity).

Cofactor

Cu2+ (UniProtKB | Rhea| CHEBI:29036 )

Note: Binds 1 copper ion per subunit.

Features

Showing features for binding site.

124420406080100120140160180200220240
TypeIDPosition(s)Description
Binding site24Cu2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Cellular Componentside of membrane
Molecular Functionmetal ion binding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Lytic polysaccharide monooxygenase-like protein ANIA_04702
  • Short names
    LPMO-like protein ANIA_04702
  • Alternative names
    • X325 family protein ANIA_04702

Gene names

    • ORF names
      ANIA_04702

Organism names

Accessions

  • Primary accession
    Q5B428
  • Secondary accessions
    • C8VAX4

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Lipid-anchor, GPI-anchor
Note: Proteins attached to a GPI anchor via their C terminus are found in the outer leaflet of the lipid bilayer facing the extracellular environment. GPI anchors can also be considered as predetermined breaking points, which allow the release of proteins into the extracellular environment upon enzymatic cleavage.

Keywords

PTM/Processing

Features

Showing features for signal, modified residue, chain, glycosylation, disulfide bond, lipidation, propeptide.

Type
IDPosition(s)Description
Signal1-23
Modified residue24Methylhistidine
ChainPRO_501029210424-215Lytic polysaccharide monooxygenase-like protein ANIA_04702
Glycosylation57N-linked (GlcNAc...) asparagine
Disulfide bond72↔177
Glycosylation80N-linked (GlcNAc...) asparagine
Glycosylation118N-linked (GlcNAc...) asparagine
Disulfide bond142↔196
Glycosylation159N-linked (GlcNAc...) asparagine
Glycosylation192N-linked (GlcNAc...) asparagine
Glycosylation198N-linked (GlcNAc...) asparagine
Lipidation215GPI-anchor amidated asparagine
PropeptidePRO_0000459758216-244Removed in mature form

Post-translational modification

The catalytically essential N-terminal histidine His-24 is post-translationally modified by methylation to prevent protonation of the histidine side chain, and protect the critical active site of the enzyme from oxidative damage.

Keywords

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the X325 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    244
  • Mass (Da)
    26,012
  • Last updated
    2005-04-26 v1
  • Checksum
    3275C46C9C0A2664
MLMSTSPSPWLAAAMLCIGLANAHTVIVYPGYRGNNLHTTGTVEGADGLGIAWSSDNETLIYPYGMQWSYPCGGMPTSENRTKWPVQGGAVSFQPGWFQGHSRAQIYINIGLGTVPPNMSHPMITPFEIVGPDNDPYPGTICLPQVRLPAGIEVQVGDNATIQVIELAQHGAALYNCADITFAEPEDVAEVNSTNCFNSSHISFETIFTTSSLENAGLEAVTVPSFLTAVVPTFLGIAYGLLMA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BN001303
EMBL· GenBank· DDBJ
CBF76965.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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