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Protein

Laccase-2

Gene

lcc2

Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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)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 bindingi417 – 4171Copper 4; type 1By similarity
Metal bindingi420 – 4201Copper 1; type 2By similarity
Metal bindingi422 – 4221Copper 3; type 3By similarity
Metal bindingi470 – 4701Copper 3; type 3By similarity
Metal bindingi471 – 4711Copper 4; type 1By similarity
Metal bindingi472 – 4721Copper 2; type 3By similarity
Metal bindingi476 – 4761Copper 4; type 1By similarity

GO - Molecular functioni

GO - Biological processi

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
Laccase II
Urishiol oxidase 2
Gene namesi
Name:lcc2
OrganismiAgaricus bisporus (White button mushroom)
Taxonomic identifieri5341 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 520501Laccase-2PRO_0000002919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi492 – 4921N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ12542.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 145125Plastocyanin-like 1Add
BLAST
Domaini157 – 305149Plastocyanin-like 2Add
BLAST
Domaini375 – 488114Plastocyanin-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. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q12542-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFSNAFVLV AACISSVLAD TKTFNFDLVN TRLAPDGFER DTVVINGEFP
60 70 80 90 100
GTLVQVNKGD SVRIPVNNKL TSSTMRRSVS IHWHGFFQAR TSGQDGPAFV
110 120 130 140 150
NQCPQPPNTT FTYEFSVADE SGTFWYHSHL STQYCDGLRG AFVVYDPEDP
160 170 180 190 200
LGHLYDVDDE TTVITLAEWY HVLAPDINNE FFSSGIIPVQ DSGLINGKGR
210 220 230 240 250
FNGGPETPFA VVNVEQGKRY RFRVIAISCR PFFTFSVDNH NLTFMEADSV
260 270 280 290 300
EHDPVEIQNV DIYAAQRVSV ILNANQPVDN YWMRAPMTGG NPDRNPNLNI
310 320 330 340 350
SLTLAILRYK GAPEVEPTTV NVPGHKLLDQ EMHPIAQEGP GKLGDGPPDK
360 370 380 390 400
HITLNIAQPN APFFDINGIS YISPTVPVLL QILSGAKRPE DVLPSEQIFF
410 420 430 440 450
VPKNSLIEVN IPGEGAHPFH LHGHNFDVVL ASNDDTFNFV NPPRRDVYPI
460 470 480 490 500
NGGNTTFRFF TDNPGAWFLH CHIDWHLEAG LAIVFAEAPE DNVSGPQSQI
510 520
TPQDWLDLCP EYNAIEPEFQ
Length:520
Mass (Da):57,823
Last modified:November 1, 1996 - v1
Checksum:iEF100145F0A697AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10663 mRNA. Translation: AAA17035.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10663 mRNA. Translation: AAA17035.1.

3D structure databases

ProteinModelPortaliQ12542.
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. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of two laccase genes in the cultivated mushroom Agaricus bisporus."
    Perry C.R., Smith M., Britnell C.H., Wood D.A., Thurston C.F.
    J. Gen. Microbiol. 139:1209-1218(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: D649.

Entry informationi

Entry nameiLAC2_AGABI
AccessioniPrimary (citable) accession number: Q12542
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.