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Protein

Laccase

Gene

LAC-1

Organism
Cryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi126 – 1261Copper 1; type 2By similarity
Metal bindingi128 – 1281Copper 2; type 3By similarity
Metal bindingi171 – 1711Copper 2; type 3By similarity
Metal bindingi173 – 1731Copper 3; type 3By similarity
Metal bindingi463 – 4631Copper 4; type 1By similarity
Metal bindingi466 – 4661Copper 1; type 2By similarity
Metal bindingi468 – 4681Copper 3; type 3By similarity
Metal bindingi533 – 5331Copper 3; type 3By similarity
Metal bindingi534 – 5341Copper 4; type 1By similarity
Metal bindingi535 – 5351Copper 2; type 3By similarity
Metal bindingi539 – 5391Copper 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 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase
Diphenol oxidase
Urishiol oxidase
Gene namesi
Name:LAC-1
OrganismiCryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Taxonomic identifieri5116 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeDiaporthalesCryphonectriaceaeCryphonectria-Endothia complexCryphonectria

Subcellular locationi

Secreted Curated

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 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 591571LaccasePRO_0000002920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi407 – 4071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi425 – 4251N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ03966.
SMRiQ03966. Positions 33-591.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 189124Plastocyanin-like 1Add
BLAST
Domaini198 – 356159Plastocyanin-like 2Add
BLAST
Domaini416 – 551136Plastocyanin-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.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q03966-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPSFFRALFS GLIASQLSWA APSLLHPLEP RQQPNCNTAS NRACWISGSY
60 70 80 90 100
DITTDYEVKT PLTGVVRQYD LTLTQAENWL GPDGVVKEDV MLVNGNILGP
110 120 130 140 150
VIHAQWGDTI SVTVTNNLKY NGTTIHWHGI RQLNTNLQDG VNGITECPIP
160 170 180 190 200
PNGGSKTYTF IAHQYGTSWY HSHFSAQYGN GIVGAIQIDG PASLPYDIDL
210 220 230 240 250
GPLVLSDYYY KTADELVVYT QSNAPPASDN VLFNGTNINP ANTTQGQYKT
260 270 280 290 300
ITLTPGKRHR LRIINTSVEN NFQVSIVGHS MTVIESDFVP VDSFTTDSLF
310 320 330 340 350
VGIGQRYDVT IDASQATDNY WMNVTFGGGG FCGKSNNPYP AAIIHYNGAS
360 370 380 390 400
NSHPTNKGVA PADHECLDLL NLVPVVPRSI PTSGFVAASD NTLDVQLSTT
410 420 430 440 450
TRKWTINGST LDVDWGHPIT QYVINKSTAW PSTDNVWLVE EANQWAYWLI
460 470 480 490 500
ENDPTATGNA LPHPIHLHGH DFVVLGRSPN VSPTAQTPYT FTSSDVSSLN
510 520 530 540 550
GNNPIRRDVV MLPPKGWLLI AFQTTNPGAW LMHCHIAWHV SAGLGNTFLE
560 570 580 590
QPSAFVAGLN TNDVNQLNSQ CKSWNAYYPS KDIFKQDDSG V
Length:591
Mass (Da):64,696
Last modified:November 1, 1996 - v1
Checksum:iB2F44CB2AAD77701
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73257 Genomic DNA. Translation: AAA33105.1.
S38903 Genomic DNA. Translation: AAA09235.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73257 Genomic DNA. Translation: AAA33105.1.
S38903 Genomic DNA. Translation: AAA09235.1.

3D structure databases

ProteinModelPortaliQ03966.
SMRiQ03966. Positions 33-591.
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.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular analysis of the laccase gene from the chestnut blight fungus and selective suppression of its expression in an isogenic hypovirulent strain."
    Choi G.H., Larson T.G., Nuss D.L.
    Mol. Plant Microbe Interact. 5:119-128(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiLAC1_CRYPA
AccessioniPrimary (citable) accession number: Q03966
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 79 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.