ID A0A162K920_CORDF Unreviewed; 585 AA.
AC A0A162K920;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=LEL_05516 {ECO:0000313|EMBL:OAA78693.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA78693.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA78693.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA78693.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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 -!- 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:OAA78693.1}.
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DR EMBL; AZHF01000003; OAA78693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162K920; -.
DR STRING; 1081108.A0A162K920; -.
DR OrthoDB; 1908494at2759; -.
DR Proteomes; UP000076881; 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:SF76; TYROSINASE; 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 3: Inferred from homology;
KW Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881}.
FT DOMAIN 285..303
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 532..543
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 585 AA; 66774 MW; 63D4D98D69B4E496 CRC64;
MDQFDNLSHL TRPQVEKLPR LNQPPRINTS YAVKCETQAS VSASIEELGA VTWFKTPPLT
AETIGMLRAV KLFAESHDQG AVSGLVPGIW TWFQLAIFSD QNATSPKRGR DEQELVVTSH
SNKAGTTEFE WLEGATFDTR RKLVKGLDQP GNVIGVRLCA RFRGWEIFAA NGYLVLDIGE
DNHTVPITPS PIDTEKSIPV RQCVQKWYKK SKTCHETGLQ VSLFIRAMRA FQSLPPENQL
SYYRIAAIHG EPSNVPWNME KPVIALDDPK KNDLLEQAQG GWYCHHNDDL FPTWHRAYMM
LFEDIAASER PDDGRSQNPR RRIRRMDHGR TSLAFAILGR ASDPTLPEIA SEKTIRVIKS
WKRHGEPQME ILDNPMYRFQ MPGGKPMGDV AYGNFRIQIK EPDPDDGPWE ECIGTSRHSI
TDDDPERRWV QGESDAAKVN ASLQGTGEKK HHRTLRDSVF RLLTKEYATK YVPFASTKYQ
PKNTEEEKAS ANDVKFFLNL EQVHNNIHTY VGGEKTQGGG GHMSAVPVAA FDPVFWLHHC
NIDRIFHLWQ TVKPRNWFRQ KDEEVEFSPQ RELIPFHASD DNKHR
//
