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Q9Y780

- Q9Y780_COPCI

UniProt

Q9Y780 - Q9Y780_COPCI

Protein
Submitted name:

Laccase 1

Gene

lcc1

Organism
Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi84 – 841Copper 1; via pros nitrogenImported
    Metal bindingi127 – 1271Copper 1; via tele nitrogenImported
    Metal bindingi129 – 1291Copper 2; via tele nitrogenImported
    Binding sitei175 – 1751Mannose; via carbonyl oxygenImported
    Metal bindingi414 – 4141Copper 3; via pros nitrogenImported
    Metal bindingi417 – 4171Copper 2; via tele nitrogenImported
    Metal bindingi419 – 4191Copper 2; via tele nitrogenImported
    Metal bindingi469 – 4691Copper 2; via tele nitrogenImported
    Sitei469 – 4691Important for catalytic activityImported
    Metal bindingi470 – 4701Copper 3Imported
    Sitei470 – 4701Important for catalytic activityImported
    Metal bindingi471 – 4711Copper 1; via tele nitrogenImported
    Sitei471 – 4711Important for catalytic activityImported
    Metal bindingi475 – 4751Copper 3; via pros nitrogenImported
    Binding sitei520 – 5201MannoseImported

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    OxidoreductaseSAAS annotationImported

    Keywords - Ligandi

    CopperSAAS annotationImported, Metal-bindingSAAS annotationImported

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Laccase 1Imported (EC:1.10.3.2Imported)
    Gene namesi
    Name:lcc1Imported
    OrganismiCoprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)Imported
    Taxonomic identifieri5346 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPsathyrellaceaeCoprinopsis

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi361 – 3611N-linked (GlcNAc...)

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A65X-ray2.23A19-522[»]
    1HFUX-ray1.68A20-521[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y780.

    Family & Domainsi

    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. 2 hits.
    PS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y780-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKNLLSFAL LAISVANAQI VNSVDTMTLT NANVSPDGFT RAGILVNGVH    50
    GPLIRGGKND NFELNVVNDL DNPTMLRPTS IHWHGLFQRG TNWADGADGV 100
    NQCPISPGHA FLYKFTPAGH AGTFWYHSHF GTQYCDGLRG PMVIYDDNDP 150
    HAALYDEDDE NTIITLADWY HIPAPSIQGA AQPDATLING KGRYVGGPAA 200
    ELSIVNVEQG KKYRMRLISL SCDPNWQFSI DGHELTIIEV DGQLTEPHTV 250
    DRLQIFTGQR YSFVLDANQP VDNYWIRAQP NKGRNGLAGT FANGVNSAIL 300
    RYAGAANADP TTSANPNPAQ LNEADLHALI DPAAPGIPTP GAADVNLRFQ 350
    LGFSGGRFTI NGTAYESPSV PTLLQIMSGA QSANDLLPAG SVYELPRNQV 400
    VELVVPAGVL GGPHPFHLHG HAFSVVRSAG SSTYNFVNPV KRDVVSLGVT 450
    GDEVTIRFVT DNPGPWFFHC HIEFHLMNGL AIVFAEDMAN TVDANNPPVE 500
    WAQLCEIYDD LPPEATSIQT VVRRAEPTGF SAKFRREGL 539
    Length:539
    Mass (Da):58,385
    Last modified:November 1, 1999 - v1
    Checksum:iFC45584BBE6142A9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF118267 Genomic DNA. Translation: AAD30964.1.
    AY338756 Genomic DNA. Translation: AAR01241.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF118267 Genomic DNA. Translation: AAD30964.1 .
    AY338756 Genomic DNA. Translation: AAR01241.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A65 X-ray 2.23 A 19-522 [» ]
    1HFU X-ray 1.68 A 20-521 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q9Y780.

    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. 2 hits.
    PS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution."
      Ducros V., Brzozowski A.M., Wilson K.S., Brown S.H., Ostergaard P., Schneider P., Yaver D.S., Pedersen A.H., Davies G.J.
      Nat. Struct. Biol. 5:310-316(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 19-522 IN COMPLEX WITH COPPER, ACTIVE SITE, GLYCOSYLATION AT ASN-361.
    2. "Molecular characterization of laccase genes from the basidiomycete Coprinus cinereus and heterologous expression of the laccase lcc1."
      Yaver D.S., Overjero M.D., Xu F., Nelson B.A., Brown K.M., Halkier T., Bernauer S., Brown S.H., Kauppinen S.
      Appl. Environ. Microbiol. 65:4943-4948(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: A3387Imported.
    3. "Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Cu-depleted' isoforms."
      Ducros V., Brzozowski A.M., Wilson K.S., Ostergaard P., Schneider P., Svendson A., Davies G.J.
      Acta Crystallogr. D 57:333-336(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 20-521 IN COMPLEX WITH COPPER AND MANNOSE.
    4. "The laccase gene family in Coprinopsis cinerea (Coprinus cinereus)."
      Hoegger P.J., Navarro-Gonzalez M., Kilaru S., Hoffmann M., Westbrook E.D., Kues U.
      Curr. Genet. 45:9-18(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: AT8Imported.

    Entry informationi

    Entry nameiQ9Y780_COPCI
    AccessioniPrimary (citable) accession number: Q9Y780
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 1, 1999
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3