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Protein

Laccase-1

Gene

lcc1

Organism
Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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 bindingi119Copper 1; type 2By similarity1
Metal bindingi121Copper 2; type 3By similarity1
Metal bindingi163Copper 2; type 3By similarity1
Metal bindingi165Copper 3; type 3By similarity1
Metal bindingi445Copper 4; type 1By similarity1
Metal bindingi448Copper 1; type 2By similarity1
Metal bindingi450Copper 3; type 3By similarity1
Metal bindingi504Copper 3; type 3By similarity1
Metal bindingi505Copper 4; type 1By similarity1
Metal bindingi506Copper 2; type 3By similarity1
Metal bindingi510Copper 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-1 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 1
Diphenol oxidase 1
Urishiol oxidase 1
Gene namesi
Name:lcc1
Synonyms:lac1
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
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000008558421 – 561Laccase-1Add BLAST541

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi71N-linked (GlcNAc...)Sequence analysis1
Glycosylationi87N-linked (GlcNAc...)Sequence analysis1
Glycosylationi114N-linked (GlcNAc...)Sequence analysis1
Glycosylationi226N-linked (GlcNAc...)Sequence analysis1
Glycosylationi284N-linked (GlcNAc...)Sequence analysis1
Glycosylationi327N-linked (GlcNAc...)Sequence analysis1
Glycosylationi391N-linked (GlcNAc...)Sequence analysis1
Glycosylationi398N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

Not induced by resveratrol or tannins.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi40559.EDN17560.

Structurei

3D structure databases

ProteinModelPortaliQ12570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini68 – 185Plastocyanin-like 1Add BLAST118
Domaini191 – 337Plastocyanin-like 2Add BLAST147
Domaini396 – 525Plastocyanin-like 3Add BLAST130

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

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: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12570-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNSFFSSLA KFASLSLAFA LPTAEVIPSA LEERQSCANT ATTRSCWGQY
60 70 80 90 100
SASTNSYTTV PKTGYWLVVQ NTTLSADGVS RPTLNFNGTI PGPQITADWG
110 120 130 140 150
DDVIVHVTNK LTSNGTSIHW HGIRQLNNAQ YDGVPGITQC PIAPGGTLTY
160 170 180 190 200
KFHADNYGSS WYHSHFILQY GDGLFGPLVI NGPATANYDV DLGMLFLNDW
210 220 230 240 250
NHVPVQSLWD KAKTGAPPTL LTGLMNGTNT YNGAGKKFQT TFTPGLKYRI
260 270 280 290 300
RVVNTAVDGH FQFSIDGHSF QVIAMDFVPI VPYNATSILV SIAQRYDIIV
310 320 330 340 350
TANAAVGNYW IRAGWQTACS GNTNAANITG ILRYTGSSST ADPTTTSTVT
360 370 380 390 400
ASTSCLDEPL ASLVPFVPIN PVASSIMKTT LTTGGGQWLF NGSSLLLNWT
410 420 430 440 450
DPTLLTVLNS GNIWPTEYNV IPIESTTANK GWAVLAISGP NGPNHPIHLH
460 470 480 490 500
GHDFWTLSQG TGAYTATTAL NLVNPPRRDV MTLPTGGHLV IAFQIDNPGS
510 520 530 540 550
WLMHCHIAWH ASEGLALQFV ESESSILPTI GTADVSTFQN TCAAWKAWTP
560
TEPFPQDDSG I
Length:561
Mass (Da):60,337
Last modified:December 12, 2006 - v3
Checksum:i7F366B289EF73C23
GO

Sequence cautioni

The sequence AAB41823 differs from that shown. Reason: Erroneous gene model prediction. The sequence does probably not originate from mRNA or it was not properly spliced.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti117 – 118SI → TM in AAB41823 (Ref. 2) Curated2
Sequence conflicti372V → I in AAB41823 (Ref. 2) Curated1
Sequence conflicti429N → K in AAB41823 (Ref. 2) Curated1
Sequence conflicti481M → L in AAB41823 (Ref. 2) Curated1
Sequence conflicti484P → S in AAB41823 (Ref. 2) Curated1
Sequence conflicti511A → V in AAB41823 (Ref. 2) Curated1
Sequence conflicti547A → G in AAB41823 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF243854 Genomic DNA. Translation: AAK77952.1.
U20192 mRNA. Translation: AAB41823.1. Sequence problems.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF243854 Genomic DNA. Translation: AAK77952.1.
U20192 mRNA. Translation: AAB41823.1. Sequence problems.

3D structure databases

ProteinModelPortaliQ12570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi40559.EDN17560.

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 nameiLAC1_BOTFU
AccessioniPrimary (citable) accession number: Q12570
Secondary accession number(s): Q96WN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 12, 2006
Last modified: September 7, 2016
This is version 80 of the entry and version 3 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.