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Protein

Laccase-3

Gene

lcc3

Organism
Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Lignin degradation and detoxification of lignin-derived products.By similarity

Catalytic activityi

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

Cofactori

Cu cationBy similarityNote: Binds 4 Cu cations per monomer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi29 – 291Copper 1; type 2By similarity
Metal bindingi31 – 311Copper 2; type 3By similarity
Metal bindingi73 – 731Copper 2; type 3By similarity
Metal bindingi75 – 751Copper 3; type 3By similarity
Metal bindingi375 – 3751Copper 4; type 1By similarity
Metal bindingi378 – 3781Copper 1; type 2By similarity
Metal bindingi380 – 3801Copper 3; type 3By similarity
Metal bindingi437 – 4371Copper 3; type 3By similarity
Metal bindingi438 – 4381Copper 4; type 1By similarity
Metal bindingi439 – 4391Copper 2; type 3By similarity
Metal bindingi443 – 4431Copper 4; type 1By similarity

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. hydroquinone:oxygen oxidoreductase activity Source: UniProtKB-EC

GO - Biological processi

  1. lignin catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Laccase-3 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 3
Diphenol oxidase 3
Urishiol oxidase 3
Gene namesi
Name:lcc3
OrganismiBotryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)
Taxonomic identifieri40559 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeBotrytis

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›454›454Laccase-3PRO_0000267639Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ96UM2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini‹1 – 95›95Plastocyanin-like 1Add
BLAST
Domaini101 – 252152Plastocyanin-like 2Add
BLAST
Domaini319 – 454136Plastocyanin-like 3Add
BLAST

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q96UM2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
PGPTLYADWG DMIQVTLKNS MPDNGTGIHW HGLRQYHTCT EDGVPGITEC
60 70 80 90 100
PLAPGDTKTY TFQATQFGTS WYHSHYSSQY GEGMLGGIVI NGPATSNYDV
110 120 130 140 150
DLGVYTISDW YYTPVFALGE RIAHSQAGPP SGDNGLINGS MVAPAGQTGG
160 170 180 190 200
KYTTNTITAG KKYRLRLINT SVDNHFMVSL DNHAFTVITS DFVPIVPYTA
210 220 230 240 250
NWIFIGIGQR YDVIITANQT VGSYWFRAEV QNGCGTNNNN GNIKSIFTYS
260 270 280 290 300
GAASTTPSSS ATPYTGRCTD ETGIIPFWDS FVPSGPLSGN VEQLNVAINI
310 320 330 340 350
GVDASGPIVT WGINLSAIDV DWKKPILQYV LDGNNSWPAS ENLIELPNAA
360 370 380 390 400
QWYYWVIQEV PGNVNGNPVS INVPHPMHLH GHDFFLLGTG VGTYNNTING
410 420 430 440 450
PSLDYDNPTR RDVAMLPAGG WMVLAFQTDN PGAWLMHCHI AWHVSEGLAV

QFQG
Length:454
Mass (Da):49,323
Last modified:December 1, 2001 - v1
Checksum:iEB56A720394D912A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei454 – 4541

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY047482 Genomic DNA. Translation: AAL06114.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY047482 Genomic DNA. Translation: AAL06114.1.

3D structure databases

ProteinModelPortaliQ96UM2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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].
    Strain: SAS56.

Entry informationi

Entry nameiLAC3_BOTFU
AccessioniPrimary (citable) accession number: Q96UM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 1, 2001
Last modified: January 7, 2015
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.