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Protein

Laccase-5

Gene

LCC5

Organism
Trametes versicolor (White-rot fungus) (Coriolus versicolor)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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 bindingi87 – 871Copper 1; type 2By similarity
Metal bindingi89 – 891Copper 2; type 3By similarity
Metal bindingi132 – 1321Copper 2; type 3By similarity
Metal bindingi134 – 1341Copper 3; type 3By similarity
Metal bindingi425 – 4251Copper 4; type 1By similarity
Metal bindingi428 – 4281Copper 1; type 2By similarity
Metal bindingi430 – 4301Copper 3; type 3By similarity
Metal bindingi480 – 4801Copper 3; type 3By similarity
Metal bindingi481 – 4811Copper 4; type 1By similarity
Metal bindingi482 – 4821Copper 2; type 3By similarity
Metal bindingi486 – 4861Copper 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-5 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 5
Diphenol oxidase 5
Laccase IV
Urishiol oxidase 5
Gene namesi
Name:LCC5
Synonyms:LCCIV
OrganismiTrametes versicolor (White-rot fungus) (Coriolus versicolor)
Taxonomic identifieri5325 [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 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 527504Laccase-5PRO_0000002942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi366 – 3661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi393 – 3931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ12717.
SMRiQ12717. Positions 24-526.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 150126Plastocyanin-like 1Add
BLAST
Domaini162 – 306145Plastocyanin-like 2Add
BLAST
Domaini373 – 498126Plastocyanin-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.

Q12717-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKFHSFVNV VALSLSLSGR VFGAIGPVTD LTISNADVTP DGITRAAVLA
60 70 80 90 100
GGVFPGPLIT GNKGDEFQIN VIDNLTNETM LKSTTIHWHG IFQAGTNWAD
110 120 130 140 150
GAAFVNQCPI ATGNSFLYDF TVPDQAGTFW YHSHLSTQYC DGLRGPLVVY
160 170 180 190 200
DPDDANASLY DVDDDTTVIT LADWYHTAAK LGPAFPAGPD SVLINGLGRF
210 220 230 240 250
SGDGGGATNL TVITVTQGKR YRFRLVSISC DPNFTFSIDG HNMTIIEVGG
260 270 280 290 300
VNHEALDVDS IQIFAGQRYS FILNANQSID NYWIRAIPNT GTTDTTGGVN
310 320 330 340 350
SAILRYDTAE EIEPTTNATT SVIPLTETDL VPLDNPAAPG DPQVGGVDLA
360 370 380 390 400
MSLDFSFNGS NFFINNETFV PPTVPVLLQI LSGAQDAASL LPNGSVYTLP
410 420 430 440 450
SNSTIEISFP IITTDGALNA PGAPHPFHLH GHTFSVVRSA GSSTFNYANP
460 470 480 490 500
VRRDTVSTGN SGDNVTIRFT TDNPGPWFLH CHIDFHLDAG FAIVFAEDTA
510 520
DTASANPVPT AWSDLCPTYD ALDSSDL
Length:527
Mass (Da):56,094
Last modified:November 1, 1996 - v1
Checksum:iD9597491F1F79825
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44431 mRNA. Translation: AAC49829.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44431 mRNA. Translation: AAC49829.1.

3D structure databases

ProteinModelPortaliQ12717.
SMRiQ12717. Positions 24-526.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
ProtoNetiSearch...

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.

Entry informationi

Entry nameiLAC5_TRAVE
AccessioniPrimary (citable) accession number: Q12717
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 76 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.