Reviewed,
UniProtKB/Swiss-Prot P56193 (LAC1_THACU)
Last modified
November 25, 2008.
Version 55.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Laccase-1 EC=1.10.3.2 Alternative name(s): Benzenediol:oxygen oxidoreductase 1 Urishiol oxidase 1 Diphenol oxidase 1 | ||
| Gene names |
| ||
| Organism | Thanatephorus cucumeris (Black scurf of potato) (Rhizoctonia solani) | ||
| Taxonomic identifier | 107832 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Cantharellales › Ceratobasidiaceae › Thanatephorus |
Protein attributes
| Sequence length | 576 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Lignin degradation and detoxification of lignin-derived products Probable. |
| Catalytic activity | 4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O. |
| Cofactor | Binds 4 copper ions per monomer By similarity. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Tissue specificity | In mycelia, at a lower level than LCC4. |
| Sequence similarities | Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains. |
| Biophysicochemical properties | pH dependence: Optimum pH is 6. |
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 – 19 | 19 | Potential | ||||||
| Chain | 20 – 576 | 557 | Laccase-1 | PRO_0000002935 | |||||
Regions | |||||||||
| Domain | 21 – 145 | 125 | Plastocyanin-like 1 | ||||||
| Domain | 157 – 304 | 148 | Plastocyanin-like 2 | ||||||
| Domain | 376 – 576 | 201 | Plastocyanin-like 3 | ||||||
Sites | |||||||||
| Metal binding | 82 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 84 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 127 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 129 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 471 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 474 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 476 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 523 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 524 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 525 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 529 | 1 | Copper 4; type 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 41 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 182 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 228 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 294 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 368 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "The identification and characterization of four laccases from the plant pathogenic fungus Rhizoctonia solani." Wahleithner J.A., Xu F., Brown K.M., Brown S.H., Golightly E.J., Halkier T., Kauppinen S., Pederson A., Schneider P. Curr. Genet. 29:395-403(1996) [PubMed: 8598061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: R22. |
Cross-references
Sequence databases | |
|---|---|
| Z54275 Genomic DNA. No translation available. | |
| PIR | S68117. |
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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LAC1_THACU | ||||||||
| Accession | Primary (citable) accession number: P56193 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


