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Reviewed, UniProtKB/Swiss-Prot Q02079 (LAC3_THACU)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Laccase-3
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 3
    Urishiol oxidase 3
    Diphenol oxidase 3
Gene names
Name: LCC3
OrganismThanatephorus cucumeris (Black scurf of potato) (Rhizoctonia solani)
Taxonomic identifier107832 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaHomobasidiomycetesCantharellalesCeratobasidiaceaeThanatephorus

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Subunit structure

Homodimer By similarity.

Subcellular location

Secreted.

Tissue specificity

In mycelia, at a lower level than LCC4.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

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: UniProtKB-KW

laccase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 572554Laccase-3
PRO_0000002937

Regions

Domain21 – 145125Plastocyanin-like 1
Domain157 – 304148Plastocyanin-like 2
Domain422 – 540119Plastocyanin-like 3

Sites

Metal binding821Copper 1; type 2 By similarity
Metal binding841Copper 2; type 3 By similarity
Metal binding1271Copper 2; type 3 By similarity
Metal binding1291Copper 3; type 3 By similarity
Metal binding4701Copper 4; type 1 By similarity
Metal binding4731Copper 1; type 2 By similarity
Metal binding4751Copper 3; type 3 By similarity
Metal binding5221Copper 3; type 3 By similarity
Metal binding5231Copper 4; type 1 By similarity
Metal binding5241Copper 2; type 3 By similarity
Metal binding5281Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential
Glycosylation4051N-linked (GlcNAc...) Potential

Natural variations

Natural variant1591D → N
Natural variant3591R → H
Natural variant4181H → Y
Natural variant4481I → V

Sequences

Sequence LengthMass (Da)Tools
Q02079-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: DF1E2AF9FF108CE4

FASTA57263,747
        10         20         30         40         50         60 
MARTTFLVSV SLFVSAVLAR TVEYNLKISN GKIAPDGVER DATLVNGGYP GPLIFANKGD 

        70         80         90        100        110        120 
TLKVKVQNKL TNPDMYRTTS IHWHGLLQHR NADDDGPAFV TQCPIVPQAS YTYTMPLGDQ 

       130        140        150        160        170        180 
TGTYWYHSHL SSQYVDGLRG PLVIYDPKDP HRRLYDIDDE KTVLIIGDWY HTSSKAILAT 

       190        200        210        220        230        240 
GNITLQQPDS ATINGKGRFD PDNTPANPNT LYTLKVKRGK RYRLRVINSS AIASFRMSIQ 

       250        260        270        280        290        300 
GHKMTVIAAD GVSTKPYQVD SFDILAGQRI DAVVEANQEP DTYWINAPLT NVANKTAQAL 

       310        320        330        340        350        360 
LIYEDDRRPY HPPKGPYRKW SVSEAIIKYW KHKHGRGLLS GHGGLKARMM EGSLHLHGRR 

       370        380        390        400        410        420 
DIVKRQNETT TVVMDETKLV PLEHPGAACG SKPADLVIDL TFGVNFTTGH WMINGIPHKS 

       430        440        450        460        470        480 
PDMPTLLKIL TDTDGVTESD FTQPEHTIIL PKNKCVEFNI KGNSGLGIVH PIHLHGHTFD 

       490        500        510        520        530        540 
VVQFGNNPPN YVNPPRRDVV GATDEGVRFQ FKTDNPGPWF LHCHIDWHLE EGFAMVFAEA 

       550        560        570 
PEAIKGGPKS VPVDRQWKDL CRKYGSLPAG FL 

« Hide

References

[1]"The identification and characterization of four laccases from the plant pathogenic fungus Rhizoctonia solani."
Wahleithner J.A., Xu F., Brown K.M., Brown S.H., Golightly E.J., Halkier T., Kauppinen S., Pederson A., Schneider P.
Curr. Genet. 29:395-403(1996) [PubMed: 8598061] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RS22.

Cross-references

Sequence databases

Z54215 Genomic DNA. Translation: CAA90942.1.
PIRS68119.

3D structure databases

HSSPHSSP built from PDB template 1HFU based on UniProtKB Q9Y780.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.10.3.2. 81600.

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. 3 hits.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
PROSITEPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAC3_THACU
AccessionPrimary (citable) accession number: Q02079
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents