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Protein

Laccase-3

Gene

LCC3

Organism
Trametes villosa (White-rot fungus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Lignin degradation and detoxification of lignin-derived products.Curated

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 bindingi85 – 851Copper 1; type 2By similarity
Metal bindingi87 – 871Copper 2; type 3By similarity
Metal bindingi130 – 1301Copper 2; type 3By similarity
Metal bindingi132 – 1321Copper 3; type 3By similarity
Metal bindingi410 – 4101Copper 4; type 1By similarity
Metal bindingi413 – 4131Copper 1; type 2By similarity
Metal bindingi415 – 4151Copper 3; type 3By similarity
Metal bindingi426 – 4261Copper 3; type 3By similarity
Metal bindingi427 – 4271Copper 4; type 1By similarity
Metal bindingi428 – 4281Copper 2; type 3By similarity
Metal bindingi432 – 4321Copper 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
OrganismiTrametes villosa (White-rot fungus)
Taxonomic identifieri47662 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesTrametes

Subcellular locationi

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
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 473452Laccase-3PRO_0000002945Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi346 – 3461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ99049.
SMRiQ99049. Positions 22-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 148126Plastocyanin-like 1Add
BLAST
Domaini160 – 298139Plastocyanin-like 2Add
BLAST
Domaini365 – 44480Plastocyanin-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. 4 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.

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

Q99049-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFSSLRRAL VFLGACSSAL ASIGPVTELD IVNKVIAPDG VARDTVLAGG
60 70 80 90 100
TFPGPLITGK KGDNFRINVV DKLVNQTMLT STTIHWHGMF QHTTNWADGP
110 120 130 140 150
AFVTQCPITT GDDFLYNFRV PDQTGTYWYH SHLALQYCDG LRGPLVIYDP
160 170 180 190 200
HDPQAYLYDV DDESTVITLA DWYHTPAPLL PPAATLINGL GRWPGNPTAD
210 220 230 240 250
LAVIEVQHGK RYRFRLVSTS CDPNYNFTID GHTMTIIEAD GQNTQPHQVD
260 270 280 290 300
GLQIFAAQRY SFVLNANQAV NNYWIRANPN RANTTGFANG INSAILRYKG
310 320 330 340 350
APIKEPTTNQ TTIRNFLWET DLHPLTDPRA PGLPFKGGVD HALNLNLTFN
360 370 380 390 400
GSEFFINDAP FVPPTVPVLL QILNGTLDAN DLLPPGSVYN LPPDSTIELS
410 420 430 440 450
IPGGVTGGPH PFHLHGTDNP GPWFLHCHID FHLQAGLAIV FAEDAQDTKL
460 470
VNPVPEDWNK LCPTFDKAMN ITV
Length:473
Mass (Da):51,924
Last modified:November 1, 1996 - v1
Checksum:iB29FDE944DCCE547
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L78076 Genomic DNA. Translation: AAB47733.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L78076 Genomic DNA. Translation: AAB47733.1.

3D structure databases

ProteinModelPortaliQ99049.
SMRiQ99049. Positions 22-466.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.420. 4 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]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of three laccase genes from the white-rot basidiomycete Trametes villosa: genomic organization of the laccase gene family."
    Yaver D.S., Golightly E.J.
    Gene 181:95-102(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiLAC3_TRAVI
AccessioniPrimary (citable) accession number: Q99049
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 75 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.