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Q96WM9

- LAC2_BOTFU

UniProt

Q96WM9 - LAC2_BOTFU

Protein

Laccase-2

Gene

lcc2

Organism
Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

    Cofactori

    Binds 4 copper ions per monomer.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi125 – 1251Copper 1; type 2By similarity
    Metal bindingi127 – 1271Copper 2; type 3By similarity
    Metal bindingi169 – 1691Copper 2; type 3By similarity
    Metal bindingi171 – 1711Copper 3; type 3By similarity
    Metal bindingi464 – 4641Copper 4; type 1By similarity
    Metal bindingi467 – 4671Copper 1; type 2By similarity
    Metal bindingi469 – 4691Copper 3; type 3By similarity
    Metal bindingi526 – 5261Copper 3; type 3By similarity
    Metal bindingi527 – 5271Copper 4; type 1By similarity
    Metal bindingi528 – 5281Copper 2; type 3By similarity
    Metal bindingi532 – 5321Copper 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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lignin degradation

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laccase-2 (EC:1.10.3.2)
    Alternative name(s):
    Benzenediol:oxygen oxidoreductase 2
    Diphenol oxidase 2
    Urishiol oxidase 2
    Gene namesi
    Name:lcc2
    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

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 581562Laccase-2PRO_0000267638Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi408 – 4081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi441 – 4411N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Inductioni

    By resveratrol and tannins.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ96WM9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini74 – 191118Plastocyanin-like 1Add
    BLAST
    Domaini197 – 353157Plastocyanin-like 2Add
    BLAST
    Domaini413 – 547135Plastocyanin-like 3Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat, Signal

    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: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q96WM9-1 [UniParc]FASTAAdd to Basket

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    MKYSTVFTAL TALFAQASAT AIPAVRSPLA PRQSTTASCA NSATSRSCWG    50
    EYSIDTNWYD VTPNTGVTRE YWLSVENSTI TPDGYTRSAM TFNGTVPGPA 100
    ITADWGDNLI IHVTNNLQHN GTSIHWHGIR QLGSLEYDGV PGVTQCPIAP 150
    GDTLTYKFQA TQYGTTWYHS HFSLQYADGL FGPLIINGPA TADYDEDVGA 200
    IFLQDWAHKS VFEIWDSARQ GAPPALENTL MNGTNIYDCS ASTDANCVGG 250
    GKKFELTFVE GTKYRLRLIN VGIDSHFEFA IDNHTLTVIA NDLVPIVPYT 300
    TDTLLIGIGQ RYDVIVEANA AADNYWIRGN WGTTCSSNSE AANATGILRY 350
    DSSSTVDPTS VGVTPRGTCA DEPVASLVPH LALDVGGYSL VDEQVSFAFT 400
    NYFTWTINSS SLLLDWSSPT TLKIFNNETI FPTDYNVVAL NQTDANEEWV 450
    VYVIEDLTGF GIWHPIHLHG HDFYVVAQET DVFSATKSPA NFNLVNPPRR 500
    DVAALPGNGY LAIAFKLDNP GSWLLHCHIA WHASEGLAMQ FVESQSSIAI 550
    GMSDTDIFED TCANWNAYTP TELFAEDDSG I 581
    Length:581
    Mass (Da):63,434
    Last modified:December 1, 2001 - v1
    Checksum:i674947DAFD6BC757
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF243855 Genomic DNA. Translation: AAK77953.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF243855 Genomic DNA. Translation: AAK77953.1 .

    3D structure databases

    ProteinModelPortali Q96WM9.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.40.420. 3 hits.
    InterProi IPR001117. Cu-oxidase.
    IPR011706. Cu-oxidase_2.
    IPR011707. Cu-oxidase_3.
    IPR002355. Cu_oxidase_Cu_BS.
    IPR008972. Cupredoxin.
    [Graphical view ]
    Pfami PF00394. Cu-oxidase. 1 hit.
    PF07731. Cu-oxidase_2. 1 hit.
    PF07732. Cu-oxidase_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49503. SSF49503. 3 hits.
    PROSITEi PS00079. MULTICOPPER_OXIDASE1. 1 hit.
    PS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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], INDUCTION.
      Strain: SAS56.

    Entry informationi

    Entry nameiLAC2_BOTFU
    AccessioniPrimary (citable) accession number: Q96WM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 63 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