Reviewed, UniProtKB/Swiss-Prot Q12718 (LAC2_TRAVE)

Names and origin

Protein names

Recommended name:
    Laccase-2
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 2
    Urishiol oxidase 2
    Diphenol oxidase 2
    Laccase I

Gene names

Name:	LCC2
Synonyms:	LCCI

Organism

Trametes versicolor (White-rot fungus) (Coriolus versicolor)

Taxonomic identifier

5325 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Trametes

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Lignin degradation and detoxification of lignin-derived products Probable.
Catalytic activity	4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O.
Cofactor	Binds 4 copper ions per monomer.
Subcellular location	Secreted.
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains.

Ontologies

Keywords
Biological process	Lignin degradation
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: InterPro laccase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 519

499

Laccase-2

PRO_0000002940

Regions

Domain

22 – 147

126

Plastocyanin-like 1

Domain

159 – 301

143

Plastocyanin-like 2

Domain

368 – 490

123

Plastocyanin-like 3

Sites

Metal binding

84

1

Copper 1; type 2

Metal binding

86

1

Copper 2; type 3

Metal binding

129

1

Copper 2; type 3

Metal binding

131

1

Copper 3; type 3

Metal binding

415

1

Copper 4; type 1

Metal binding

418

1

Copper 1; type 2

Metal binding

420

1

Copper 3; type 3

Metal binding

472

1

Copper 3; type 3

Metal binding

473

1

Copper 4; type 1

Metal binding

474

1

Copper 2; type 3

Metal binding

478

1

Copper 4; type 1

Amino acid modifications

Glycosylation

74

1

N-linked (GlcNAc...)

Glycosylation

161

1

N-linked (GlcNAc...) Potential

Glycosylation

228

1

N-linked (GlcNAc...) Potential

Glycosylation

237

1

N-linked (GlcNAc...)

Glycosylation

271

1

N-linked (GlcNAc...)

Glycosylation

353

1

N-linked (GlcNAc...)

Glycosylation

361

1

N-linked (GlcNAc...)

Glycosylation

456

1

N-linked (GlcNAc...)

Experimental info

Sequence conflict

69

1

D → V in AAC49828. Ref.1

Secondary structure

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519

Helix Strand Turn

Details...

Beta strand

24 – 35

12

Beta strand

42 – 47

6

Beta strand

50 – 52

3

Beta strand

56 – 59

4

Beta strand

63 – 70

8

Helix

75 – 77

3

Beta strand

83 – 86

4

Helix

94 – 96

3

Turn

100 – 102

3

Beta strand

111 – 118

8

Beta strand

124 – 130

7

Helix

135 – 138

4

Beta strand

141 – 147

7

Helix

154 – 156

3

Helix

162 – 164

3

Beta strand

165 – 171

7

Turn

176 – 178

3

Beta strand

187 – 191

5

Beta strand

207 – 210

4

Beta strand

215 – 222

8

Beta strand

229 – 233

5

Beta strand

238 – 243

6

Beta strand

246 – 258

13

Beta strand

263 – 269

7

Beta strand

274 – 287

14

Helix

291 – 293

3

Beta strand

296 – 301

6

Beta strand

317 – 319

3

Helix

322 – 324

3

Beta strand

327 – 329

3

Beta strand

342 – 347

6

Beta strand

350 – 352

3

Beta strand

357 – 359

3

Helix

371 – 376

6

Turn

382 – 384

3

Beta strand

385 – 387

3

Beta strand

390 – 394

5

Beta strand

399 – 405

7

Beta strand

416 – 419

4

Beta strand

424 – 428

5

Beta strand

437 – 439

3

Beta strand

442 – 447

6

Helix

451 – 453

3

Beta strand

456 – 462

7

Beta strand

467 – 475

9

Helix

476 – 480

5

Beta strand

484 – 489

6

Helix

491 – 493

3

Helix

494 – 497

4

Helix

502 – 512

11

Helix

516 – 518

3

Sequences

	Sequence		Length	Mass (Da)
	Q12718-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BFFB5B4CD0007702	FASTA	519	55,811
	10 20 30 40 50 60 MGLQRFSFFV TLALVARSLA AIGPVASLVV ANAPVSPDGF LRDAIVVNGV VPSPLITGKK 70 80 90 100 110 120 GDRFQLNVDD TLTNHSMLKS TSIHWHGFFQ AGTNWADGPA FVNQCPIASG HSFLYDFHVP 130 140 150 160 170 180 DQAGTFWYHS HLSTQYCDGL RGPFVVYDPK DPHASRYDVD NESTVITLTD WYHTAARLGP 190 200 210 220 230 240 RFPLGADATL INGLGRSAST PTAALAVINV QHGKRYRFRL VSISCDPNYT FSIDGHNLTV 250 260 270 280 290 300 IEVDGINSQP LLVDSIQIFA AQRYSFVLNA NQTVGNYWVR ANPNFGTVGF AGGINSAILR 310 320 330 340 350 360 YQGAPVAEPT TTQTTSVIPL IETNLHPLAR MPVPGSPTPG GVDKALNLAF NFNGTNFFIN 370 380 390 400 410 420 NATFTPPTVP VLLQILSGAQ TAQDLLPAGS VYPLPAHSTI EITLPATALA PGAPHPFHLH 430 440 450 460 470 480 GHAFAVVRSA GSTTYNYNDP IFRDVVSTGT PAAGDNVTIR FQTDNPGPWF LHCHIDFHLD 490 500 510 AGFAIVFAED VADVKAANPV PKAWSDLCPI YDGLSEANQ

References

[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: 9322748] [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: 12163489] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

U44851 Genomic DNA. Translation: AAA86659.1.
U44430 mRNA. Translation: AAC49828.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GYC	X-ray	1.90	A	21-519	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]

Gene3D

G3DSA:2.60.40.420. Cupredoxin. 3 hits.

Pfam

PF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]

PROSITE

PS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. False negative.
[Graphical view]