[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 200478 / PB; TISSUE=Mycelium; PubMed=9572949 [NCBI, ExPASy, EBI, Israel, Japan] Eggert C., LaFayette P.R., Temp U., Eriksson K.-E.L., Dean J.F.D.; "Molecular analysis of a laccase gene from the white rot fungus Pycnoporus cinnabarinus."; Appl. Environ. Microbiol. 64:1766-1772(1998).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Dhawan S., Lal R., Kuhad R.C.; "Cloning, characterization and expression of laccase gene from white rot fungus Pycnoporus cinnabarinus."; Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE OF 85-131. TISSUE=Mycelium; Luis P., Buscot F.; "Molecular biological monitoring of soil fungi with laccase genes."; Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[4]	PROTEIN SEQUENCE OF 22-42, CHARACTERIZATION, AND INDUCTION. STRAIN=ATCC 200478 / PB; TISSUE=Mycelium; PubMed=8919775 [NCBI, ExPASy, EBI, Israel, Japan] Eggert C., Temp U., Eriksson K.-E.L.; "The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: purification and characterization of the laccase."; Appl. Environ. Microbiol. 62:1151-1158(1996).

Comments

FUNCTION: Most probably plays an important role in lignin degradation. Cleaves the C-C and C-O bonds of some phenolic lignin model compounds (such as O- and P-quinols, aminophenols and phenylenediamine). May also be involved in synthesis of phenoxazinone pigments.
CATALYTIC ACTIVITY: 4 benzenediol + O₂ = 4 benzosemiquinone + 2 H₂O.
COFACTOR: Binds 4 copper ions per monomer (By similarity).
SUBCELLULAR LOCATION: Secreted.
INDUCTION: By lignosulfonate, veratryl alcohol and 2,5-xylidine.
SIMILARITY: Belongs to the multicopper oxidase family.
SIMILARITY: Contains 3 plastocyanin-like domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF025481; AAC39469.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY147188; AAN71597.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ420334; CAD12461.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q96UT7; 1KYA. [HSSP ENTRY / PDB]

SMR

O59896; 22-517.

ModBase

O59896.

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 of domain structure.

Gene3D

G3DSA:2.60.40.420; Cupredoxin; 3.

Pfam

PF00394; Cu-oxidase; 1.
PF07731; Cu-oxidase_2; 1.
PF07732; Cu-oxidase_3; 1.
Pfam graphical view of domain structure.

PROSITE

PS00079; MULTICOPPER_OXIDASE1; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Copper; Direct protein sequencing; Glycoprotein; Lignin degradation; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`
`CHAIN`	`22 518`	`497`	`Laccase.`	`PRO_0000002934`
`DOMAIN`	`23 148`	`126`	`Plastocyanin-like 1.`
`DOMAIN`	`160 302`	`143`	`Plastocyanin-like 2.`
`DOMAIN`	`369 489`	`121`	`Plastocyanin-like 3.`
`METAL`	`85 85`		`Copper 1; type 2 (By similarity).`
`METAL`	`87 87`		`Copper 2; type 3 (By similarity).`
`METAL`	`130 130`		`Copper 2; type 3 (By similarity).`
`METAL`	`132 132`		`Copper 3; type 3 (By similarity).`
`METAL`	`416 416`		`Copper 4; type 1 (By similarity).`
`METAL`	`419 419`		`Copper 1; type 2 (By similarity).`
`METAL`	`421 421`		`Copper 3; type 3 (By similarity).`
`METAL`	`471 471`		`Copper 3; type 3 (By similarity).`
`METAL`	`472 472`		`Copper 4; type 1 (By similarity).`
`METAL`	`473 473`		`Copper 2; type 3 (By similarity).`
`METAL`	`477 477`		`Copper 4; type 1 (By similarity).`
`CARBOHYD`	`72 72`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`75 75`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`229 229`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`354 354`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`362 362`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`398 398`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`455 455`		`N-linked (GlcNAc...) (Potential).`
`CONFLICT`	`348 348`		`N -> S (in Ref. 2; AAN71597).`

Sequence information

Length: 518 AA [This is the length of the unprocessed precursor]

Molecular weight: 55986 Da [This is the MW of the unprocessed precursor]

CRC64: 31B4386AFDB8DF9D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRFQSLLSF VLVSLAAVAN AAIGPVADLT LTNAAVSPDG FSREAVVVNG ITPAPLIAGQ 

        70         80         90        100        110        120 
KGDRFQLNVI DNLTNHTMLK TTSIHWHGFF QHGTNWADGV SFVNQCPIAS GHSFLYDFQV 

       130        140        150        160        170        180 
PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP NDPQASLYDI DNDDTVITLA DWYHVAAKLG 

       190        200        210        220        230        240 
PRFPLGADAT LINGLGRSPG TTTADLAVIK VTQGKRYRFR LVSLSCDPNH TFSIDGHTMT 

       250        260        270        280        290        300 
VIEADSVNTQ PLEVDSIQIF AAQRYSFVLD ASQPVDNYWI RANPAFGNVG FAGGINSAIL 

       310        320        330        340        350        360 
RYDGAPEVEP TTTQTTSTKP LNEADLHPLT PMPVPGRPEA GGVDKPLNMV FNFNGTNFFI 

       370        380        390        400        410        420 
NNHSFVPPSV PVLLQILSGA QAAQDLVPDG SVYVLPSNSS IEISFPATAN APGTPHPFHL 

       430        440        450        460        470        480 
HGHTFAVVRS AGSSEYNYDN PIFRDVVSTG QPGDNVTIRF QTNNPGPWFL HCHIDFHLEA 

       490        500        510 
GFAVVLAEDT PDTAAVNPVP QSWSDLCPIY DALDPSDL

O59896 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools