ID A0A540M014_MALBA Unreviewed; 593 AA.
AC A0A540M014;
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_022319 {ECO:0000313|EMBL:TQD92087.1};
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:TQD92087.1, ECO:0000313|Proteomes:UP000315295};
RN [1] {ECO:0000313|EMBL:TQD92087.1, 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:TQD92087.1};
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:TQD92087.1}.
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DR EMBL; VIEB01000401; TQD92087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A540M014; -.
DR STRING; 106549.A0A540M014; -.
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 196..213
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 354..365
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 205
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 327
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 331
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 361
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 100..115
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 114..176
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 179..196
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 593 AA; 65738 MW; DBBB9F6CB939FECF CRC64;
MTSLSPPVVT TPTVPNPATK PLSPFSQNNS QVSLLTKPKR SFARKVSCKA TNNDENDQAQ
SKLDRRNVLL GLGGLYGVAG MGTDPFAFAK PIAPPDVSKC GPADLPQGAA PTNCCPPPST
KIIDFKLPAP AKLRIRPPAH AVDQAYRDKY YKAMELMKAL PDDDPRSFKQ QAAVHCAYCD
GAYDQVGFPE LELQIHNSWL FFPFHRYYLY FFEKILGKLI NDPTFALPFW NWDSPAGMPL
PAIYADPKSP LYDKLRSAQH QPPTLVDLDY NGTEDNVSKE TTINANLKIM YRQMVSNSKN
AKLFFGNPYR AGDEPDPGGG SIEGTPHSPV HLWTGDNTQP NFEDMGNFYS AGRDPIFFAH
HSNVDRMWSI WKTLGGKRTD LTDSDWLDSG FLFYNENAEL VRVKVRDCLE TKNLGYVYQD
VDIPWLSSKP TPRRAKVALS KIAKKLGVAH AAVASSSKVV AGTEFPISLG SKISTVVKRP
KQKKRSKKAK EDEEEILVIE GIEFDRDVAV KFDVYVNDVD DLPSGPDKTE FAGSFVSVPH
SHKHKKKMNT ILRLGLTDLL EEIEAEDDDS VVVTLVPKFG AVKIGGIKIE FAS
//
