NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=R22;
DOI=10.1007/s002940050061; PubMed=8598061 [NCBI, ExPASy, EBI, Israel, Japan]
Wahleithner J.A., Xu F., Brown K.M., Brown S.H., Golightly E.J., Halkier T., Kauppinen S., Pederson A., Schneider P.;
"The identification and characterization of four laccases from the plant pathogenic fungus Rhizoctonia solani.";
Curr. Genet. 29:395-403(1996).

Comments

FUNCTION: Lignin degradation and detoxification of lignin-derived products (Probable).
CATALYTIC ACTIVITY: 4 benzenediol + O₂ = 4 benzosemiquinone + 2 H₂O.
COFACTOR: Binds 4 copper ions per monomer (By similarity).
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 6;
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: In mycelia, at a lower level than LCC4.
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

Z54275; -; NOT_ANNOTATED_CDS; Genomic_DNA.

[EMBL / GenBank / DDBJ]

PIR

S68117; S68117.

3D structure databases

HSSP

Q9Y780; 1HFU. [HSSP ENTRY / PDB]

ModBase

P56193.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0008471;	Molecular function: laccase activity (inferred from electronic annotation from EC).
GO:0046274;	Biological process: lignin catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.
PS00080; MULTICOPPER_OXIDASE2; FALSE_NEG.

Other

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`	`Potential.`
`CHAIN`	`20 576`	`557`	`Laccase-1.`	`PRO_0000002935`
`DOMAIN`	`21 145`	`125`	`Plastocyanin-like 1.`
`DOMAIN`	`157 304`	`148`	`Plastocyanin-like 2.`
`DOMAIN`	`376 576`	`201`	`Plastocyanin-like 3.`
`METAL`	`82 82`		`Copper 1; type 2 (By similarity).`
`METAL`	`84 84`		`Copper 2; type 3 (By similarity).`
`METAL`	`127 127`		`Copper 2; type 3 (By similarity).`
`METAL`	`129 129`		`Copper 3; type 3 (By similarity).`
`METAL`	`471 471`		`Copper 4; type 1 (By similarity).`
`METAL`	`474 474`		`Copper 1; type 2 (By similarity).`
`METAL`	`476 476`		`Copper 3; type 3 (By similarity).`
`METAL`	`523 523`		`Copper 3; type 3 (By similarity).`
`METAL`	`524 524`		`Copper 4; type 1 (By similarity).`
`METAL`	`525 525`		`Copper 2; type 3 (By similarity).`
`METAL`	`529 529`		`Copper 4; type 1 (By similarity).`
`CARBOHYD`	`41 41`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`182 182`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`228 228`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`294 294`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`368 368`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 576 AA [This is the length of the unprocessed precursor]

Molecular weight: 64377 Da [This is the MW of the unprocessed precursor]

CRC64: CE5E32918038AE48 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MARTTFLVSV SLFVSAVLAR TVEYGLKISD GEIAPDGVKR NATLVNGGYP GPLIFANKGD 

        70         80         90        100        110        120 
TLKVKVQNKL TNPEMYRTTS IHWHGLLQHR NADDDGPSFV TQCPIVPRES YTYTIPLDDQ 

       130        140        150        160        170        180 
TGTYWYHSHL SSQYVDGLRG PLVIYDPKDP HRRLYDVDDE KTVLIIGDWY HESSKAILAS 

       190        200        210        220        230        240 
GNITRQRPVS ATINGKGRFD PDNTPANPDT LYTLKVKRGK RYRLRVINSS EIASFRFSVE 

       250        260        270        280        290        300 
GHKVTVIAAD GVSTKPYQVD AFDILAGQRI DCVVEANQEP DTYWINAPLT NVPNKTAQAL 

       310        320        330        340        350        360 
LVYEEDRRPY HPPKGPYRKW SVSEAIIKYW NHKHKHGRGL LSGHGGLKAR MIEGSHHLHS 

       370        380        390        400        410        420 
RSVVKRQNET TTVVMDESKL VPLEYPGAAC GSKPADLVLD LTFGLNFATG HWMINGIPYE 

       430        440        450        460        470        480 
SPKIPTLLKI LTDEDGVTES DFTKEEHTVI LPKNKCIEFN IKGNSGIPIT HPVHLHGHTW 

       490        500        510        520        530        540 
DVVQFGNNPP NYVNPPRRDV VGSTDAGVRI QFKTDNPGPW FLHCHIDWHL EEGFAMVFAE 

       550        560        570 
APEAVKGGPK SVAVDSQWEG LCGKYDNWLK SNPGQL

P56193 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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