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Q12570 (LAC1_BOTFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 70. 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-1
EC=1.10.3.2
Alternative name(s):
Benzenediol:oxygen oxidoreductase 1
Diphenol oxidase 1
Urishiol oxidase 1
Gene names
Name:lcc1
Synonyms:lac1
OrganismBotryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)
Taxonomic identifier40559 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Leotiomycetes › Helotiales › Sclerotiniaceae › Botryotinia

Protein attributes

Sequence length561 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

Secreted Potential.

Induction

Not induced by resveratrol or tannins. Ref.1

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Sequence caution

The sequence AAB41823.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence does probably not originate from mRNA or it was not properly spliced.

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 – 2020 Potential
Chain21 – 561541Laccase-1
PRO_0000085584

Regions

Domain68 – 185118Plastocyanin-like 1
Domain191 – 337147Plastocyanin-like 2
Domain396 – 525130Plastocyanin-like 3

Sites

Metal binding1191Copper 1; type 2 By similarity
Metal binding1211Copper 2; type 3 By similarity
Metal binding1631Copper 2; type 3 By similarity
Metal binding1651Copper 3; type 3 By similarity
Metal binding4451Copper 4; type 1 By similarity
Metal binding4481Copper 1; type 2 By similarity
Metal binding4501Copper 3; type 3 By similarity
Metal binding5041Copper 3; type 3 By similarity
Metal binding5051Copper 4; type 1 By similarity
Metal binding5061Copper 2; type 3 By similarity
Metal binding5101Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation2841N-linked (GlcNAc...) Potential
Glycosylation3271N-linked (GlcNAc...) Potential
Glycosylation3911N-linked (GlcNAc...) Potential
Glycosylation3981N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict117 – 1182SI → TM in AAB41823. Ref.2
Sequence conflict3721V → I in AAB41823. Ref.2
Sequence conflict4291N → K in AAB41823. Ref.2
Sequence conflict4811M → L in AAB41823. Ref.2
Sequence conflict4841P → S in AAB41823. Ref.2
Sequence conflict5111A → V in AAB41823. Ref.2
Sequence conflict5471A → G in AAB41823. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q12570 [UniParc].

Last modified December 12, 2006. Version 3.
Checksum: 7F366B289EF73C23

FASTA56160,337
        10         20         30         40         50         60 
MKNSFFSSLA KFASLSLAFA LPTAEVIPSA LEERQSCANT ATTRSCWGQY SASTNSYTTV 

        70         80         90        100        110        120 
PKTGYWLVVQ NTTLSADGVS RPTLNFNGTI PGPQITADWG DDVIVHVTNK LTSNGTSIHW 

       130        140        150        160        170        180 
HGIRQLNNAQ YDGVPGITQC PIAPGGTLTY KFHADNYGSS WYHSHFILQY GDGLFGPLVI 

       190        200        210        220        230        240 
NGPATANYDV DLGMLFLNDW NHVPVQSLWD KAKTGAPPTL LTGLMNGTNT YNGAGKKFQT 

       250        260        270        280        290        300 
TFTPGLKYRI RVVNTAVDGH FQFSIDGHSF QVIAMDFVPI VPYNATSILV SIAQRYDIIV 

       310        320        330        340        350        360 
TANAAVGNYW IRAGWQTACS GNTNAANITG ILRYTGSSST ADPTTTSTVT ASTSCLDEPL 

       370        380        390        400        410        420 
ASLVPFVPIN PVASSIMKTT LTTGGGQWLF NGSSLLLNWT DPTLLTVLNS GNIWPTEYNV 

       430        440        450        460        470        480 
IPIESTTANK GWAVLAISGP NGPNHPIHLH GHDFWTLSQG TGAYTATTAL NLVNPPRRDV 

       490        500        510        520        530        540 
MTLPTGGHLV IAFQIDNPGS WLMHCHIAWH ASEGLALQFV ESESSILPTI GTADVSTFQN 

       550        560 
TCAAWKAWTP TEPFPQDDSG I

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: SAS56.
[2]"A laccase cDNA from Botrytis cinerea."
Cantone F.A., Staples R.C.
Phytopathology 83:1383-1383(1993)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 115-561.
Strain: SAS56.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF243854 Genomic DNA. Translation: AAK77952.1.
U20192 mRNA. Translation: AAB41823.1. Sequence problems.

3D structure databases

ProteinModelPortalQ12570.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.420. 3 hits.
InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAC1_BOTFU
AccessionPrimary (citable) accession number: Q12570
Secondary accession number(s): Q96WN0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 12, 2006
Last modified: April 3, 2013
This is version 70 of the entry and version 3 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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