Reviewed,
UniProtKB/Swiss-Prot Q12717 (LAC5_TRAVE)
Last modified
June 16, 2009.
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-5 EC=1.10.3.2 Alternative name(s): Benzenediol:oxygen oxidoreductase 5 Urishiol oxidase 5 Diphenol oxidase 5 Laccase IV | ||||
| Gene names |
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| 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 | 527 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
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. |
| 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-SubCell |
| Molecular function | copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 23 | 23 | Potential | ||||||
| Chain | 24 – 527 | 504 | Laccase-5 | PRO_0000002942 | |||||
Regions | |||||||||
| Domain | 25 – 150 | 126 | Plastocyanin-like 1 | ||||||
| Domain | 162 – 306 | 145 | Plastocyanin-like 2 | ||||||
| Domain | 373 – 498 | 126 | Plastocyanin-like 3 | ||||||
Sites | |||||||||
| Metal binding | 87 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 89 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 132 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 134 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 425 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 428 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 430 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 480 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 481 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 482 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 486 | 1 | Copper 4; type 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 74 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 77 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 156 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 209 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 233 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 242 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 276 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 317 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 358 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 366 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 393 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 402 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 464 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Cloning and sequence analysis of two laccase complementary DNAs from the ligninolytic basidiomycete Trametes versicolor." Ong E., Pollock W.B., Smith M. Gene 196:113-119(1997) [PubMed: 9322748] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 20869 / PAP 52 / 52J. |
Cross-references
Sequence databases | |
|---|---|
| U44431 mRNA. Translation: AAC49829.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1KYA based on UniProtKB Q96UT7. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.10.3.2. 276061. |
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 | LAC5_TRAVE | ||||||||
| Accession | Primary (citable) accession number: Q12717 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


