ID A0A540M063_MALBA Unreviewed; 603 AA.
AC A0A540M063;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00497, ECO:0000259|PROSITE:PS00498};
GN ORFNames=C1H46_022320 {ECO:0000313|EMBL:TQD92088.1};
OS Malus baccata (Siberian crab apple) (Pyrus baccata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=106549 {ECO:0000313|EMBL:TQD92088.1, ECO:0000313|Proteomes:UP000315295};
RN [1] {ECO:0000313|EMBL:TQD92088.1, ECO:0000313|Proteomes:UP000315295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shandingzi {ECO:0000313|Proteomes:UP000315295};
RC TISSUE=Leaves {ECO:0000313|EMBL:TQD92088.1};
RA Chen X.;
RT "Sequencing of a Wild Apple (Malus baccata) Genome Unravels the Differences
RT Between Cultivated and Wild Apple Species Regarding Disease Resistance and
RT Cold Tolerance.";
RL G3 (Bethesda) 9:1785-1793(2019).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|PIRSR:PIRSR000290-1};
CC Note=Binds 2 copper ions per subunit. {ECO:0000256|PIRSR:PIRSR000290-
CC 1};
CC -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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:TQD92088.1}.
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DR EMBL; VIEB01000401; TQD92088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A540M063; -.
DR STRING; 106549.A0A540M063; -.
DR Proteomes; UP000315295; Unassembled WGS sequence.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046148; P:pigment biosynthetic process; 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; IPR016213; Polyphenol_oxidase.
DR InterPro; IPR022740; Polyphenol_oxidase_C.
DR InterPro; IPR022739; Polyphenol_oxidase_cen.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF138; OS04G0624500 PROTEIN; 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 PIRSF; PIRSF000290; PPO_plant; 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 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR000290-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000290-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000290-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000315295};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 211..228
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 369..380
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 50..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 211
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 220
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 342
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 346
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 376
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 115..130
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 129..191
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 194..211
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 603 AA; 66863 MW; 4E02C3B4183C46DA CRC64;
MASMSAPLVT SATSIIPATS LSPFSQKYHR ISSVGNPRHS NLQAVSCKAT NNSSDQNKNP
STSSNNHDHE NPSPVNLDRR NVLIGLGSLY GGVAGLGSDP FAVAKPVSPP DLTKCGPADF
PSGAVPTNCC PPTSQKIVDF KFPSPTKLRV RPAAHAVDKA YIEKYSKAIE LMKALPDDDP
RSFTQQADVH CAYCNGAYDQ VGFPNLELQI HQCWLFFPFH RFYLYFHERI LAKLIDDPTF
ALPFWNWDAP AGMQLPALYA NPDSPLYDEL RAASHQPPTL IDLDFNGTDE TMSKDAQIKA
NLKIMYRQMV SNSKKPLLFF GSPYRAGTEP DPGAGAIEQT PHGPVHTWTG DNTQPNYEDM
GNFYSTARDP IFFAHHLNLD RMWNIWKSIG TKNKDINDKD WLDTGFLFYD ENAELVRVTV
RDTLDNKKLG YTYEDVEIPW LKSRPTPRRT KLARKAKAAG VAKAAETTSS GKVVAGKDFP
INLETKISTV VSRPKPKKRS KKEKEDEEEI LVIRGIELDK DVAVKFDVYV NDVDDEDAAP
SGPDKSEFAG SFVSVPHKQK EKSKSCLRLG LTDLLEDLGA EDNLSTTMGA HSLISDFTCE
FVN
//
