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Reviewed, UniProtKB/Swiss-Prot A2Y9C2 (LAC20_ORYSI)

Last modified October 13, 2009. Version 17. 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-20
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 20
    Urishiol oxidase 20
    Diphenol oxidase 20
Gene names
Name: LAC20
ORF Names: OsI_020915
OrganismOryza sativa subsp. indica (Rice)
Taxonomic identifier39946 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length580 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 By similarity.

Catalytic activity

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

Cofactor

Binds 4 copper ions per monomer By similarity.

Subcellular location

Secretedextracellular spaceapoplast Potential.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Ontologies

Keywords
   Biological processLignin degradation
   Cellular componentApoplast
Secreted
   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 componentapoplast

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 – 2323 Potential
Chain24 – 580557Laccase-20
PRO_0000291906

Regions

Domain31 – 147117Plastocyanin-like 1
Domain156 – 310155Plastocyanin-like 2
Domain419 – 561143Plastocyanin-like 3

Sites

Metal binding811Copper 1 By similarity
Metal binding831Copper 2 By similarity
Metal binding1261Copper 2 By similarity
Metal binding1281Copper 3 By similarity
Metal binding4781Copper 4 Potential
Metal binding4811Copper 1 By similarity
Metal binding4831Copper 3 By similarity
Metal binding5401Copper 3 By similarity
Metal binding5411Copper 4 Potential
Metal binding5421Copper 2 By similarity
Metal binding5461Copper 4 Potential
Metal binding5511Copper 4 Potential

Amino acid modifications

Glycosylation361N-linked (GlcNAc...) Potential
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation3391N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Glycosylation4601N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A2Y9C2-1 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 5482B2ED2D717F67

FASTA58064,907
        10         20         30         40         50         60 
MVASLLCTVA VAVLAVAAVG GEAGVVEHTF VVHEMNVTHL CNTTKIFVVN GQLPGPTVDV 

        70         80         90        100        110        120 
TEGDTVVVHV VNKIPHGLTI HWHGVRQLRS CWADGAGFIT ECPIPPGSER TYRFNVTDQV 

       130        140        150        160        170        180 
GTLWWHAHVT CLRSTINGAF IIRPRDGKYP FPTPVKDVPI IIGEWWELDL VELDRRMRDG 

       190        200        210        220        230        240 
NFDDNPLSAT INGKLGDLSN CSGIVEESFV LNVKHGESYL LRVINTAFFS EYYFKVAGHT 

       250        260        270        280        290        300 
FTVVGADGNY LTPFKTDMVT VAPGEAIDVL MVADAPPAHY HMIVLANQPP EPDPQIPEYI 

       310        320        330        340        350        360 
SRGLVRYTSA DANNNGLPVP MPIMPNQHNT MPSYYFHANL TGLMHPKHRR VPMHVDERIF 

       370        380        390        400        410        420 
IILGLGTICR GRKHTCKRQR SLETIELSTM NNVSFTHPYT TALLERYYDG TPEGVYTEDF 

       430        440        450        460        470        480 
PVRPPRPYNY TNPALIPPGP LEEVLEPTFK ATKLKRFKYN TSVEIIFQSS TLLMSDSNPM 

       490        500        510        520        530        540 
HLHGYDVFLL AQGLGSFNAK RDIRKFNYHN PQLRNTILVP RGGWAAVRFI TDNPGMWYLH 

       550        560        570        580 
CHFEFHIIMG MATAFIVEDG PTPETSLPPP PPEFKRCDAS 

« Hide

Cross-references

Sequence databases

CM000131 Genomic DNA. Translation: EAY99682.1.

3D structure databases

ModBaseSearch...

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAC20_ORYSI
AccessionPrimary (citable) accession number: A2Y9C2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: March 20, 2007
Last modified: October 13, 2009
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant 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