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Protein

Laccase-3

Gene

lcc3

Organism
Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Lignin degradation and detoxification of lignin-derived products.By similarity

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 bindingi29Copper 1; type 2By similarity1
Metal bindingi31Copper 2; type 3By similarity1
Metal bindingi73Copper 2; type 3By similarity1
Metal bindingi75Copper 3; type 3By similarity1
Metal bindingi375Copper 4; type 1By similarity1
Metal bindingi378Copper 1; type 2By similarity1
Metal bindingi380Copper 3; type 3By similarity1
Metal bindingi437Copper 3; type 3By similarity1
Metal bindingi438Copper 4; type 1By similarity1
Metal bindingi439Copper 2; type 3By similarity1
Metal bindingi443Copper 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
OrganismiBotryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)
Taxonomic identifieri40559 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeBotrytis

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000267639‹1 – ›454Laccase-3Add BLAST›454

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi24N-linked (GlcNAc...)Sequence analysis1
Glycosylationi138N-linked (GlcNAc...)Sequence analysis1
Glycosylationi169N-linked (GlcNAc...)Sequence analysis1
Glycosylationi218N-linked (GlcNAc...)Sequence analysis1
Glycosylationi314N-linked (GlcNAc...)Sequence analysis1
Glycosylationi334N-linked (GlcNAc...)Sequence analysis1
Glycosylationi395N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi40559.EDN31422.

Structurei

3D structure databases

ProteinModelPortaliQ96UM2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini‹1 – 95Plastocyanin-like 1Add BLAST›95
Domaini101 – 252Plastocyanin-like 2Add BLAST152
Domaini319 – 454Plastocyanin-like 3Add BLAST136

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1263. Eukaryota.
COG2132. LUCA.

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.
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.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q96UM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
PGPTLYADWG DMIQVTLKNS MPDNGTGIHW HGLRQYHTCT EDGVPGITEC
60 70 80 90 100
PLAPGDTKTY TFQATQFGTS WYHSHYSSQY GEGMLGGIVI NGPATSNYDV
110 120 130 140 150
DLGVYTISDW YYTPVFALGE RIAHSQAGPP SGDNGLINGS MVAPAGQTGG
160 170 180 190 200
KYTTNTITAG KKYRLRLINT SVDNHFMVSL DNHAFTVITS DFVPIVPYTA
210 220 230 240 250
NWIFIGIGQR YDVIITANQT VGSYWFRAEV QNGCGTNNNN GNIKSIFTYS
260 270 280 290 300
GAASTTPSSS ATPYTGRCTD ETGIIPFWDS FVPSGPLSGN VEQLNVAINI
310 320 330 340 350
GVDASGPIVT WGINLSAIDV DWKKPILQYV LDGNNSWPAS ENLIELPNAA
360 370 380 390 400
QWYYWVIQEV PGNVNGNPVS INVPHPMHLH GHDFFLLGTG VGTYNNTING
410 420 430 440 450
PSLDYDNPTR RDVAMLPAGG WMVLAFQTDN PGAWLMHCHI AWHVSEGLAV

QFQG
Length:454
Mass (Da):49,323
Last modified:December 1, 2001 - v1
Checksum:iEB56A720394D912A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei4541

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY047482 Genomic DNA. Translation: AAL06114.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY047482 Genomic DNA. Translation: AAL06114.1.

3D structure databases

ProteinModelPortaliQ96UM2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi40559.EDN31422.

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1263. Eukaryota.
COG2132. LUCA.

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.
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.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAC3_BOTFU
AccessioniPrimary (citable) accession number: Q96UM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 1, 2001
Last modified: September 7, 2016
This is version 62 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.