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Q99049 (LAC3_TRAVI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Laccase-3
EC=1.10.3.2
Alternative name(s):
Benzenediol:oxygen oxidoreductase 3
Diphenol oxidase 3
Urishiol oxidase 3
Gene names
Name:LCC3
OrganismTrametes villosa (White-rot fungus)
Taxonomic identifier47662 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Trametes

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Ontologies

Keywords
   Biological processLignin degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processlignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

hydroquinone:oxygen oxidoreductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 473452Laccase-3
PRO_0000002945

Regions

Domain23 – 148126Plastocyanin-like 1
Domain160 – 298139Plastocyanin-like 2
Domain365 – 44480Plastocyanin-like 3

Sites

Metal binding851Copper 1; type 2 By similarity
Metal binding871Copper 2; type 3 By similarity
Metal binding1301Copper 2; type 3 By similarity
Metal binding1321Copper 3; type 3 By similarity
Metal binding4101Copper 4; type 1 By similarity
Metal binding4131Copper 1; type 2 By similarity
Metal binding4151Copper 3; type 3 By similarity
Metal binding4261Copper 3; type 3 By similarity
Metal binding4271Copper 4; type 1 By similarity
Metal binding4281Copper 2; type 3 By similarity
Metal binding4321Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation3461N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation4701N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q99049 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B29FDE944DCCE547

FASTA47351,924
        10         20         30         40         50         60 
MSFSSLRRAL VFLGACSSAL ASIGPVTELD IVNKVIAPDG VARDTVLAGG TFPGPLITGK 

        70         80         90        100        110        120 
KGDNFRINVV DKLVNQTMLT STTIHWHGMF QHTTNWADGP AFVTQCPITT GDDFLYNFRV 

       130        140        150        160        170        180 
PDQTGTYWYH SHLALQYCDG LRGPLVIYDP HDPQAYLYDV DDESTVITLA DWYHTPAPLL 

       190        200        210        220        230        240 
PPAATLINGL GRWPGNPTAD LAVIEVQHGK RYRFRLVSTS CDPNYNFTID GHTMTIIEAD 

       250        260        270        280        290        300 
GQNTQPHQVD GLQIFAAQRY SFVLNANQAV NNYWIRANPN RANTTGFANG INSAILRYKG 

       310        320        330        340        350        360 
APIKEPTTNQ TTIRNFLWET DLHPLTDPRA PGLPFKGGVD HALNLNLTFN GSEFFINDAP 

       370        380        390        400        410        420 
FVPPTVPVLL QILNGTLDAN DLLPPGSVYN LPPDSTIELS IPGGVTGGPH PFHLHGTDNP 

       430        440        450        460        470 
GPWFLHCHID FHLQAGLAIV FAEDAQDTKL VNPVPEDWNK LCPTFDKAMN ITV

« Hide

References

[1]"Cloning and characterization of three laccase genes from the white-rot basidiomycete Trametes villosa: genomic organization of the laccase gene family."
Yaver D.S., Golightly E.J.
Gene 181:95-102(1996) [PubMed: 8973314] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L78076 Genomic DNA. Translation: AAB47733.1.

3D structure databases

ProteinModelPortalQ99049.
SMRQ99049. Positions 22-466.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 4 hits.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMSSF49503. Cupredoxin. 3 hits.
PROSITEPS00079. MULTICOPPER_OXIDASE1. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAC3_TRAVI
AccessionPrimary (citable) accession number: Q99049
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 16, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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