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Protein

Laccase-2

Gene

LCC2

Organism
Trametes versicolor (White-rot fungus) (Coriolus versicolor)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Lignin degradation and detoxification of lignin-derived products.Curated

Catalytic activityi

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

Cofactori

Cu cationNote: Binds 4 Cu cations per monomer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi84 – 841Copper 1; type 2
Metal bindingi86 – 861Copper 2; type 3
Metal bindingi129 – 1291Copper 2; type 3
Metal bindingi131 – 1311Copper 3; type 3
Metal bindingi415 – 4151Copper 4; type 1
Metal bindingi418 – 4181Copper 1; type 2
Metal bindingi420 – 4201Copper 3; type 3
Metal bindingi472 – 4721Copper 3; type 3
Metal bindingi473 – 4731Copper 4; type 1
Metal bindingi474 – 4741Copper 2; type 3
Metal bindingi478 – 4781Copper 4; type 1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17211.

Names & Taxonomyi

Protein namesi
Recommended name:
Laccase-2 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 2
Diphenol oxidase 2
Laccase I
Urishiol oxidase 2
Gene namesi
Name:LCC2
Synonyms:LCCI
OrganismiTrametes versicolor (White-rot fungus) (Coriolus versicolor)
Taxonomic identifieri5325 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesTrametes

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 519499Laccase-2PRO_0000002940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi237 – 2371N-linked (GlcNAc...)
Glycosylationi271 – 2711N-linked (GlcNAc...)
Glycosylationi353 – 3531N-linked (GlcNAc...)
Glycosylationi361 – 3611N-linked (GlcNAc...)
Glycosylationi456 – 4561N-linked (GlcNAc...)

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1
519
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 3512Combined sources
Beta strandi42 – 476Combined sources
Beta strandi50 – 523Combined sources
Beta strandi56 – 594Combined sources
Beta strandi63 – 708Combined sources
Helixi75 – 773Combined sources
Beta strandi83 – 864Combined sources
Helixi94 – 963Combined sources
Turni100 – 1023Combined sources
Beta strandi111 – 1188Combined sources
Beta strandi124 – 1307Combined sources
Helixi135 – 1384Combined sources
Beta strandi141 – 1477Combined sources
Helixi154 – 1563Combined sources
Helixi162 – 1643Combined sources
Beta strandi165 – 1717Combined sources
Turni176 – 1783Combined sources
Beta strandi187 – 1915Combined sources
Beta strandi207 – 2104Combined sources
Beta strandi215 – 2228Combined sources
Beta strandi229 – 2335Combined sources
Beta strandi238 – 2436Combined sources
Beta strandi246 – 25813Combined sources
Beta strandi263 – 2697Combined sources
Beta strandi274 – 28714Combined sources
Helixi291 – 2933Combined sources
Beta strandi296 – 3016Combined sources
Beta strandi317 – 3193Combined sources
Helixi322 – 3243Combined sources
Beta strandi327 – 3293Combined sources
Beta strandi342 – 3476Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi357 – 3593Combined sources
Helixi371 – 3766Combined sources
Turni382 – 3843Combined sources
Beta strandi385 – 3873Combined sources
Beta strandi390 – 3945Combined sources
Beta strandi399 – 4057Combined sources
Beta strandi416 – 4194Combined sources
Beta strandi424 – 4285Combined sources
Beta strandi437 – 4393Combined sources
Beta strandi442 – 4476Combined sources
Helixi451 – 4533Combined sources
Beta strandi456 – 4627Combined sources
Beta strandi467 – 4759Combined sources
Helixi476 – 4805Combined sources
Beta strandi484 – 4896Combined sources
Helixi491 – 4933Combined sources
Helixi494 – 4974Combined sources
Helixi502 – 51211Combined sources
Helixi516 – 5183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYCX-ray1.90A21-519[»]
ProteinModelPortaliQ12718.
SMRiQ12718. Positions 21-519.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12718.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 147126Plastocyanin-like 1Add
BLAST
Domaini159 – 301143Plastocyanin-like 2Add
BLAST
Domaini368 – 490123Plastocyanin-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.

Q12718-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLQRFSFFV TLALVARSLA AIGPVASLVV ANAPVSPDGF LRDAIVVNGV
60 70 80 90 100
VPSPLITGKK GDRFQLNVDD TLTNHSMLKS TSIHWHGFFQ AGTNWADGPA
110 120 130 140 150
FVNQCPIASG HSFLYDFHVP DQAGTFWYHS HLSTQYCDGL RGPFVVYDPK
160 170 180 190 200
DPHASRYDVD NESTVITLTD WYHTAARLGP RFPLGADATL INGLGRSAST
210 220 230 240 250
PTAALAVINV QHGKRYRFRL VSISCDPNYT FSIDGHNLTV IEVDGINSQP
260 270 280 290 300
LLVDSIQIFA AQRYSFVLNA NQTVGNYWVR ANPNFGTVGF AGGINSAILR
310 320 330 340 350
YQGAPVAEPT TTQTTSVIPL IETNLHPLAR MPVPGSPTPG GVDKALNLAF
360 370 380 390 400
NFNGTNFFIN NATFTPPTVP VLLQILSGAQ TAQDLLPAGS VYPLPAHSTI
410 420 430 440 450
EITLPATALA PGAPHPFHLH GHAFAVVRSA GSTTYNYNDP IFRDVVSTGT
460 470 480 490 500
PAAGDNVTIR FQTDNPGPWF LHCHIDFHLD AGFAIVFAED VADVKAANPV
510
PKAWSDLCPI YDGLSEANQ
Length:519
Mass (Da):55,811
Last modified:November 1, 1996 - v1
Checksum:iBFFB5B4CD0007702
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691D → V in AAC49828 (PubMed:9322748).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44851 Genomic DNA. Translation: AAA86659.1.
U44430 mRNA. Translation: AAC49828.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44851 Genomic DNA. Translation: AAA86659.1.
U44430 mRNA. Translation: AAC49828.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYCX-ray1.90A21-519[»]
ProteinModelPortaliQ12718.
SMRiQ12718. Positions 21-519.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17211.

Miscellaneous databases

EvolutionaryTraceiQ12718.

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. "Cloning and sequence analysis of two laccase complementary DNAs from the ligninolytic basidiomycete Trametes versicolor."
    Ong E., Pollock W.B., Smith M.
    Gene 196:113-119(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ATCC 20869 / PAP 52 / 52J.
  2. "Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers."
    Piontek K., Antorini M., Choinowski T.
    J. Biol. Chem. 277:37663-37669(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiLAC2_TRAVE
AccessioniPrimary (citable) accession number: Q12718
Secondary accession number(s): Q12716
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 83 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.