Reviewed,
UniProtKB/Swiss-Prot Q12719 (LAC4_TRAVE)
Last modified
November 25, 2008.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Laccase-4 EC=1.10.3.2 Alternative name(s): Benzenediol:oxygen oxidoreductase 4 Urishiol oxidase 4 Diphenol oxidase 4 | ||||
| Gene names |
| ||||
| Organism | Trametes versicolor (White-rot fungus) (Coriolus versicolor) | ||||
| Taxonomic identifier | 5325 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Trametes |
Protein attributes
| Sequence length | 520 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 Probable. |
| Catalytic activity | 4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O. |
| Cofactor | Binds 4 copper ions per monomer By similarity. |
| Subcellular location | |
| 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 – 22 | 22 | Potential | ||||||||
| Chain | 23 – 520 | 498 | Laccase-4 | PRO_0000002941 | |||||||
Regions | |||||||||||
| Domain | 24 – 149 | 126 | Plastocyanin-like 1 | ||||||||
| Domain | 161 – 303 | 143 | Plastocyanin-like 2 | ||||||||
| Domain | 370 – 491 | 122 | Plastocyanin-like 3 | ||||||||
Sites | |||||||||||
| Metal binding | 86 | 1 | Copper 1; type 2 By similarity | ||||||||
| Metal binding | 88 | 1 | Copper 2; type 3 By similarity | ||||||||
| Metal binding | 131 | 1 | Copper 2; type 3 By similarity | ||||||||
| Metal binding | 133 | 1 | Copper 3; type 3 By similarity | ||||||||
| Metal binding | 418 | 1 | Copper 4; type 1 By similarity | ||||||||
| Metal binding | 421 | 1 | Copper 1; type 2 By similarity | ||||||||
| Metal binding | 423 | 1 | Copper 3; type 3 By similarity | ||||||||
| Metal binding | 473 | 1 | Copper 3; type 3 By similarity | ||||||||
| Metal binding | 474 | 1 | Copper 4; type 1 By similarity | ||||||||
| Metal binding | 475 | 1 | Copper 2; type 3 By similarity | ||||||||
| Metal binding | 479 | 1 | Copper 4; type 1 By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 73 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 76 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 239 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 399 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 457 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 497 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 107 ↔ 509 | Probable | |||||||||
| Disulfide bond | 139 ↔ 227 | Probable | |||||||||
Sequences
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References
| [1] | "Characterization of a laccase gene from the white-rot fungus Trametes versicolor and structural features of basidiomycete laccases." Joensson L.J., Sjoestroem K., Haeggstroem I., Nyman P.O. Biochim. Biophys. Acta 1251:210-215(1995) [PubMed: 7669813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PRL 572. |
Cross-references
Sequence databases | |
|---|---|
| X84683 Genomic DNA. Translation: CAA59161.1. | |
| PIR | S59533. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1KYA based on UniProtKB Q96UT7. |
| SMR | Q12719. Positions 23-519. |
| 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 | LAC4_TRAVE | ||||||||
| Accession | Primary (citable) accession number: Q12719 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


