Reviewed,
UniProtKB/Swiss-Prot A2XCN6 (LAC18_ORYSI)
Last modified
June 16, 2009.
Version 15.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative laccase-18 EC=1.10.3.2 Alternative name(s): Benzenediol:oxygen oxidoreductase 18 Urishiol oxidase 18 Diphenol oxidase 18 | ||||
| Gene names |
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| Organism | Oryza sativa subsp. indica (Rice) | ||||
| Taxonomic identifier | 39946 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza |
Protein attributes
| Sequence length | 595 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 + O2 = 4 benzosemiquinone + 2 H2O. |
| Cofactor | Binds 4 copper ions per monomer By similarity. |
| Subcellular location | Secreted › extracellular space › apoplast Potential. |
| Sequence similarities | Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lignin degradation |
| Cellular component | Apoplast 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 | apoplast Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular spaceInferred 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 – 29 | 29 | Potential | ||||||
| Chain | 30 – 595 | 566 | Putative laccase-18 | PRO_0000291902 | |||||
Regions | |||||||||
| Domain | 37 – 153 | 117 | Plastocyanin-like 1 | ||||||
| Domain | 162 – 316 | 155 | Plastocyanin-like 2 | ||||||
| Domain | 429 – 571 | 143 | Plastocyanin-like 3 | ||||||
Sites | |||||||||
| Metal binding | 87 | 1 | Copper 1 By similarity | ||||||
| Metal binding | 89 | 1 | Copper 2 By similarity | ||||||
| Metal binding | 132 | 1 | Copper 2 By similarity | ||||||
| Metal binding | 134 | 1 | Copper 3 By similarity | ||||||
| Metal binding | 488 | 1 | Copper 4 Potential | ||||||
| Metal binding | 491 | 1 | Copper 1 By similarity | ||||||
| Metal binding | 493 | 1 | Copper 3 By similarity | ||||||
| Metal binding | 550 | 1 | Copper 3 By similarity | ||||||
| Metal binding | 551 | 1 | Copper 4 Potential | ||||||
| Metal binding | 552 | 1 | Copper 2 By similarity | ||||||
| Metal binding | 556 | 1 | Copper 4 Potential | ||||||
| Metal binding | 561 | 1 | Copper 4 Potential | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 42 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 48 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 121 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 206 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 345 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 382 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 402 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 409 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 439 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 470 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. Yang H.PLoS Biol. 3:266-281(2005) [PubMed: 15685292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. 93-11. |
Cross-references
Sequence databases | |
|---|---|
| CM000128 Genomic DNA. Translation: EAY88596.1. | |
3D structure databases | |
| 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 | LAC18_ORYSI | ||||||||
| Accession | Primary (citable) accession number: A2XCN6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


