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Database: UniProt
Entry: A0A074WJS2_9PEZI
LinkDB: A0A074WJS2_9PEZI
Original site: A0A074WJS2_9PEZI 
ID   A0A074WJS2_9PEZI        Unreviewed;       390 AA.
AC   A0A074WJS2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Di-copper centre-containing protein {ECO:0000313|EMBL:KEQ70067.1};
GN   ORFNames=M436DRAFT_66478 {ECO:0000313|EMBL:KEQ70067.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ70067.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ70067.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ70067.1,
RC   ECO:0000313|Proteomes:UP000027730};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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DR   EMBL; KL584718; KEQ70067.1; -; Genomic_DNA.
DR   RefSeq; XP_013424360.1; XM_013568906.1.
DR   AlphaFoldDB; A0A074WJS2; -.
DR   STRING; 1043004.A0A074WJS2; -.
DR   GeneID; 25414053; -.
DR   HOGENOM; CLU_035914_0_0_1; -.
DR   OrthoDB; 4070889at2759; -.
DR   Proteomes; UP000027730; 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:SF125; TYROSINASE COPPER-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..390
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001701532"
FT   DOMAIN          114..131
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          308..319
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   390 AA;  42348 MW;  87B6E55369EBFBB5 CRC64;
     MHFSILATAV SLLCASATAF TPASTSGTDK LNDHGMTKLK TYLHKNRGQN TCNLDTAVKR
     QEWSTLSNAN KKKYINAVLC LQSKPAKSGS IAPGAKSRYD DFLATHINQT LTIHGTGNFL
     SWHRYYTYTF EEALRNECGY RGYLPYANWG KYAEDLLNSP IFDGSAYSIS GNGEYRNYSG
     AFIPSEATPL IHLPAGSGGG CVTTGPFKDM TVNLGPVAPV FTDVPPNPRP DGLGYNPRCL
     RRDVGAYAAS IASTDANSTD LIRQNSYIGD FQTVMQGDFA AGLLGVHTAG HYFAGGDGGG
     DIFVSPSDPW FWLHHAQIDR TWWIWQNQDP ASRSTAKGNN SLAGTITLNN LPPSRNTRLD
     DVIDLGVNAK SILVEDVLST TSGPFCYVYV
//
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