ID   A0A166WVH1_9PEZI        Unreviewed;       393 AA.
AC   A0A166WVH1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:KZL76023.1};
GN   ORFNames=CT0861_08365 {ECO:0000313|EMBL:KZL76023.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL76023.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL76023.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL76023.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL76023.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LFIV01000018; KZL76023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166WVH1; -.
DR   STRING; 708197.A0A166WVH1; -.
DR   OrthoDB; 4070889at2759; -.
DR   Proteomes; UP000076552; 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:UP000076552};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..393
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007882019"
FT   DOMAIN          123..140
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          316..327
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   393 AA;  43013 MW;  106F2A988AB2CB08 CRC64;
     MHPVKIMAVL GLSAVASAAP LDTPLEARDA GDILADLQAQ AMENLKAAEA NGTISKRGSC
     NLFNAHVRRD WAAFSTKERK EYISAVQCLL TSPSKSDPSF APGARNRYDD FVAVHINQTR
     SIHGTGNFLT WHRYYTWAYE NALKTECGYK GAQPYWNWFA HTDDPRKSPV YDGSETSLSG
     DGAYVPHNGS VSASPFGEIF VPSGQGGGCV TSGPLVNMTV NLGPVSPGMR GLEANPNGAM
     EYNPRCLRRD LSPFAASTWM TPTNLLNVTI GQASKNIKSF QDELQGRFDQ GFLGMHAAGH
     FVANGDASDL YASPTDPSFF LHHAMVDRVY WLWQALHLWE AFEIAGTITI LNLPPSRDAT
     KEDVIEMGVL TQNRPIKDLL NTIDGSPFCY VYL
//