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Q02075 (LAC2_THACU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 68. 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-2
EC=1.10.3.2
Alternative name(s):
Benzenediol:oxygen oxidoreductase 2
Diphenol oxidase 2
Urishiol oxidase 2
Gene names
Name:LCC2
OrganismThanatephorus cucumeris (Black scurf of potato) (Rhizoctonia solani)
Taxonomic identifier107832 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Cantharellales › Ceratobasidiaceae › Thanatephorus

Protein attributes

Sequence length599 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
   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 – 1919 Potential
Chain20 – 599580Laccase-2
PRO_0000002936

Regions

Domain21 – 145125Plastocyanin-like 1
Domain157 – 307151Plastocyanin-like 2
Domain450 – 567118Plastocyanin-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 binding4971Copper 4; type 1 By similarity
Metal binding5001Copper 1; type 2 By similarity
Metal binding5021Copper 3; type 3 By similarity
Metal binding5491Copper 3; type 3 By similarity
Metal binding5501Copper 4; type 1 By similarity
Metal binding5511Copper 2; type 3 By similarity
Metal binding5551Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation3971N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q02075 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F01DD5C52D0CBB91

FASTA59966,540
        10         20         30         40         50         60 
MARSTTSLFA LSLVASAFAR VVDYGFDVAN GAVAPDGVTR NAVLVNGRFP GPLITANKGD 

        70         80         90        100        110        120 
TLKITVRNKL SDPTMRRSTT IHWHGLLQHR TAEEDGPAFV TQCPIPPQES YTYTMPLGEQ 

       130        140        150        160        170        180 
TGTYWYHSHL SSQYVDGLRG PIVIYDPHDP YRNYYDVDDE RTVFTLADWY HTPSEAIIAT 

       190        200        210        220        230        240 
HDVLKTIPDS GTINGKGKYD PASANTNNTT LENLYTLKVK RGKRYRLRII NASAIASFRF 

       250        260        270        280        290        300 
GVQGHKCTII EADGVLTKPI EVDAFDILAG QRYSCILKAD QDPDSYWINA PITNVLNTNV 

       310        320        330        340        350        360 
QALLVYEDDK RPTHYPWKPF LTWKISNEII QYWQHKHGSH GHKGKGHHHK VRAIGGVSGL 

       370        380        390        400        410        420 
SSRVKSRASD LSKKAVELAA ALVAGEAELD KRQNEDNSTI VLDETKLIAL VQPGAPGGSR 

       430        440        450        460        470        480 
PADVVVPLDF GLNFANGLWT INNVSYSPPD VPTLLKILTD KDKVDASDFT ADEHTYILPK 

       490        500        510        520        530        540 
NQVVELHIKG QALGIVHPLH LHGHAFDVVQ FGDNAPNYVN PPRRDVVGVT DAGVRIQFRT 

       550        560        570        580        590 
DNPGPWFLHC HIDWHLEEGF AMVFAEAPED IKKGSQSVKP DGQWKKLCEK YEKLPEALQ

« 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: R22.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z54276 Genomic DNA. Translation: CAA91041.1.
PIRS68118.

3D structure databases

ProteinModelPortalQ02075.
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. 3 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. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAC2_THACU
AccessionPrimary (citable) accession number: Q02075
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 16, 2011
This is version 68 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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