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Reviewed, UniProtKB/Swiss-Prot P17489 (LAC1_EMENI)

Last modified January 19, 2010. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Laccase-1
    EC=1.10.3.2
Alternative name(s):
    Laccase I
    Benzenediol:oxygen oxidoreductase 1
    Urishiol oxidase 1
    Diphenol oxidase 1
    Conidial laccase
Gene names
Name: yA
ORF Names: AN6635
OrganismEmericella nidulans (Aspergillus nidulans) [Complete proteome]
Taxonomic identifier162425 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

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Protein attributes

Sequence length609 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Required for the conversion of the yellow polyketide pigment synthesized by wA to the conidial green pigment. Ref.3

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. Ref.3

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

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Ontologies

Keywords
   Biological processConidiation
Sporulation
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processconidium formation

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

sporulation resulting in formation of a cellular spore

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

laccase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 609589Laccase-1
PRO_0000002927

Regions

Domain45 – 14197Plastocyanin-like 1
Domain270 – 372103Plastocyanin-like 2
Domain463 – 602140Plastocyanin-like 3

Sites

Metal binding791Copper 1; type 2 Probable
Metal binding811Copper 2; type 3 Probable
Metal binding1231Copper 2; type 3 Probable
Metal binding1251Copper 3; type 3 Probable
Metal binding5081Copper 4; type 1 Probable
Metal binding5111Copper 1; type 2 Probable
Metal binding5131Copper 3; type 3 Probable
Metal binding5851Copper 3; type 3 Probable
Metal binding5861Copper 4; type 1 Probable
Metal binding5871Copper 2; type 3 Probable
Metal binding5911Copper 4; type 1 Probable
Metal binding5961Copper 4; type 1 Probable

Amino acid modifications

Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation2571N-linked (GlcNAc...) Potential
Glycosylation2681N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Glycosylation4861N-linked (GlcNAc...) Potential
Glycosylation5311N-linked (GlcNAc...) Potential
Glycosylation5461N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict225 – 2295DGLTA → TALLS in CAA36787. Ref.1
Sequence conflict3591G → A in CAA36787. Ref.1
Sequence conflict4211G → A in CAA36787. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P17489-1 [UniParc].

Last modified May 26, 2009. Version 3.
Checksum: 529A20B2DD9AA73E

FASTA60967,981
        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 EVSDDGLTAV LEGTHLTEKG 

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

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

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

       430        440        450        460        470        480 
GVPPPPPSSE 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

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References

« Hide 'large scale' references
[1]"Sequence and molecular structure of the Aspergillus nidulans yA (laccase I) gene."
Aramayo R., Timberlake W.E.
Nucleic Acids Res. 18:3415-3415(1990) [PubMed: 2192364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FGSC A4 / M139 and Winter.
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / M139.
[3]"Molecular characterization of the Aspergillus nidulans yA locus."
O'Hara E.B., Timberlake W.E.
Genetics 121:249-254(1989) [PubMed: 2659435] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X52552 Genomic DNA. Translation: CAA36787.1.
AACD01000110 Genomic DNA. Translation: EAA58164.1.
PIRKSASL1. S10149.
RefSeqXP_664239.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2870381.
KEGGani:AN6635.2.

Phylogenomic databases

PhylomeDBP17489.

Enzyme and pathway databases

BRENDA1.10.3.2. 3859.

Family and domain databases

InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 3 hits.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
PROSITEPS00079. MULTICOPPER_OXIDASE1. False negative.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLAC1_EMENI
AccessionPrimary (citable) accession number: P17489
Secondary accession number(s): Q5AYJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 26, 2009
Last modified: January 19, 2010
This is version 77 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents