Laccase-2 precursor - Botryotinia fuckeliana (Noble rot fungus)

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Reviewed, UniProtKB/Swiss-Prot Q96WM9 (LAC2_BOTFU)

Last modified June 16, 2009. Version 40. History...

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

Names and origin

Protein names

Recommended name:
    Laccase-2
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 2
    Urishiol oxidase 2
    Diphenol oxidase 2

Gene names

Name:

lcc2

Organism

Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Leotiomycetes › Helotiales › Sclerotiniaceae › Botryotinia

Protein attributes

Sequence length	581 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted Potential.
Induction	By resveratrol and tannins. Ref.1
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains.

Ontologies

Keywords
Biological process	Lignin degradation
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW laccase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

19

Potential

Chain

562

Laccase-2

PRO_0000267638

Regions

Domain

118

Plastocyanin-like 1

Domain

157

Plastocyanin-like 2

Domain

135

Plastocyanin-like 3

Sites

Metal binding

1

Copper 1; type 2 By similarity

Metal binding

1

Copper 2; type 3 By similarity

Metal binding

1

Copper 2; type 3 By similarity

Metal binding

1

Copper 3; type 3 By similarity

Metal binding

1

Copper 4; type 1 By similarity

Metal binding

1

Copper 1; type 2 By similarity

Metal binding

1

Copper 3; type 3 By similarity

Metal binding

1

Copper 3; type 3 By similarity

Metal binding

1

Copper 4; type 1 By similarity

Metal binding

1

Copper 2; type 3 By similarity

Metal binding

1

Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q96WM9-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 674947DAFD6BC757
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581

63,434

        10         20         30         40         50         60 
MKYSTVFTAL TALFAQASAT AIPAVRSPLA PRQSTTASCA NSATSRSCWG EYSIDTNWYD 

        70         80         90        100        110        120 
VTPNTGVTRE YWLSVENSTI TPDGYTRSAM TFNGTVPGPA ITADWGDNLI IHVTNNLQHN 

       130        140        150        160        170        180 
GTSIHWHGIR QLGSLEYDGV PGVTQCPIAP GDTLTYKFQA TQYGTTWYHS HFSLQYADGL 

       190        200        210        220        230        240 
FGPLIINGPA TADYDEDVGA IFLQDWAHKS VFEIWDSARQ GAPPALENTL MNGTNIYDCS 

       250        260        270        280        290        300 
ASTDANCVGG GKKFELTFVE GTKYRLRLIN VGIDSHFEFA IDNHTLTVIA NDLVPIVPYT 

       310        320        330        340        350        360 
TDTLLIGIGQ RYDVIVEANA AADNYWIRGN WGTTCSSNSE AANATGILRY DSSSTVDPTS 

       370        380        390        400        410        420 
VGVTPRGTCA DEPVASLVPH LALDVGGYSL VDEQVSFAFT NYFTWTINSS SLLLDWSSPT 

       430        440        450        460        470        480 
TLKIFNNETI FPTDYNVVAL NQTDANEEWV VYVIEDLTGF GIWHPIHLHG HDFYVVAQET 

       490        500        510        520        530        540 
DVFSATKSPA NFNLVNPPRR DVAALPGNGY LAIAFKLDNP GSWLLHCHIA WHASEGLAMQ 

       550        560        570        580 
FVESQSSIAI GMSDTDIFED TCANWNAYTP TELFAEDDSG I

References

[1]

"Resveratrol acts as a natural profungicide and induces self-intoxication by a specific laccase."
Schouten A., Wagemakers L., Stefanato F.L., van der Kaaij R.M., van Kan J.A.L.
Mol. Microbiol. 43:883-894(2002) [PubMed: 11929539] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: SAS56.

Cross-references

Sequence databases
	AF243855 Genomic DNA. Translation: AAK77953.1.
3D structure databases
HSSP	HSSP built from PDB template 1HFU based on UniProtKB Q9Y780.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.10.3.2. 290409.
Family and domain databases
InterPro	IPR001117. Cu-oxidase. IPR011706. Cu-oxidase_2. IPR011707. Cu-oxidase_3. IPR002355. Cu_oxidase_Cu_BS. IPR008972. Cupredoxin. [Graphical view]
Gene3D	G3DSA:2.60.40.420. Cupredoxin. 3 hits.
Pfam	PF00394. Cu-oxidase. 1 hit. PF07731. Cu-oxidase_2. 1 hit. PF07732. Cu-oxidase_3. 1 hit. [Graphical view]
PROSITE	PS00079. MULTICOPPER_OXIDASE1. 1 hit. PS00080. MULTICOPPER_OXIDASE2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LAC2_BOTFU

Accession

Primary (citable) accession number: Q96WM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (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