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Database: UniProt
Entry: A0A179IMT0_CORDF
LinkDB: A0A179IMT0_CORDF
Original site: A0A179IMT0_CORDF 
ID   A0A179IMT0_CORDF        Unreviewed;       619 AA.
AC   A0A179IMT0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE            EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN   ORFNames=LLEC1_07414 {ECO:0000313|EMBL:OAR03172.1};
OS   Cordyceps confragosa (Lecanicillium lecanii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces.
OX   NCBI_TaxID=2714763 {ECO:0000313|EMBL:OAR03172.1, ECO:0000313|Proteomes:UP000243081};
RN   [1] {ECO:0000313|EMBL:OAR03172.1, ECO:0000313|Proteomes:UP000243081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UM487 {ECO:0000313|EMBL:OAR03172.1,
RC   ECO:0000313|Proteomes:UP000243081};
RA   Jackson D., Zemenick K.A., Malloure B., Quandt C.A., James T.Y.;
RT   "Fine-scale spatial genetic structure of a fungal parasite of coffee scale
RT   insects.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504,
CC         ChEBI:CHEBI:57924; EC=1.14.18.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000426};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924,
CC         ChEBI:CHEBI:58315; EC=1.14.18.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001038};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
CC   -!- SIMILARITY: Belongs to the tyrosinase family.
CC       {ECO:0000256|ARBA:ARBA00009928}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAR03172.1}.
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DR   EMBL; LUKN01000285; OAR03172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A179IMT0; -.
DR   OMA; WNSEMAN; -.
DR   OrthoDB; 1908494at2759; -.
DR   Proteomes; UP000243081; Unassembled WGS sequence.
DR   GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
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; IPR041640; Tyrosinase_C.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF76; TYROSINASE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF18132; Tyosinase_C; 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   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243081};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..619
FT                   /note="tyrosinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008104597"
FT   DOMAIN          123..140
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          323..334
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
FT   REGION          230..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   619 AA;  68371 MW;  A36F5AA2991E3A74 CRC64;
     MRSVTYTAVI LALAFDGLVA LGQSYDFGPA AVVSRAATAK LTVTQSLPPR DDGSTPYREE
     IRDLAANKHK WDLFILALSS LMSVSQDDAS SYYQIAGIHG APFQPYNGVT AFGRNVQSGY
     CMHNSVLFPT WHRPYLSLFE TRMYALANTI AAQFGDDEAD EYQKAAAEFR VPYWDWSSYA
     PAGESHFPDV FWNAKISQYG PNGLQTIKNP LYSYQFRPLD SRALSISPLN RWPETKRSPD
     TRYSDPPSDN SQVSSAMYRR TPQIQQRLYN MYSSYNDYQS FSNKAWATEN NRYADSIESL
     HDLVHTYTGL GGHMAYIPIA AFDPLFFLHH ANVDRLVAIW QVLNNDSWIS PMRAEEQTFA
     APRGTWQDGS TPLYPFAASD NGDMWTSDMA RSTESFGYTY ADTDAQAGDL RASLIRKINQ
     WYGGHSPANM KVSRVRHRAP DSMPHANGSA AIFNVAPGAK APAISKVVEN NQYTEWTARI
     IVNVEALDGV LGIHLFMGEP PANAADWETA AHLVGTAAIP GMGSSTGSAA RVSSVIPLTS
     SLMKLVAAGQ VPSLDPESVV PFLKRNLRFS ALDRHNNMAN ETMMSGLQIG IDSASVRMPA
     SAEELPQWGT TVTRIDLLE
//
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