Q99044 (LAC1_TRAVI) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 65.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Laccase-1 EC=1.10.3.2 Alternative name(s): Benzenediol:oxygen oxidoreductase 1 Diphenol oxidase 1 Urishiol oxidase 1 | ||
| Gene names |
| ||
| Organism | Trametes villosa (White-rot fungus) | ||
| Taxonomic identifier | 47662 [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 + O2 = 4 benzosemiquinone + 2 H2O. |
| Cofactor | Binds 4 copper ions per monomer By similarity. |
| Subunit structure | Homodimer. |
| 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 |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | copper ion binding Inferred from electronic annotation. Source: InterPro hydroquinone:oxygen oxidoreductase 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 – 21 | 21 | Potential | ||||||
| Chain | 22 – 520 | 499 | Laccase-1 | PRO_0000002943 | |||||
Regions | |||||||||
| Domain | 23 – 148 | 126 | Plastocyanin-like 1 | ||||||
| Domain | 160 – 302 | 143 | Plastocyanin-like 2 | ||||||
| Domain | 369 – 491 | 123 | Plastocyanin-like 3 | ||||||
Sites | |||||||||
| Metal binding | 85 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 87 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 130 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 132 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 416 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 419 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 421 | 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 | 72 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 75 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 229 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 238 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 354 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 361 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 457 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Purification, characterization, molecular cloning, and expression of two laccase genes from the white rot basidiomycete Trametes villosa." Yaver D.S., Xu F., Golightly E.J., Brown K.M., Brown S.H., Rey M.W., Schneider P., Halkier T., Mondorf K., Dalboge H. Appl. Environ. Microbiol. 62:834-841(1996) [PubMed: 8975613] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Mycelium. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L49376 Genomic DNA. Translation: AAC41686.1. |
3D structure databases | |
| ProteinModelPortal | Q99044. |
| SMR | Q99044. Positions 22-520. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | 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] |
| SUPFAM | SSF49503. Cupredoxin. 3 hits. |
| PROSITE | PS00079. MULTICOPPER_OXIDASE1. 1 hit. PS00080. MULTICOPPER_OXIDASE2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LAC1_TRAVI | ||||||||
| Accession | Primary (citable) accession number: Q99044 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with