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Database: UniProt
Entry: A0A1V9YSH7_9STRA
LinkDB: A0A1V9YSH7_9STRA
Original site: A0A1V9YSH7_9STRA 
ID   A0A1V9YSH7_9STRA        Unreviewed;       273 AA.
AC   A0A1V9YSH7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00497};
DE   Flags: Fragment;
GN   ORFNames=ACHHYP_06739 {ECO:0000313|EMBL:OQR88581.1};
OS   Achlya hypogyna.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR88581.1, ECO:0000313|Proteomes:UP000243579};
RN   [1] {ECO:0000313|EMBL:OQR88581.1, ECO:0000313|Proteomes:UP000243579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR88581.1,
RC   ECO:0000313|Proteomes:UP000243579};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
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:OQR88581.1}.
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DR   EMBL; JNBR01001196; OQR88581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9YSH7; -.
DR   STRING; 1202772.A0A1V9YSH7; -.
DR   OrthoDB; 63705at2759; -.
DR   Proteomes; UP000243579; 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:SF124; TYROSINASE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
PE   4: Predicted;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243579}.
FT   DOMAIN          144..161
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OQR88581.1"
FT   NON_TER         273
FT                   /evidence="ECO:0000313|EMBL:OQR88581.1"
SQ   SEQUENCE   273 AA;  29193 MW;  79E67CAD59EA1936 CRC64;
     PTDAPTPVPT TVPTAAPTTV TPAPTDAPTT FTPAPTTVTP APTTVTPAPT TLTPAPTTVT
     PAPTTVTPAP TTVTPAPTTV TPAPTTVTPT TAPPACSRTR RSWDSYTAAE KATYKKAIET
     AMNKGYYETF AKIHRNQMTW YEAHGTCVFL YWHRRFLLGF ENMLRSLGSE FACVTIPYFD
     YVQDSVAFRA GTCKSVSSCS AIARELAGFK ASFSWNRGDW TKAKFTPDMS HVNIKQTVLP
     SGKSLTLADV SSSIEGRVHN SVHNLLGGDM TTA
//
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