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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//