ID   A0A176WCF4_MARPO        Unreviewed;       659 AA.
AC   A0A176WCF4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00498};
GN   ORFNames=AXG93_3943s1190 {ECO:0000313|EMBL:OAE30888.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE30888.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE30888.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE30888.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAE30888.1}.
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DR   EMBL; LVLJ01001228; OAE30888.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176WCF4; -.
DR   OrthoDB; 314332at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0004097; F:catechol oxidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR022740; Polyphenol_oxidase_C.
DR   InterPro; IPR022739; Polyphenol_oxidase_cen.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF76; TYROSINASE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF12142; PPO1_DWL; 1.
DR   Pfam; PF12143; PPO1_KFDV; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW   Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT   DOMAIN          398..409
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   659 AA;  75832 MW;  078100DF4128602D CRC64;
     MQERRSWNYG VLGLKIKPSI PSCWYLKAES RELLYAQSSA VKMGDRAIQK ESWGRSRASL
     GVVATGRKLV WASFLCSIVL VLQYLAQPAS ADPVLATSIG QCNPVALQAT NDSKTRTEQC
     CLPAPKRARI PFKLPKVHRL RIRRPAHELA NDVVYVNKYN LAHEKMNALP PDDPRSFLRQ
     WHAHCSFCKS AFLQRRLNNS TTGYPLQLHY SWTFLPWHRM LIYFHEKILG SLINDPDFTL
     PFWNWDNQLD DTAGQIPQIF LPYKQFARKK HGRHGKIRNT FLYEGKRRNP NHMPPKILPL
     TFDRKLEKER ANWTHSQIRH ANLGQVYQMV YNKVSAREYM GGPYNTNSNF TEVADVNVGE
     SGGAESLHNT AHEWVGNLDN SAYPDNEDMG VFTYAGRDPI FYSHHANVDR LWHVWKGLPD
     NITRDGHRIR KDYDDYDFLE TEFTFFDENA DMVVVKVKDT LDIHKLGYKY KSMREADSLW
     INHKPNGTKA SYKRSEVVVS ISNTIGRQPT SFKLRRRAPT AADLPGTQAL NVQQLSEGVV
     FEHVRVPEYM YVRFDVFLDL PTATAETDED ESAYVGTFTH LPSGVMTVED VGQKKVHVRN
     DDMYRTLNIR FSTSLALKAL GITGWNTEIT VTVVPRFRPH GYGWNIKGIK FDCLRQEFT
//