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Database: UniProt
Entry: A0A4S2MM39_9PEZI
LinkDB: A0A4S2MM39_9PEZI
Original site: A0A4S2MM39_9PEZI 
ID   A0A4S2MM39_9PEZI        Unreviewed;       361 AA.
AC   A0A4S2MM39;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Di-copper centre-containing protein {ECO:0000313|EMBL:TGZ78102.1};
GN   ORFNames=EX30DRAFT_343491 {ECO:0000313|EMBL:TGZ78102.1};
OS   Ascodesmis nigricans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Ascodesmidaceae; Ascodesmis.
OX   NCBI_TaxID=341454 {ECO:0000313|EMBL:TGZ78102.1, ECO:0000313|Proteomes:UP000298138};
RN   [1] {ECO:0000313|EMBL:TGZ78102.1, ECO:0000313|Proteomes:UP000298138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 389.68 {ECO:0000313|EMBL:TGZ78102.1,
RC   ECO:0000313|Proteomes:UP000298138};
RG   DOE Joint Genome Institute;
RA   Lutkenhaus R., Traeger S., Breuer J., Kuo A., Lipzen A., Pangilinan J.,
RA   Dilworth D., Sandor L., Poggeler S., Barry K., Grigoriev I.V.,
RA   Nowrousian M.;
RT   "Comparative genomics and transcriptomics to analyze fruiting body
RT   development in filamentous ascomycetes.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
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DR   EMBL; ML220145; TGZ78102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S2MM39; -.
DR   STRING; 341454.A0A4S2MM39; -.
DR   InParanoid; A0A4S2MM39; -.
DR   Proteomes; UP000298138; 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; PS00497; TYROSINASE_1; 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:UP000298138};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..361
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5020330816"
FT   DOMAIN          90..107
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          264..275
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   361 AA;  39815 MW;  BA7B069526048CE8 CRC64;
     MKLSTILAGV TTAVGFASAA PVLEARSGTC TNPAVRKEWR NMGVLEKANY LLSVQCLMIK
     PSKLKSQFPN AKTRWDDFIS LHKDVTPQVH FVPQFLTWHR AFLHVFETAL REECFYKYRL
     PYWNMDLDHD NWLASPVLDS ILGFGSNGEE IGGDPNFPGS TGGGCISSGL FKYTRVNIPY
     SDATTPLRAP RCVKRAFLGI NNDLWLTEQA VQNTIANSAT YEEFEAALEG DINFADLSAK
     LGLHNAGHSS VGGDMSDMFI STGDPLFYLH HANVDRIYWL WQQQQSSRHY EVNGALAPRP
     NPMLIWPNPP SGDFTLAYEM LGLMVPGTNT PIQAGMVTNT KGKGVSPPSG GANGLLCYQY
     A
//
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