Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Laccase-3

Gene

LCC3

Organism
Thanatephorus cucumeris (Black scurf of potato) (Rhizoctonia solani)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi82 – 821Copper 1; type 2By similarity
Metal bindingi84 – 841Copper 2; type 3By similarity
Metal bindingi127 – 1271Copper 2; type 3By similarity
Metal bindingi129 – 1291Copper 3; type 3By similarity
Metal bindingi470 – 4701Copper 4; type 1By similarity
Metal bindingi473 – 4731Copper 1; type 2By similarity
Metal bindingi475 – 4751Copper 3; type 3By similarity
Metal bindingi522 – 5221Copper 3; type 3By similarity
Metal bindingi523 – 5231Copper 4; type 1By similarity
Metal bindingi524 – 5241Copper 2; type 3By similarity
Metal bindingi528 – 5281Copper 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
OrganismiThanatephorus cucumeris (Black scurf of potato) (Rhizoctonia solani)
Taxonomic identifieri107832 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCantharellalesCeratobasidiaceaeThanatephorus

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 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 572554Laccase-3PRO_0000002937Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

In mycelia, at a lower level than LCC4.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ02079.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 145125Plastocyanin-like 1Add
BLAST
Domaini157 – 304148Plastocyanin-like 2Add
BLAST
Domaini422 – 540119Plastocyanin-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.

Q02079-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTTFLVSV SLFVSAVLAR TVEYNLKISN GKIAPDGVER DATLVNGGYP
60 70 80 90 100
GPLIFANKGD TLKVKVQNKL TNPDMYRTTS IHWHGLLQHR NADDDGPAFV
110 120 130 140 150
TQCPIVPQAS YTYTMPLGDQ TGTYWYHSHL SSQYVDGLRG PLVIYDPKDP
160 170 180 190 200
HRRLYDIDDE KTVLIIGDWY HTSSKAILAT GNITLQQPDS ATINGKGRFD
210 220 230 240 250
PDNTPANPNT LYTLKVKRGK RYRLRVINSS AIASFRMSIQ GHKMTVIAAD
260 270 280 290 300
GVSTKPYQVD SFDILAGQRI DAVVEANQEP DTYWINAPLT NVANKTAQAL
310 320 330 340 350
LIYEDDRRPY HPPKGPYRKW SVSEAIIKYW KHKHGRGLLS GHGGLKARMM
360 370 380 390 400
EGSLHLHGRR DIVKRQNETT TVVMDETKLV PLEHPGAACG SKPADLVIDL
410 420 430 440 450
TFGVNFTTGH WMINGIPHKS PDMPTLLKIL TDTDGVTESD FTQPEHTIIL
460 470 480 490 500
PKNKCVEFNI KGNSGLGIVH PIHLHGHTFD VVQFGNNPPN YVNPPRRDVV
510 520 530 540 550
GATDEGVRFQ FKTDNPGPWF LHCHIDWHLE EGFAMVFAEA PEAIKGGPKS
560 570
VPVDRQWKDL CRKYGSLPAG FL
Length:572
Mass (Da):63,747
Last modified:November 1, 1996 - v1
Checksum:iDF1E2AF9FF108CE4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti159 – 1591D → N.
Natural varianti359 – 3591R → H.
Natural varianti418 – 4181H → Y.
Natural varianti448 – 4481I → V.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54215 Genomic DNA. Translation: CAA90942.1.
PIRiS68119.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54215 Genomic DNA. Translation: CAA90942.1.
PIRiS68119.

3D structure databases

ProteinModelPortaliQ02079.
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. "The identification and characterization of four laccases from the plant pathogenic fungus Rhizoctonia solani."
    Wahleithner J.A., Xu F., Brown K.M., Brown S.H., Golightly E.J., Halkier T., Kauppinen S., Pederson A., Schneider P.
    Curr. Genet. 29:395-403(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: R22 / IMI 358730 / AG-6.

Entry informationi

Entry nameiLAC3_THACU
AccessioniPrimary (citable) accession number: Q02079
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 7, 2015
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

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.