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Protein

Laccase-2

Gene

LCC2

Organism
Thanatephorus cucumeris (Black scurf of potato) (Rhizoctonia solani)
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 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 bindingi497 – 4971Copper 4; type 1By similarity
Metal bindingi500 – 5001Copper 1; type 2By similarity
Metal bindingi502 – 5021Copper 3; type 3By similarity
Metal bindingi549 – 5491Copper 3; type 3By similarity
Metal bindingi550 – 5501Copper 4; type 1By similarity
Metal bindingi551 – 5511Copper 2; type 3By similarity
Metal bindingi555 – 5551Copper 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-2 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 2
Diphenol oxidase 2
Urishiol oxidase 2
Gene namesi
Name:LCC2
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 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 599580Laccase-2PRO_0000002936Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi443 – 4431N-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

ProteinModelPortaliQ02075.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 145125Plastocyanin-like 1Add
BLAST
Domaini157 – 307151Plastocyanin-like 2Add
BLAST
Domaini450 – 567118Plastocyanin-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.

Q02075-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARSTTSLFA LSLVASAFAR VVDYGFDVAN GAVAPDGVTR NAVLVNGRFP
60 70 80 90 100
GPLITANKGD TLKITVRNKL SDPTMRRSTT IHWHGLLQHR TAEEDGPAFV
110 120 130 140 150
TQCPIPPQES YTYTMPLGEQ TGTYWYHSHL SSQYVDGLRG PIVIYDPHDP
160 170 180 190 200
YRNYYDVDDE RTVFTLADWY HTPSEAIIAT HDVLKTIPDS GTINGKGKYD
210 220 230 240 250
PASANTNNTT LENLYTLKVK RGKRYRLRII NASAIASFRF GVQGHKCTII
260 270 280 290 300
EADGVLTKPI EVDAFDILAG QRYSCILKAD QDPDSYWINA PITNVLNTNV
310 320 330 340 350
QALLVYEDDK RPTHYPWKPF LTWKISNEII QYWQHKHGSH GHKGKGHHHK
360 370 380 390 400
VRAIGGVSGL SSRVKSRASD LSKKAVELAA ALVAGEAELD KRQNEDNSTI
410 420 430 440 450
VLDETKLIAL VQPGAPGGSR PADVVVPLDF GLNFANGLWT INNVSYSPPD
460 470 480 490 500
VPTLLKILTD KDKVDASDFT ADEHTYILPK NQVVELHIKG QALGIVHPLH
510 520 530 540 550
LHGHAFDVVQ FGDNAPNYVN PPRRDVVGVT DAGVRIQFRT DNPGPWFLHC
560 570 580 590
HIDWHLEEGF AMVFAEAPED IKKGSQSVKP DGQWKKLCEK YEKLPEALQ
Length:599
Mass (Da):66,540
Last modified:November 1, 1996 - v1
Checksum:iF01DD5C52D0CBB91
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54276 Genomic DNA. Translation: CAA91041.1.
PIRiS68118.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54276 Genomic DNA. Translation: CAA91041.1.
PIRiS68118.

3D structure databases

ProteinModelPortaliQ02075.
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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: R22 / IMI 358730 / AG-6.

Entry informationi

Entry nameiLAC2_THACU
AccessioniPrimary (citable) accession number: Q02075
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.