NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=RS22;
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 7;
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: In mycelia, at a higher level than LCC1, LCC2 and LCC3.
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

Z54277; CAA91042.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S68120; S68120.

3D structure databases

HSSP

Q9Y780; 1HFU. [HSSP ENTRY / PDB]

ModBase

Q02081.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
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; FALSE_NEG.
PS00080; MULTICOPPER_OXIDASE2; FALSE_NEG.

ProtoNet

Q02081.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`
`CHAIN`	`20 531`	`512`	`Laccase-4.`	`PRO_0000002938`
`DOMAIN`	`23 146`	`124`	`Plastocyanin-like 1.`
`DOMAIN`	`158 315`	`158`	`Plastocyanin-like 2.`
`DOMAIN`	`384 507`	`124`	`Plastocyanin-like 3.`
`METAL`	`83 83`		`Copper 1; type 2 (By similarity).`
`METAL`	`85 85`		`Copper 2; type 3 (By similarity).`
`METAL`	`128 128`		`Copper 2; type 3 (By similarity).`
`METAL`	`130 130`		`Copper 3; type 3 (By similarity).`
`METAL`	`427 427`		`Copper 4; type 1 (By similarity).`
`METAL`	`430 430`		`Copper 1; type 2 (By similarity).`
`METAL`	`432 432`		`Copper 3; type 3 (By similarity).`
`METAL`	`479 479`		`Copper 3; type 3 (By similarity).`
`METAL`	`480 480`		`Copper 4; type 1 (By similarity).`
`METAL`	`481 481`		`Copper 2; type 3 (By similarity).`
`CARBOHYD`	`66 66`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`109 109`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`186 186`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`231 231`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`280 280`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`395 395`		`N-linked (GlcNAc...) (Potential).`
`VARIANT`	`42 42`	`1`	`P -> S.`
`VARIANT`	`119 119`	`1`	`H -> R.`
`VARIANT`	`246 246`	`1`	`R -> S.`
`VARIANT`	`256 256`	`1`	`P -> L.`
`VARIANT`	`261 261`	`1`	`P -> A.`

Sequence information

Length: 531 AA [This is the length of the unprocessed precursor]

Molecular weight: 57545 Da [This is the MW of the unprocessed precursor]

CRC64: 737339803F75AB19 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSSITLLPL LAAVSTPAFA AVRNYKFDIK NVNVAPDGFQ RPIVSVNGLV PGTLITANKG 

        70         80         90        100        110        120 
DTLRINVTNQ LTDPSMRRAT TIHWHGLFQA TTADEDGPAF VTQCPIAQNL SYTYEIPLHG 

       130        140        150        160        170        180 
QTGTMWYHAH LASQYVDGLR GPLVIYDPND PHKSRYDVDD ASTVVMLEDW YHTPAPVLEK 

       190        200        210        220        230        240 
QMFSTNNTAL LSPVPDSGLI NGKGRYVGGP AVPRSVINVK RGKRYRLRVI NASAIGSFTF 

       250        260        270        280        290        300 
SIEGHRLTVI EADGIPHQPL PVDSFQIYAG QRYSVIVEAN QTAANYWIRA PMTVAGAGTN 

       310        320        330        340        350        360 
ANLDPTNVFA VLHYEGAPNA EPTTEQGSAI GTALVEENLH ALINPGAPGG SAPADVSLNL 

       370        380        390        400        410        420 
AIGRSTVDGI LRFTFNNIKY EAPSLPTLLK ILANNASNDA DFTPNEHTIV LPHNKVIGAQ 

       430        440        450        460        470        480 
HHRGADHPIH LHGHVFDIVK SLGGTPNYVN PPRRDVVRVG GTGVVLRFKA DNPGPWFVHC 

       490        500        510        520        530 
HIDCTWRLGS HLSLPRPPAR FARVSSRSSP TMPGTSSAPS TRLFLPICSK W

Q02081 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