ID A0A022R1L7_ERYGU Unreviewed; 594 AA.
AC A0A022R1L7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00497, ECO:0000259|PROSITE:PS00498};
GN ORFNames=MIMGU_mgv1a003279mg {ECO:0000313|EMBL:EYU34166.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU34166.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU34166.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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}.
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DR EMBL; KI630717; EYU34166.1; -; Genomic_DNA.
DR RefSeq; XP_012841283.1; XM_012985829.1.
DR AlphaFoldDB; A0A022R1L7; -.
DR STRING; 4155.A0A022R1L7; -.
DR GeneID; 105961598; -.
DR KEGG; egt:105961598; -.
DR eggNOG; ENOG502QVBP; Eukaryota.
DR OMA; YDENANM; -.
DR OrthoDB; 4070889at2759; -.
DR PhylomeDB; A0A022R1L7; -.
DR Proteomes; UP000030748; 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 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:SF87; POLYPHENOL OXIDASE CHLOROPLASTIC; 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|ARBA:ARBA00023157,
KW 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:UP000030748};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 200..217
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 356..367
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 209
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 328
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 332
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 363
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 101..119
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 118..180
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 183..200
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 594 AA; 65820 MW; 6E4B178F5B0DDBDF CRC64;
MASLHQVLPA AAPSSSSLRS SSSTATRPVV FAKPSHFLTH AKRNHHRRLI SCSSSSSNEG
SKVDRRNMLL GLGGMYGAAN LLSTPDSASA NPIQAPQIDK CGNSTYDTSA GVATQINCCP
PFTGTIIDYK LPNFPKTKVR PSAHRLSPEY LFKFNTAVDR MRRLPKDDPR SFMQQANIHC
AYCNGGYDQP GQGTLDLQVH NGWLFFPFHR WYLYFYERIL GKLIGDPTFA LPFWNWDNPK
GMTIPPAFID PKSALYDAKR NPDNMPPAVV DLGFTGSTDP LQVVSNNLTI MYTEMVRGNS
DVYDFMGKAY REGTPVNPGP GSSERGSHTA IHAFVGDYKN QPAGEDMGNF YSAGRDPLFY
SHHSNVDRMW TLWQFFLPSN KIPDKKITDP DFLNTAFLFY DENAQLVRVT VKDCLDNLKM
GFEYERVDLP WLDYRPPAQA ASAKVTRAGK TTVKVEDTVF PIVLDKIVRV LLPKTKKGKA
DELLVIENIV VDTSKFLKFD VFVNDEDDNV AEIDKASYAG TYAQIPHKTK EKTATTSIRL
KLTDVYEDMD VTDDDTILVT LVPRHEGPGV TIGGIKIIEN PTPAPAAAAA APAS
//
