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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)DescriptionActionsGraphical viewLength
Metal bindingi82Copper 1; type 2By similarity1
Metal bindingi84Copper 2; type 3By similarity1
Metal bindingi127Copper 2; type 3By similarity1
Metal bindingi129Copper 3; type 3By similarity1
Metal bindingi470Copper 4; type 1By similarity1
Metal bindingi473Copper 1; type 2By similarity1
Metal bindingi475Copper 3; type 3By similarity1
Metal bindingi522Copper 3; type 3By similarity1
Metal bindingi523Copper 4; type 1By similarity1
Metal bindingi524Copper 2; type 3By similarity1
Metal bindingi528Copper 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-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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000293719 – 572Laccase-3Add BLAST554

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi182N-linked (GlcNAc...)Sequence analysis1
Glycosylationi228N-linked (GlcNAc...)Sequence analysis1
Glycosylationi294N-linked (GlcNAc...)Sequence analysis1
Glycosylationi367N-linked (GlcNAc...)Sequence analysis1
Glycosylationi405N-linked (GlcNAc...)Sequence analysis1

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)DescriptionActionsGraphical viewLength
Domaini21 – 145Plastocyanin-like 1Add BLAST125
Domaini157 – 304Plastocyanin-like 2Add BLAST148
Domaini422 – 540Plastocyanin-like 3Add BLAST119

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.

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)DescriptionActionsGraphical viewLength
Natural varianti159D → N.1
Natural varianti359R → H.1
Natural varianti418H → Y.1
Natural varianti448I → V.1

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...

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 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: September 7, 2016
This is version 82 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

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.