[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=FGSC 4, and Winter; DOI=10.1093/nar/18.11.3415; PubMed=2192364 [NCBI, ExPASy, EBI, Israel, Japan] Aramayo R., Timberlake W.E.; "Sequence and molecular structure of the Aspergillus nidulans yA (laccase I) gene."; Nucleic Acids Res. 18:3415-3415(1990).
[2]	FUNCTION, AND DEVELOPMENTAL STAGE. PubMed=2659435 [NCBI, ExPASy, EBI, Israel, Japan] O'Hara E.B., Timberlake W.E.; "Molecular characterization of the Aspergillus nidulans yA locus."; Genetics 121:249-254(1989).

Comments

FUNCTION: Required for the conversion of the yellow polyketide pigment synthesized by wA to the conidial green pigment.
CATALYTIC ACTIVITY: 4 benzenediol + O₂ = 4 benzosemiquinone + 2 H₂O.
COFACTOR: Binds 4 copper ions per subunit. The copper ions are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear (By similarity).
SUBCELLULAR LOCATION: Secreted (Potential).
DEVELOPMENTAL STAGE: Specifically expressed late during asexual development.
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

X52552; CAA36787.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S10149; KSASL1.

3D structure databases

HSSP

Q9Y780; 1HFU. [HSSP ENTRY / PDB]

ModBase

P17489.

Ontologies

GO:0008471;	Molecular function: laccase activity (inferred from electronic annotation from EC).
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; 1.

Other

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

Keywords

Conidiation; Copper; Glycoprotein; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal; Sporulation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`Potential.`
`CHAIN`	`21 609`	`589`	`Laccase-1.`	`PRO_0000002927`
`DOMAIN`	`45 141`	`97`	`Plastocyanin-like 1.`
`DOMAIN`	`270 372`	`103`	`Plastocyanin-like 2.`
`DOMAIN`	`463 602`	`140`	`Plastocyanin-like 3.`
`METAL`	`79 79`		`Copper (type 2) (Probable).`
`METAL`	`81 81`		`Copper (type 3) (Probable).`
`METAL`	`123 123`		`Copper (type 3) (Probable).`
`METAL`	`125 125`		`Copper (type 3) (Probable).`
`METAL`	`508 508`		`Copper (type 1) (Probable).`
`METAL`	`511 511`		`Copper (type 2) (Probable).`
`METAL`	`513 513`		`Copper (type 3) (Probable).`
`METAL`	`585 585`		`Copper (type 3) (Probable).`
`METAL`	`586 586`		`Copper (type 1) (Probable).`
`METAL`	`587 587`		`Copper (type 3) (Probable).`
`METAL`	`591 591`		`Copper (type 1) (Probable).`
`METAL`	`596 596`		`Copper (type 1) (Probable).`
`CARBOHYD`	`75 75`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`257 257`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`268 268`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`403 403`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`443 443`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`486 486`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`531 531`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`546 546`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 609 AA [This is the length of the unprocessed precursor]

Molecular weight: 68038 Da [This is the MW of the unprocessed precursor]

CRC64: E667A42EF5909512 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYLSTVLFPL LALNLGLSHA RFVRETLELT WEYGSPNGGT PREMVFTNGE YPGPDLIFDE 

        70         80         90        100        110        120 
DDDVEVLVIN NLPFNTTVHW HGLEMRETPE ADGVPGLTQT PIEPGATFTY RFRAYPAGTF 

       130        140        150        160        170        180 
WYHSHYKGLM QDGQVGAMYI RRKPDALRPY AVITEDPREL AEIQYAEDNP YLMLATDWTY 

       190        200        210        220        230        240 
LTSAEYHNIE VESGYNVFCV DSLLINGRGS VYCPGYQYLE EVSDTALLSV LEGTHLTEKG 

       250        260        270        280        290        300 
CLQPDLHNVQ GDYGPWNLSA VPTEVVFNCT PSSVEPPVIY VDPEFNGWVS LNFIGGAAQK 

       310        320        330        340        350        360 
AITFSVDNHP MWVYEVDGQF VEPREVEMVG VYSGARYAVM IKLDQTPGDY AIRIAVNGAD 

       370        380        390        400        410        420 
QVMSVYAILS YVNQDWIHRE NVPKAAIGPH TDTVGYMNYG GGNTSADVRQ LLFTENLPAF 

       430        440        450        460        470        480 
AVPPPPPSSE VSTTLRTGMI RVNNSYSWSL GNNVLYEPEM TSSTPLLFEP DPLAVIAPKY 

       490        500        510        520        530        540 
ALTTENNTWV DIVLEITADP RDLIHPPHPI HKHGNRAYII GNGVGKFRWE NVSAAEAEVP 

       550        560        570        580        590        600 
DLFYVNETAA LRDTFVTDFF DSRLMDGAWI VIRYFVQDKF PSILHCHIAS HQMGGMALAL 


LDGVDVWDS

P17489 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