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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)DescriptionActionsGraphical viewLength
Metal bindingi84Copper 1; type 21
Metal bindingi86Copper 2; type 31
Metal bindingi129Copper 2; type 31
Metal bindingi131Copper 3; type 31
Metal bindingi415Copper 4; type 11
Metal bindingi418Copper 1; type 21
Metal bindingi420Copper 3; type 31
Metal bindingi472Copper 3; type 31
Metal bindingi473Copper 4; type 11
Metal bindingi474Copper 2; type 31
Metal bindingi478Copper 4; type 11

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.

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000000294021 – 519Laccase-2Add BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi74N-linked (GlcNAc...)1
Glycosylationi161N-linked (GlcNAc...)Sequence analysis1
Glycosylationi228N-linked (GlcNAc...)Sequence analysis1
Glycosylationi237N-linked (GlcNAc...)1
Glycosylationi271N-linked (GlcNAc...)1
Glycosylationi353N-linked (GlcNAc...)1
Glycosylationi361N-linked (GlcNAc...)1
Glycosylationi456N-linked (GlcNAc...)1

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1519
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 35Combined sources12
Beta strandi42 – 47Combined sources6
Beta strandi50 – 52Combined sources3
Beta strandi56 – 59Combined sources4
Beta strandi63 – 70Combined sources8
Helixi75 – 77Combined sources3
Beta strandi83 – 86Combined sources4
Helixi94 – 96Combined sources3
Turni100 – 102Combined sources3
Beta strandi111 – 118Combined sources8
Beta strandi124 – 130Combined sources7
Helixi135 – 138Combined sources4
Beta strandi141 – 147Combined sources7
Helixi154 – 156Combined sources3
Helixi162 – 164Combined sources3
Beta strandi165 – 171Combined sources7
Turni176 – 178Combined sources3
Beta strandi187 – 191Combined sources5
Beta strandi207 – 210Combined sources4
Beta strandi215 – 222Combined sources8
Beta strandi229 – 233Combined sources5
Beta strandi238 – 243Combined sources6
Beta strandi246 – 258Combined sources13
Beta strandi263 – 269Combined sources7
Beta strandi274 – 287Combined sources14
Helixi291 – 293Combined sources3
Beta strandi296 – 301Combined sources6
Beta strandi317 – 319Combined sources3
Helixi322 – 324Combined sources3
Beta strandi327 – 329Combined sources3
Beta strandi342 – 347Combined sources6
Beta strandi350 – 352Combined sources3
Beta strandi357 – 359Combined sources3
Helixi371 – 376Combined sources6
Turni382 – 384Combined sources3
Beta strandi385 – 387Combined sources3
Beta strandi390 – 394Combined sources5
Beta strandi399 – 405Combined sources7
Beta strandi416 – 419Combined sources4
Beta strandi424 – 428Combined sources5
Beta strandi437 – 439Combined sources3
Beta strandi442 – 447Combined sources6
Helixi451 – 453Combined sources3
Beta strandi456 – 462Combined sources7
Beta strandi467 – 475Combined sources9
Helixi476 – 480Combined sources5
Beta strandi484 – 489Combined sources6
Helixi491 – 493Combined sources3
Helixi494 – 497Combined sources4
Helixi502 – 512Combined sources11
Helixi516 – 518Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ12718.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 147Plastocyanin-like 1Add BLAST126
Domaini159 – 301Plastocyanin-like 2Add BLAST143
Domaini368 – 490Plastocyanin-like 3Add BLAST123

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.
IPR033138. Cu_oxidase_CS.
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)DescriptionActionsGraphical viewLength
Sequence conflicti69D → V in AAC49828 (PubMed:9322748).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GYCX-ray1.90A21-519[»]
ProteinModelPortaliQ12718.
SMRiQ12718.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

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.
IPR033138. Cu_oxidase_CS.
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...

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: November 2, 2016
This is version 89 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

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.