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Protein

Laccase-5

Gene

LCC5

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)DescriptionActionsGraphical viewLength
Metal bindingi87Copper 1; type 2By similarity1
Metal bindingi89Copper 2; type 3By similarity1
Metal bindingi132Copper 2; type 3By similarity1
Metal bindingi134Copper 3; type 3By similarity1
Metal bindingi425Copper 4; type 1By similarity1
Metal bindingi428Copper 1; type 2By similarity1
Metal bindingi430Copper 3; type 3By similarity1
Metal bindingi480Copper 3; type 3By similarity1
Metal bindingi481Copper 4; type 1By similarity1
Metal bindingi482Copper 2; type 3By similarity1
Metal bindingi486Copper 4; type 1By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation

Keywords - Ligandi

Copper, Metal-binding

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Laccase-5 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 5
Diphenol oxidase 5
Urishiol oxidase 5
Gene namesi
Name:LCC5
OrganismiTrametes villosa (White-rot fungus)
Taxonomic identifieri47662 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesTrametes

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000000294724 – 527Laccase-5Add BLAST504

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi74N-linked (GlcNAc...)Sequence analysis1
Glycosylationi77N-linked (GlcNAc...)Sequence analysis1
Glycosylationi156N-linked (GlcNAc...)Sequence analysis1
Glycosylationi209N-linked (GlcNAc...)Sequence analysis1
Glycosylationi233N-linked (GlcNAc...)Sequence analysis1
Glycosylationi242N-linked (GlcNAc...)Sequence analysis1
Glycosylationi276N-linked (GlcNAc...)Sequence analysis1
Glycosylationi317N-linked (GlcNAc...)Sequence analysis1
Glycosylationi358N-linked (GlcNAc...)Sequence analysis1
Glycosylationi366N-linked (GlcNAc...)Sequence analysis1
Glycosylationi393N-linked (GlcNAc...)Sequence analysis1
Glycosylationi402N-linked (GlcNAc...)Sequence analysis1
Glycosylationi464N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ99056.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 150Plastocyanin-like 1Add BLAST126
Domaini162 – 306Plastocyanin-like 2Add BLAST145
Domaini373 – 498Plastocyanin-like 3Add BLAST126

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.
IPR033138. Cu_oxidase_CS.
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.

Q99056-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKYHSFVNV 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
DPDDPNASLY DVDDDTTVIT LADWYHTAAK LGPAFPAGPD SVLINGLGRF
210 220 230 240 250
SGDGGGATNL TVITVTQGKR YRFRLVSISC DPNFTFSIDG HNMTIIEVDG
260 270 280 290 300
VNHEALDVDS IQIFAGQRYS FILNANQSID NYWIRAIPNT GTTDTTGGVN
310 320 330 340 350
SAILRYDTAE DIEPTTNATT SVIPLTETDL VPLDNPAAPG DPQVGGVDLA
360 370 380 390 400
MSLDFSFNGS NFFINNETFV PPTVPVLLQI LSGAQDAASL LPNGSVYTLP
410 420 430 440 450
SNSTIEISFP IITTDGVLNA PGAPHPFHLH GHTFSVVRSA GSSTFNYANP
460 470 480 490 500
VRRDTVSTGN SGDNVTIRFT TDNPGPWFLH CHIDFHLEAG FAIVWGEDTA
510 520
DTASANPVPT AWSDLCPTYD ALDSSDL
Length:527
Mass (Da):56,247
Last modified:August 14, 2001 - v2
Checksum:iF1BE638D65FFA478
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L78078 Genomic DNA. Translation: AAB47735.2.
PIRiJC5357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L78078 Genomic DNA. Translation: AAB47735.2.
PIRiJC5357.

3D structure databases

ProteinModelPortaliQ99056.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

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.
IPR033138. Cu_oxidase_CS.
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...

Entry informationi

Entry nameiLAC5_TRAVI
AccessioniPrimary (citable) accession number: Q99056
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 14, 2001
Last modified: September 7, 2016
This is version 79 of the entry and version 2 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

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 one 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.