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Q12718

- LAC2_TRAVE

UniProt

Q12718 - LAC2_TRAVE

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Protein

Laccase-2

Gene

LCC2

Organism
Trametes versicolor (White-rot fungus) (Coriolus versicolor)
Status
Reviewed - 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

Binds 4 copper ions 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

  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

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
Links Updated
U44851 Genomic DNA. Translation: AAA86659.1.
U44430 mRNA. Translation: AAC49828.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U44851 Genomic DNA. Translation: AAA86659.1 .
U44430 mRNA. Translation: AAC49828.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GYC X-ray 1.90 A 21-519 [» ]
ProteinModelPortali Q12718.
SMRi Q12718. Positions 21-519.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17211.

Miscellaneous databases

EvolutionaryTracei Q12718.

Family and domain databases

Gene3Di 2.60.40.420. 3 hits.
InterProi IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view ]
Pfami PF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view ]
SUPFAMi SSF49503. SSF49503. 3 hits.
PROSITEi PS00079. MULTICOPPER_OXIDASE1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 81 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