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Reviewed, UniProtKB/Swiss-Prot Q12718 (LAC2_TRAVE)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    Laccase-2
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 2
    Urishiol oxidase 2
    Diphenol oxidase 2
    Laccase I
Gene names
Name: LCC2
Synonyms: LCCI
OrganismTrametes versicolor (White-rot fungus) (Coriolus versicolor)
Taxonomic identifier5325 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Trametes

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Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

Subcellular location

Secreted.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

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Ontologies

Keywords
   Biological processLignin degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical term3D-structure
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 519499Laccase-2
PRO_0000002940

Regions

Domain22 – 147126Plastocyanin-like 1
Domain159 – 301143Plastocyanin-like 2
Domain368 – 490123Plastocyanin-like 3

Sites

Metal binding841Copper 1; type 2
Metal binding861Copper 2; type 3
Metal binding1291Copper 2; type 3
Metal binding1311Copper 3; type 3
Metal binding4151Copper 4; type 1
Metal binding4181Copper 1; type 2
Metal binding4201Copper 3; type 3
Metal binding4721Copper 3; type 3
Metal binding4731Copper 4; type 1
Metal binding4741Copper 2; type 3
Metal binding4781Copper 4; type 1

Amino acid modifications

Glycosylation741N-linked (GlcNAc...)
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation2371N-linked (GlcNAc...)
Glycosylation2711N-linked (GlcNAc...)
Glycosylation3531N-linked (GlcNAc...)
Glycosylation3611N-linked (GlcNAc...)
Glycosylation4561N-linked (GlcNAc...)

Experimental info

Sequence conflict691D → V in AAC49828. Ref.1

Secondary structure

1 ................................................................................................... 519
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q12718-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BFFB5B4CD0007702

FASTA51955,811
        10         20         30         40         50         60 
MGLQRFSFFV TLALVARSLA AIGPVASLVV ANAPVSPDGF LRDAIVVNGV VPSPLITGKK 

        70         80         90        100        110        120 
GDRFQLNVDD TLTNHSMLKS TSIHWHGFFQ AGTNWADGPA FVNQCPIASG HSFLYDFHVP 

       130        140        150        160        170        180 
DQAGTFWYHS HLSTQYCDGL RGPFVVYDPK DPHASRYDVD NESTVITLTD WYHTAARLGP 

       190        200        210        220        230        240 
RFPLGADATL INGLGRSAST PTAALAVINV QHGKRYRFRL VSISCDPNYT FSIDGHNLTV 

       250        260        270        280        290        300 
IEVDGINSQP LLVDSIQIFA AQRYSFVLNA NQTVGNYWVR ANPNFGTVGF AGGINSAILR 

       310        320        330        340        350        360 
YQGAPVAEPT TTQTTSVIPL IETNLHPLAR MPVPGSPTPG GVDKALNLAF NFNGTNFFIN 

       370        380        390        400        410        420 
NATFTPPTVP VLLQILSGAQ TAQDLLPAGS VYPLPAHSTI EITLPATALA PGAPHPFHLH 

       430        440        450        460        470        480 
GHAFAVVRSA GSTTYNYNDP IFRDVVSTGT PAAGDNVTIR FQTDNPGPWF LHCHIDFHLD 

       490        500        510 
AGFAIVFAED VADVKAANPV PKAWSDLCPI YDGLSEANQ

« Hide

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References

[1]"Cloning and sequence analysis of two laccase complementary DNAs from the ligninolytic basidiomycete Trametes versicolor."
Ong E., Pollock W.B., Smith M.
Gene 196:113-119(1997) [PubMed: 9322748] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 20869 / PAP 52 / 52J.
[2]"Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers."
Piontek K., Antorini M., Choinowski T.
J. Biol. Chem. 277:37663-37669(2002) [PubMed: 12163489] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

U44851 Genomic DNA. Translation: AAA86659.1.
U44430 mRNA. Translation: AAC49828.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GYCX-ray1.90A21-519[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.10.3.2. 276061.

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...

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Entry information

Entry nameLAC2_TRAVE
AccessionPrimary (citable) accession number: Q12718
Secondary accession number(s): Q12716
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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