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P78722

- LAC2_PODAS

UniProt

P78722 - LAC2_PODAS

Protein

Laccase-2

Gene

LAC2

Organism
Podospora anserina (Pleurage anserina)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Probably involved in lignin degradation and in the detoxification of lignin-derived products in its natural habitat (herbivorous dung), which is rich in lignin of grasses and straw. Probably involved in melanin synthesis and in perithecia development.

    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 bindingi138 – 1381Copper 1; type 2By similarity
    Metal bindingi140 – 1401Copper 2; type 3By similarity
    Metal bindingi183 – 1831Copper 2; type 3By similarity
    Metal bindingi185 – 1851Copper 3; type 3By similarity
    Metal bindingi476 – 4761Copper 4; type 1By similarity
    Metal bindingi479 – 4791Copper 1; type 2By similarity
    Metal bindingi481 – 4811Copper 3; type 3By similarity
    Metal bindingi548 – 5481Copper 3; type 3By similarity
    Metal bindingi549 – 5491Copper 4; type 1By similarity
    Metal bindingi550 – 5501Copper 2; type 3By similarity
    Metal bindingi554 – 5541Copper 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
    2. melanin biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lignin degradation, Melanin biosynthesis

    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
    Laccase C
    Laccase II
    Urishiol oxidase 2
    Gene namesi
    Name:LAC2
    OrganismiPodospora anserina (Pleurage anserina)
    Taxonomic identifieri5145 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora

    Subcellular locationi

    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 – 2323Sequence AnalysisAdd
    BLAST
    Propeptidei24 – 4825Sequence AnalysisPRO_0000002931Add
    BLAST
    Chaini49 – 605557Laccase-2PRO_0000002932Add
    BLAST
    Propeptidei606 – 62116Sequence AnalysisPRO_0000002933Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi261 – 2611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi441 – 4411N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Proteolytically processed at both its N-terminus and its C-terminus.

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Developmental stagei

    Low basic levels throughout the growth phase; increases at least 20-fold at the beginning of the autolytic phase and decreases again thereafter.

    Inductioni

    Under oxidative stress on the mycelium by aromatic xenobiotics (guaiacol, hydroquinone, benzoquinone), and by copper salt at a concentration of 1 mM (growing mycelium).

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP78722.
    SMRiP78722. Positions 46-605.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini78 – 201124Plastocyanin-like 1Add
    BLAST
    Domaini210 – 367158Plastocyanin-like 2Add
    BLAST
    Domaini430 – 566137Plastocyanin-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.

    P78722-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMKSFFSAAA LLLGLVAPSA VLAAPSLPGV PREVTRDLLR PVEERQSSCH    50
    TAANRACWAP GFDINTDYEV STPNTGVTRT YTLTLTEVDN WLGPDGVVKQ 100
    KVMLVNGDIF GPTITANWGD WIQVNVINNL RTNGTSIHWH GLHQKGTNMH 150
    DGANGVTECP IPPKGGSRIY RFRAQQYGTS WYHSHFSAQY GNGVVGTIVV 200
    NGPASVPYDI DLGVFPITDY YHKPADVLVE ETMNGGPPPS DTVLFKGHGK 250
    NPQTGAGKFA NVTLTPGKRH RLRIINTSTH DHFQLKLQNH TMTIIAADMV 300
    PVQAQTVDSL FLAVGQRYDV TIDANKSVGN YWFNATFGGG LACGASLNPH 350
    PAAVFRYQGA PNTLPTNIGT PAADANCMDL NNLTPVVSRS VPTSGFTPRP 400
    NNTLPVSLTL GGTPLFVWKV NGSSINVDWD KPIVDYVIAQ NTSYPPQANV 450
    ITVNSVNQWT YWLIENDPTG PFSIPHPMHL HGHDFLVVGR SPDQPAGVPQ 500
    TRYRFNPATD MALLKSSNPV RRDVAMLPAN GWLLIAFKSD NPGAWLFHCH 550
    IAWHVSGGLS VQYLERPNDL RNGFSQADKN QHNNNCNAWR AYWPTNPFPK 600
    IDSGLKVKKW VGEHPDWYIK N 621
    Length:621
    Mass (Da):68,129
    Last modified:May 1, 1997 - v1
    Checksum:i79F85E2ED25C1CA7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08827 Genomic DNA. Translation: CAA70061.1.
    PIRiS72493.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08827 Genomic DNA. Translation: CAA70061.1 .
    PIRi S72493.

    3D structure databases

    ProteinModelPortali P78722.
    SMRi P78722. Positions 46-605.
    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. "Isolation and characterization of a laccase gene from Podospora anserina."
      Fernandez-Larrea J., Stahl U.
      Mol. Gen. Genet. 252:539-551(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 26003.

    Entry informationi

    Entry nameiLAC2_PODAS
    AccessioniPrimary (citable) accession number: P78722
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Podospora anserina contains at least 3 laccase isozymes named I, II, and III. They differ in their substrate specificity, number of subunits, isoelectronic point and heat stability.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3