Reviewed,
UniProtKB/Swiss-Prot Q03966 (LAC1_CRYPA)
Last modified
November 25, 2008.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Laccase EC=1.10.3.2 Alternative name(s): Benzenediol:oxygen oxidoreductase Urishiol oxidase Diphenol oxidase | ||
| Gene names |
| ||
| Organism | Cryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica) | ||
| Taxonomic identifier | 5116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Diaporthales › Cryphonectriaceae › Cryphonectria-Endothia complex › Cryphonectria |
Protein attributes
| Sequence length | 591 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Lignin degradation and detoxification of lignin-derived products By similarity. |
| Catalytic activity | 4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O. |
| Cofactor | Binds 4 copper ions per monomer By similarity. |
| Subcellular location | SecretedPotential. |
| Sequence similarities | Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains. |
Ontologies
Keywords | |
|---|---|
| Biological process | Lignin degradation |
| Cellular component | Secreted |
| Domain | Repeat Signal |
| Ligand | Copper Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | Glycoprotein |
Gene Ontology (GO) | |
| Biological process | lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | copper ion binding Inferred from electronic annotation. Source: InterPro laccase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 20 | 20 | Potential | ||||||
| Chain | 21 – 591 | 571 | Laccase | PRO_0000002920 | |||||
Regions | |||||||||
| Domain | 66 – 189 | 124 | Plastocyanin-like 1 | ||||||
| Domain | 198 – 356 | 159 | Plastocyanin-like 2 | ||||||
| Domain | 416 – 551 | 136 | Plastocyanin-like 3 | ||||||
Sites | |||||||||
| Metal binding | 126 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 128 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 171 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 173 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 463 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 466 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 468 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 533 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 534 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 535 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 539 | 1 | Copper 4; type 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 121 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 234 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 242 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 265 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 323 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 407 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 425 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Molecular analysis of the laccase gene from the chestnut blight fungus and selective suppression of its expression in an isogenic hypovirulent strain." Choi G.H., Larson T.G., Nuss D.L. Mol. Plant Microbe Interact. 5:119-128(1992) [PubMed: 1535523] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| M73257 Genomic DNA. Translation: AAA33105.1. S38903 Genomic DNA. Translation: AAA09235.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HFU based on UniProtKB Q9Y780. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR001117. Cu-oxidase. IPR011706. Cu-oxidase_2. IPR011707. Cu-oxidase_3. IPR002355. Cu_oxidase_Cu_BS. IPR008972. Cupredoxin. [Graphical view] |
| Gene3D | G3DSA:2.60.40.420. Cupredoxin. 3 hits. |
| Pfam | PF00394. Cu-oxidase. 1 hit. PF07731. Cu-oxidase_2. 1 hit. PF07732. Cu-oxidase_3. 1 hit. [Graphical view] |
| PROSITE | PS00079. MULTICOPPER_OXIDASE1. 1 hit. PS00080. MULTICOPPER_OXIDASE2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LAC1_CRYPA | ||||||||
| Accession | Primary (citable) accession number: Q03966 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


