ID A0A176W6H1_MARPO Unreviewed; 648 AA.
AC A0A176W6H1;
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:PS00497, ECO:0000259|PROSITE:PS00498};
GN ORFNames=AXG93_2865s1100 {ECO:0000313|EMBL:OAE28668.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE28668.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE28668.1, 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:OAE28668.1};
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:OAE28668.1}.
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DR EMBL; LVLJ01001706; OAE28668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176W6H1; -.
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; PS00497; TYROSINASE_1; 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 200..217
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 383..394
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 648 AA; 73497 MW; 04BADB22557AE3C3 CRC64;
MFKCCQPLNR VRYSGWPYIQ KPNSEFAAMA AICRQQIFSS QGEGQGRGNA GVVQMKFLWA
VSMCCALLCI QNFPQRINAE PVLASSLGFC KTVPVLRGAP LHCCLPPPAR KPIRFKFPTC
ANGGPPVMRE RRPAHVVQND PEYVRKYNLA YARMKALPDS DPRSFLNQWR VHCSFCNEAF
KQRETPGPLG KATGVLLQVH YSWTFLPWHR MYLYYHERIL ADLIGDPTFA LPFWNWDNQL
DPIASMMPFM FLPNFPVNNS ALLDVNRNAD HMPPKILYLG YNGKLEAEGK LNLTDEQIRY
ENLCVMYNQV ATKISARSFL GGPYVVGTDN TAASVNVSAG ETPGESGGME IVHNVAHEWT
GLINDPAHPD NEDMGNFIYA ARDPIFYSHH SNVDRLWDVW KTIPDKVTIA GNRKRVDYTS
NDFLDSEFTF FDENQDMVVV KIRDSLDSAK LGYKYTDVSE ADNLWINYEP LPPHKPSQPW
KPSDWPAVVP SGNNTIGKVP ASFKLERRAP TKKDLKGKGL KHTNQLQEDI LLEKVRIPHS
AYARFDVFIN FPEANRETHL YMSEYVGTFT HLPSGMVDMS SSVSQSSVTE SNGKFRFFNI
RYSAGQALRR LGIADWNTDV VVTIVSKGVR KTNPTIDFYF SNIKQDFQ
//
