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Q12718

- LAC2_TRAVE

UniProt

Q12718 - LAC2_TRAVE

Protein

Laccase-2

Gene

LCC2

Organism
Trametes versicolor (White-rot fungus) (Coriolus versicolor)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Lignin degradation and detoxification of lignin-derived products.Curated

    Catalytic activityi

    4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

    Cofactori

    Binds 4 copper ions per monomer.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi84 – 841Copper 1; type 2
    Metal bindingi86 – 861Copper 2; type 3
    Metal bindingi129 – 1291Copper 2; type 3
    Metal bindingi131 – 1311Copper 3; type 3
    Metal bindingi415 – 4151Copper 4; type 1
    Metal bindingi418 – 4181Copper 1; type 2
    Metal bindingi420 – 4201Copper 3; type 3
    Metal bindingi472 – 4721Copper 3; type 3
    Metal bindingi473 – 4731Copper 4; type 1
    Metal bindingi474 – 4741Copper 2; type 3
    Metal bindingi478 – 4781Copper 4; type 1

    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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17211.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laccase-2 (EC:1.10.3.2)
    Alternative name(s):
    Benzenediol:oxygen oxidoreductase 2
    Diphenol oxidase 2
    Laccase I
    Urishiol oxidase 2
    Gene namesi
    Name:LCC2
    Synonyms:LCCI
    OrganismiTrametes versicolor (White-rot fungus) (Coriolus versicolor)
    Taxonomic identifieri5325 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesTrametes

    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 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 519499Laccase-2PRO_0000002940Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi74 – 741N-linked (GlcNAc...)
    Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi237 – 2371N-linked (GlcNAc...)
    Glycosylationi271 – 2711N-linked (GlcNAc...)
    Glycosylationi353 – 3531N-linked (GlcNAc...)
    Glycosylationi361 – 3611N-linked (GlcNAc...)
    Glycosylationi456 – 4561N-linked (GlcNAc...)

    Keywords - PTMi

    Glycoprotein

    Structurei

    Secondary structure

    1
    519
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 3512
    Beta strandi42 – 476
    Beta strandi50 – 523
    Beta strandi56 – 594
    Beta strandi63 – 708
    Helixi75 – 773
    Beta strandi83 – 864
    Helixi94 – 963
    Turni100 – 1023
    Beta strandi111 – 1188
    Beta strandi124 – 1307
    Helixi135 – 1384
    Beta strandi141 – 1477
    Helixi154 – 1563
    Helixi162 – 1643
    Beta strandi165 – 1717
    Turni176 – 1783
    Beta strandi187 – 1915
    Beta strandi207 – 2104
    Beta strandi215 – 2228
    Beta strandi229 – 2335
    Beta strandi238 – 2436
    Beta strandi246 – 25813
    Beta strandi263 – 2697
    Beta strandi274 – 28714
    Helixi291 – 2933
    Beta strandi296 – 3016
    Beta strandi317 – 3193
    Helixi322 – 3243
    Beta strandi327 – 3293
    Beta strandi342 – 3476
    Beta strandi350 – 3523
    Beta strandi357 – 3593
    Helixi371 – 3766
    Turni382 – 3843
    Beta strandi385 – 3873
    Beta strandi390 – 3945
    Beta strandi399 – 4057
    Beta strandi416 – 4194
    Beta strandi424 – 4285
    Beta strandi437 – 4393
    Beta strandi442 – 4476
    Helixi451 – 4533
    Beta strandi456 – 4627
    Beta strandi467 – 4759
    Helixi476 – 4805
    Beta strandi484 – 4896
    Helixi491 – 4933
    Helixi494 – 4974
    Helixi502 – 51211
    Helixi516 – 5183

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GYCX-ray1.90A21-519[»]
    ProteinModelPortaliQ12718.
    SMRiQ12718. Positions 21-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12718.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 147126Plastocyanin-like 1Add
    BLAST
    Domaini159 – 301143Plastocyanin-like 2Add
    BLAST
    Domaini368 – 490123Plastocyanin-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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q12718-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLQRFSFFV TLALVARSLA AIGPVASLVV ANAPVSPDGF LRDAIVVNGV    50
    VPSPLITGKK GDRFQLNVDD TLTNHSMLKS TSIHWHGFFQ AGTNWADGPA 100
    FVNQCPIASG HSFLYDFHVP DQAGTFWYHS HLSTQYCDGL RGPFVVYDPK 150
    DPHASRYDVD NESTVITLTD WYHTAARLGP RFPLGADATL INGLGRSAST 200
    PTAALAVINV QHGKRYRFRL VSISCDPNYT FSIDGHNLTV IEVDGINSQP 250
    LLVDSIQIFA AQRYSFVLNA NQTVGNYWVR ANPNFGTVGF AGGINSAILR 300
    YQGAPVAEPT TTQTTSVIPL IETNLHPLAR MPVPGSPTPG GVDKALNLAF 350
    NFNGTNFFIN NATFTPPTVP VLLQILSGAQ TAQDLLPAGS VYPLPAHSTI 400
    EITLPATALA PGAPHPFHLH GHAFAVVRSA GSTTYNYNDP IFRDVVSTGT 450
    PAAGDNVTIR FQTDNPGPWF LHCHIDFHLD AGFAIVFAED VADVKAANPV 500
    PKAWSDLCPI YDGLSEANQ 519
    Length:519
    Mass (Da):55,811
    Last modified:November 1, 1996 - v1
    Checksum:iBFFB5B4CD0007702
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691D → V in AAC49828. (PubMed:9322748)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U44851 Genomic DNA. Translation: AAA86659.1.
    U44430 mRNA. Translation: AAC49828.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U44851 Genomic DNA. Translation: AAA86659.1 .
    U44430 mRNA. Translation: AAC49828.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GYC X-ray 1.90 A 21-519 [» ]
    ProteinModelPortali Q12718.
    SMRi Q12718. Positions 21-519.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-17211.

    Miscellaneous databases

    EvolutionaryTracei Q12718.

    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of two laccase complementary DNAs from the ligninolytic basidiomycete Trametes versicolor."
      Ong E., Pollock W.B., Smith M.
      Gene 196:113-119(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ATCC 20869 / PAP 52 / 52J.
    2. "Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers."
      Piontek K., Antorini M., Choinowski T.
      J. Biol. Chem. 277:37663-37669(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

    Entry informationi

    Entry nameiLAC2_TRAVE
    AccessioniPrimary (citable) accession number: Q12718
    Secondary accession number(s): Q12716
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 80 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3