ID   A0A395HF45_9EURO        Unreviewed;       341 AA.
AC   A0A395HF45;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Tyrosinase {ECO:0000313|EMBL:RAL04854.1};
GN   ORFNames=BO80DRAFT_346666 {ECO:0000313|EMBL:RAL04854.1};
OS   Aspergillus ibericus CBS 121593.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL04854.1, ECO:0000313|Proteomes:UP000249402};
RN   [1] {ECO:0000313|EMBL:RAL04854.1, ECO:0000313|Proteomes:UP000249402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL04854.1,
RC   ECO:0000313|Proteomes:UP000249402};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ824423; RAL04854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395HF45; -.
DR   STRING; 1448316.A0A395HF45; -.
DR   VEuPathDB; FungiDB:BO80DRAFT_346666; -.
DR   OrthoDB; 4070889at2759; -.
DR   Proteomes; UP000249402; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF141; N-ACETYL-6-HYDROXYTRYPTOPHAN OXIDASE IVOB-RELATED; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..341
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017250873"
FT   DOMAIN          111..128
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          259..270
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   341 AA;  38455 MW;  46030AEEEF2193B9 CRC64;
     MKFSSFAAAL ALAASASAAA LPHASSNLDR RDATSHEISG FFSKSCTREK MTVRKEWRNL
     TKKQQDSFLD SIQCLMDKPA KSGLTATTSR FSDLQALHRG MTNTAYADII HHVGQFLPWH
     RYYMHIYETL LRDECGYNGP LPWWDEQKDA DSGNMWQSSM WGADAFGGNG TGSDLCVRDG
     RFSNYTLHIG PGDEDTDYCL RRAWDTENVI ANANSTSLDM CNAYNTFSPW WDCISNIPHK
     GVHTYIGGVM ADIKSSPGDP IFFMHHVYID RVWWLWQKQD PINRLYDISG PTLNHTANVE
     PAGGWQNATL HYELSSFNIM PNTTIAHVMN TQGGYLCYGY E
//