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Database: UniProt
Entry: A0A168FCP7_9HYPO
LinkDB: A0A168FCP7_9HYPO
Original site: A0A168FCP7_9HYPO 
ID   A0A168FCP7_9HYPO        Unreviewed;       392 AA.
AC   A0A168FCP7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Tyrosinase central domain protein {ECO:0000313|EMBL:KZZ99727.1};
GN   ORFNames=AAL_02299 {ECO:0000313|EMBL:KZZ99727.1};
OS   Moelleriella libera RCEF 2490.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX   NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ99727.1, ECO:0000313|Proteomes:UP000078544};
RN   [1] {ECO:0000313|EMBL:KZZ99727.1, ECO:0000313|Proteomes:UP000078544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ99727.1,
RC   ECO:0000313|Proteomes:UP000078544};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ99727.1}.
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DR   EMBL; AZGY01000003; KZZ99727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168FCP7; -.
DR   STRING; 1081109.A0A168FCP7; -.
DR   OrthoDB; 4070889at2759; -.
DR   Proteomes; UP000078544; 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:SF141; N-ACETYL-6-HYDROXYTRYPTOPHAN OXIDASE IVOB-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:UP000078544};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..392
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007896862"
FT   DOMAIN          125..142
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          315..326
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
FT   REGION          230..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   392 AA;  44361 MW;  E501963E63F80701 CRC64;
     MLKTWIFLIL PLAATAHPYQ TEPQGNKVKQ QGIEPPQAFK DINNQYRATM KSVIANRPNK
     GCNRKNIRVR RSWESMKTGE RLDYIRAVKC LHQKQSQADP GVASGIRNRY DDFTYSHMNQ
     SLRMHESGLF LPWHRYFVWA YEKALREECG YKGSQPYWDS ARWTDNQLAS PLFDGSPTSL
     GGNGENINQG QSVFTLPLLP ATINITNSPT TGGGCVTTGP LLPWTVSLGP VTTSSTTPQR
     DPLGRDYNPR CLTRGFRPED SRRALNWENF LRLLRAQNIA EFRPVLMEGR DPGIHVPHHT
     ALGGDVDDIF SSPNDPAFYF LHAQIDRLWT LWQGLDWQGR RDALNGTGTF QNLPPTPEIT
     LDSWMEMVYA GGRVRVSDGM STVDGPLCYV YQ
//
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