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Reviewed, UniProtKB/Swiss-Prot Q03966 (LAC1_CRYPA)

Last modified November 25, 2008. Version 54. 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
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase
    Urishiol oxidase
    Diphenol oxidase
Gene names
Name: LAC-1
OrganismCryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Taxonomic identifier5116 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeDiaporthalesCryphonectriaceaeCryphonectria-Endothia complexCryphonectria

Protein attributes

Sequence length591 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 By similarity.

Catalytic activity

4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O.

Cofactor

Binds 4 copper ions per monomer By similarity.

Subcellular location

SecretedPotential.

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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

laccase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 591571Laccase
PRO_0000002920

Regions

Domain66 – 189124Plastocyanin-like 1
Domain198 – 356159Plastocyanin-like 2
Domain416 – 551136Plastocyanin-like 3

Sites

Metal binding1261Copper 1; type 2 By similarity
Metal binding1281Copper 2; type 3 By similarity
Metal binding1711Copper 2; type 3 By similarity
Metal binding1731Copper 3; type 3 By similarity
Metal binding4631Copper 4; type 1 By similarity
Metal binding4661Copper 1; type 2 By similarity
Metal binding4681Copper 3; type 3 By similarity
Metal binding5331Copper 3; type 3 By similarity
Metal binding5341Copper 4; type 1 By similarity
Metal binding5351Copper 2; type 3 By similarity
Metal binding5391Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation4071N-linked (GlcNAc...) Potential
Glycosylation4251N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q03966-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B2F44CB2AAD77701

FASTA59164,696
        10         20         30         40         50         60 
MPSFFRALFS GLIASQLSWA APSLLHPLEP RQQPNCNTAS NRACWISGSY DITTDYEVKT 

        70         80         90        100        110        120 
PLTGVVRQYD LTLTQAENWL GPDGVVKEDV MLVNGNILGP VIHAQWGDTI SVTVTNNLKY 

       130        140        150        160        170        180 
NGTTIHWHGI RQLNTNLQDG VNGITECPIP PNGGSKTYTF IAHQYGTSWY HSHFSAQYGN 

       190        200        210        220        230        240 
GIVGAIQIDG PASLPYDIDL GPLVLSDYYY KTADELVVYT QSNAPPASDN VLFNGTNINP 

       250        260        270        280        290        300 
ANTTQGQYKT ITLTPGKRHR LRIINTSVEN NFQVSIVGHS MTVIESDFVP VDSFTTDSLF 

       310        320        330        340        350        360 
VGIGQRYDVT IDASQATDNY WMNVTFGGGG FCGKSNNPYP AAIIHYNGAS NSHPTNKGVA 

       370        380        390        400        410        420 
PADHECLDLL NLVPVVPRSI PTSGFVAASD NTLDVQLSTT TRKWTINGST LDVDWGHPIT 

       430        440        450        460        470        480 
QYVINKSTAW PSTDNVWLVE EANQWAYWLI ENDPTATGNA LPHPIHLHGH DFVVLGRSPN 

       490        500        510        520        530        540 
VSPTAQTPYT FTSSDVSSLN GNNPIRRDVV MLPPKGWLLI AFQTTNPGAW LMHCHIAWHV 

       550        560        570        580        590 
SAGLGNTFLE QPSAFVAGLN TNDVNQLNSQ CKSWNAYYPS KDIFKQDDSG V 

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References

[1]"Molecular analysis of the laccase gene from the chestnut blight fungus and selective suppression of its expression in an isogenic hypovirulent strain."
Choi G.H., Larson T.G., Nuss D.L.
Mol. Plant Microbe Interact. 5:119-128(1992) [PubMed: 1535523] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

M73257 Genomic DNA. Translation: AAA33105.1.
S38903 Genomic DNA. Translation: AAA09235.1.

3D structure databases

HSSPHSSP built from PDB template 1HFU based on UniProtKB Q9Y780.
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 nameLAC1_CRYPA
AccessionPrimary (citable) accession number: Q03966
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 25, 2008
This is version 54 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