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Q8J130

- TYRO_ASPFU

UniProt

Q8J130 - TYRO_ASPFU

Protein

Tyrosinase

Gene

tyr1

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 2 (10 Jan 2006)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    2 L-dopa + O2 = 2 dopaquinone + 2 H2O.
    L-tyrosine + O2 = dopaquinone + H2O.

    Cofactori

    Binds 2 copper ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi69 – 691Copper ABy similarity
    Metal bindingi92 – 921Copper ABy similarity
    Metal bindingi101 – 1011Copper ABy similarity
    Metal bindingi317 – 3171Copper BBy similarity
    Metal bindingi321 – 3211Copper BBy similarity
    Metal bindingi360 – 3601Copper BBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. monophenol monooxygenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. melanin biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Melanin biosynthesis

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosinase (EC:1.14.18.1)
    Alternative name(s):
    Monophenol monooxygenase
    Gene namesi
    Name:tyr1
    ORF Names:AFUA_1G17430
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 630630TyrosinasePRO_0000186732Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki90 ↔ 922'-(S-cysteinyl)-histidine (Cys-His)By similarity

    Keywords - PTMi

    Thioether bond

    Structurei

    3D structure databases

    ProteinModelPortaliQ8J130.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tyrosinase family.Curated

    Phylogenomic databases

    eggNOGiNOG68512.
    HOGENOMiHOG000217020.
    KOiK00505.
    OrthoDBiEOG754HZ1.

    Family and domain databases

    Gene3Di1.10.1280.10. 2 hits.
    InterProiIPR016216. Monophenol_mOase_fun.
    IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view]
    PfamiPF00264. Tyrosinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000340. MPO_fungal. 1 hit.
    PRINTSiPR00092. TYROSINASE.
    SUPFAMiSSF48056. SSF48056. 2 hits.
    PROSITEiPS00497. TYROSINASE_1. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8J130-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSNKPYVIK GIPVDAGQII PVRRDIDEWY EDTSRQSRIQ LSIFIWALRE    50
    FQSIDYKDRL SYFQIAGIHH FPLITWDEEE PPVPNKPGYC VHNNVTFPTW 100
    HRPYMLLFEQ RLFEIMETTI KETVPESHKQ EWRDAARQWR LPYWDFAKTS 150
    GPHATGPLSL PVLCGLANVV ILNPANPETP IELPNPVYKY RAPDLMGNLD 200
    KPFHIPPERI DPDKDDYYPW DKCQATTKYG LLKNNPHIQD AGQDVTKSNL 250
    ALNEHPWYRP NKAGFPPLQT LTYEVHRLLS FKFSSWGAFA STKWCNEENK 300
    PPASQQTRDI LSLEYIHNNV HNWVGGTDYL GDPSKPDLQG AGHMSSVPVA 350
    AFDPIFWLYH NNVDRLTAIW QVLNQDHWFD EPHPSDAKPD DPLKPFHVSK 400
    DKYFTSDDAR FWRKYGYDYD IVKKPGTNED RAPEEVKMKI NQLYGEPISR 450
    LHEGQPVEYD YVINVIYDRY ALDGIPYTIV FYLHLKDGSY KCLGGVYTFS 500
    TKLSDAQDTE RGGCDNCREQ KKAGVLASAQ IPLTYTLYER QEWHNLGKLL 550
    PVKETADIIR QHLCWKVVGV NNSILFDSEQ PMRGDPATWR SLDVTAAYSE 600
    IHYPVDRNYK YIDRGLPAYH NYLPIHLSPT 630
    Length:630
    Mass (Da):73,032
    Last modified:January 10, 2006 - v2
    Checksum:i11A769BD9737BF35
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti322 – 33514Missing in EAL91072. (PubMed:16372009)CuratedAdd
    BLAST
    Sequence conflicti600 – 6001E → D in CAC82195. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ293806 Genomic DNA. Translation: CAC82195.1.
    AAHF01000004 Genomic DNA. Translation: EAL91072.1.
    RefSeqiXP_753110.1. XM_748017.1.

    Genome annotation databases

    GeneIDi3510142.
    KEGGiafm:AFUA_1G17430.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ293806 Genomic DNA. Translation: CAC82195.1 .
    AAHF01000004 Genomic DNA. Translation: EAL91072.1 .
    RefSeqi XP_753110.1. XM_748017.1.

    3D structure databases

    ProteinModelPortali Q8J130.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3510142.
    KEGGi afm:AFUA_1G17430.

    Phylogenomic databases

    eggNOGi NOG68512.
    HOGENOMi HOG000217020.
    KOi K00505.
    OrthoDBi EOG754HZ1.

    Family and domain databases

    Gene3Di 1.10.1280.10. 2 hits.
    InterProi IPR016216. Monophenol_mOase_fun.
    IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view ]
    Pfami PF00264. Tyrosinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000340. MPO_fungal. 1 hit.
    PRINTSi PR00092. TYROSINASE.
    SUPFAMi SSF48056. SSF48056. 2 hits.
    PROSITEi PS00497. TYROSINASE_1. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

    Entry informationi

    Entry nameiTYRO_ASPFU
    AccessioniPrimary (citable) accession number: Q8J130
    Secondary accession number(s): Q4WR60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: January 10, 2006
    Last modified: October 1, 2014
    This is version 68 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3