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Database: UniProt
Entry: A0A507F691_9FUNG
LinkDB: A0A507F691_9FUNG
Original site: A0A507F691_9FUNG 
ID   A0A507F691_9FUNG        Unreviewed;       590 AA.
AC   A0A507F691;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00498};
GN   ORFNames=CcCBS67573_g06102 {ECO:0000313|EMBL:TPX71632.1};
OS   Chytriomyces confervae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC   Chytriomycetaceae; Chytriomyces.
OX   NCBI_TaxID=246404 {ECO:0000313|EMBL:TPX71632.1, ECO:0000313|Proteomes:UP000320333};
RN   [1] {ECO:0000313|EMBL:TPX71632.1, ECO:0000313|Proteomes:UP000320333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 675.73 {ECO:0000313|EMBL:TPX71632.1,
RC   ECO:0000313|Proteomes:UP000320333};
RX   PubMed=31209237; DOI=.1038/s41598-019-45128-9;
RA   van de Vossenberg B.T.L.H., Warris S., Nguyen H.D.T.,
RA   van Gent-Pelzer M.P.E., Joly D.L., van de Geest H.C., Bonants P.J.M.,
RA   Smith D.S., Levesque C.A., van der Lee T.A.J.;
RT   "Comparative genomics of chytrid fungi reveal insights into the obligate
RT   biotrophic and pathogenic lifestyle of Synchytrium endobioticum.";
RL   Sci. Rep. 9:8672-8672(2019).
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:TPX71632.1}.
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DR   EMBL; QEAP01000245; TPX71632.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A507F691; -.
DR   STRING; 246404.A0A507F691; -.
DR   Proteomes; UP000320333; 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   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   4: Predicted;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000320333};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..590
FT                   /note="Tyrosinase copper-binding domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5021418032"
FT   DOMAIN          257..268
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   590 AA;  63715 MW;  9990A4C2C1FBDA43 CRC64;
     MKLLALLVVA GHALAQCTNP RVRQEWNTLS SSDKAAFVAA CAALAKRPLS NQYADPSIMS
     WHDFVVTHSE NAFWSHVRAV RCDSTTITKP AVALQGNAQF YPYHRAMVWQ FEKAIISTGL
     WPASKGIPYW DWSAVSQNWW TSDVFSPSYF GSASSSDPDI CVVDGAFAKG VYSVAPDALK
     NRKITTGDLT CLRRNGGQYV LPDATSMQDA LSASSYLQFT CQDPNTYYDL SNYHASGHGT
     IGGPGSDLAD ASVSPNDPIF WLHHGFVDKY WFRWQSQCPQ FKFDYTGVLK RQDATGLTDS
     SPYANLDSWP FTVQQMMDVQ GDTLCYTYGP SKGDLPASSP PACPAVKPLA AQTGTASSSA
     STTGTAKSGV DDIWLRSMFV KLVKTPSLGS FNAGTSAAGS AGIDAAGGGD SGAIIIMGRD
     NTTDQDAGAG TVAVSATGTV PATQTATVVA TSSAVASEEA VSKVDEGYIE TQLPDGSTLV
     SYTHFNHTVQ IPATHEVFLV FSRSVAAIDK KTYKKKRFFS PLEPQEYSQP ANYTDLSNEP
     GRCWLKYPQR VPESYLAGMN MDVAMYNNVY NLQMMAIDKF NMESGTSPSC
//
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