Q5B428 · X325_EMENI
- ProteinLytic polysaccharide monooxygenase-like protein ANIA_04702
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids244 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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
Note: Binds 1 copper ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 24 | Cu2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
Molecular Function | metal ion binding |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameLytic polysaccharide monooxygenase-like protein ANIA_04702
- Short namesLPMO-like protein ANIA_04702
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionQ5B428
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
PTM/Processing
Features
Showing features for signal, modified residue, chain, glycosylation, disulfide bond, lipidation, propeptide.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-23 | ||||
Modified residue | 24 | Methylhistidine | |||
Chain | PRO_5010292104 | 24-215 | Lytic polysaccharide monooxygenase-like protein ANIA_04702 | ||
Glycosylation | 57 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 72↔177 | ||||
Glycosylation | 80 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 118 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 142↔196 | ||||
Glycosylation | 159 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 192 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 198 | N-linked (GlcNAc...) asparagine | |||
Lipidation | 215 | GPI-anchor amidated asparagine | |||
Propeptide | PRO_0000459758 | 216-244 | Removed 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
- PTM
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length244
- Mass (Da)26,012
- Last updated2005-04-26 v1
- Checksum3275C46C9C0A2664
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BN001303 EMBL· GenBank· DDBJ | CBF76965.1 EMBL· GenBank· DDBJ | Genomic DNA |