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Reviewed, UniProtKB/Swiss-Prot Q8J130 (TYRO_ASPFU)

Last modified January 20, 2009. Version 34. 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:
    Tyrosinase
    EC=1.14.18.1
Alternative name(s):
    Monophenol monooxygenase
Gene names
Name: tyr1
ORF Names: AFUA_1G17430
OrganismAspergillus fumigatus (Sartorya fumigata) [Complete proteome]
Taxonomic identifier5085 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

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Protein attributes

Sequence length630 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds By similarity.

Catalytic activity

L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O.

Cofactor

Binds 2 copper ions per subunit By similarity.

Sequence similarities

Belongs to the tyrosinase family.

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Ontologies

Keywords
   Biological processMelanin biosynthesis
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMThioether bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmelanin biosynthetic process from tyrosine

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

monophenol monooxygenase 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

Chain1 – 630630Tyrosinase
PRO_0000186732

Sites

Metal binding691Copper A By similarity
Metal binding921Copper A By similarity
Metal binding1011Copper A By similarity
Metal binding3171Copper B By similarity
Metal binding3211Copper B By similarity
Metal binding3601Copper B By similarity

Amino acid modifications

Cross-link90 ↔ 922'-(S-cysteinyl)-histidine (Cys-His) By similarity

Experimental info

Sequence conflict322 – 33514Missing in EAL91072. Ref.2
Sequence conflict6001E → D in CAC82195. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q8J130-1 [UniParc].

Last modified January 10, 2006. Version 2.
Checksum: 11A769BD9737BF35

FASTA63073,032
        10         20         30         40         50         60 
MSSNKPYVIK GIPVDAGQII PVRRDIDEWY EDTSRQSRIQ LSIFIWALRE FQSIDYKDRL 

        70         80         90        100        110        120 
SYFQIAGIHH FPLITWDEEE PPVPNKPGYC VHNNVTFPTW HRPYMLLFEQ RLFEIMETTI 

       130        140        150        160        170        180 
KETVPESHKQ EWRDAARQWR LPYWDFAKTS GPHATGPLSL PVLCGLANVV ILNPANPETP 

       190        200        210        220        230        240 
IELPNPVYKY RAPDLMGNLD KPFHIPPERI DPDKDDYYPW DKCQATTKYG LLKNNPHIQD 

       250        260        270        280        290        300 
AGQDVTKSNL ALNEHPWYRP NKAGFPPLQT LTYEVHRLLS FKFSSWGAFA STKWCNEENK 

       310        320        330        340        350        360 
PPASQQTRDI LSLEYIHNNV HNWVGGTDYL GDPSKPDLQG AGHMSSVPVA AFDPIFWLYH 

       370        380        390        400        410        420 
NNVDRLTAIW QVLNQDHWFD EPHPSDAKPD DPLKPFHVSK DKYFTSDDAR FWRKYGYDYD 

       430        440        450        460        470        480 
IVKKPGTNED RAPEEVKMKI NQLYGEPISR LHEGQPVEYD YVINVIYDRY ALDGIPYTIV 

       490        500        510        520        530        540 
FYLHLKDGSY KCLGGVYTFS TKLSDAQDTE RGGCDNCREQ KKAGVLASAQ IPLTYTLYER 

       550        560        570        580        590        600 
QEWHNLGKLL PVKETADIIR QHLCWKVVGV NNSILFDSEQ PMRGDPATWR SLDVTAAYSE 

       610        620        630 
IHYPVDRNYK YIDRGLPAYH NYLPIHLSPT

« Hide

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References

« Hide 'large scale' references
[1]"Cloning of a tyrosinase gene of the human pathogenic fungus Aspergillus fumigatus."
Langfelder K., Glaser P., Brakhage A.A.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 46645 / NCPF 2109.
[2]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Af293 / CBS 101355 / FGSC A1100.

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Cross-references

Sequence databases

AJ293806 Genomic DNA. Translation: CAC82195.1.
AAHF01000004 Genomic DNA. Translation: EAL91072.1.
RefSeqXP_753110.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3510142.
KEGGafm:AFUA_1G17430.

Phylogenomic databases

HOGENOMQ8J130.

Enzyme and pathway databases

BRENDA1.14.18.1. 18841.

Family and domain databases

InterProIPR008922. Di-copper_centre.
IPR016216. Monophenol_mOase_fun.
IPR002227. Tyrosinase.
[Graphical view]
Gene3DG3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFPIRSF000340. MPO_fungal. 1 hit.
PRINTSPR00092. TYROSINASE.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameTYRO_ASPFU
AccessionPrimary (citable) accession number: Q8J130
Secondary accession number(s): Q4WR60
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: January 20, 2009
This is version 34 of the entry and version 2 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