ID A0A0S3RT50_PHAAN Unreviewed; 568 AA.
AC A0A0S3RT50;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00498};
GN Name=Vigan.04G100500 {ECO:0000313|EMBL:BAT83783.1};
GN ORFNames=VIGAN_04100500 {ECO:0000313|EMBL:BAT83783.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT83783.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT83783.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015037; BAT83783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RT50; -.
DR Proteomes; UP000291084; Chromosome 4.
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; IPR013788; Hemocyanin/hexamerin.
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; PS00210; HEMOCYANIN_2; 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:UP000291084};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 336..347
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT BINDING 157
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
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 188
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 309
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 313
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 343
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 77..93
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 92..158
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 161..179
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 568 AA; 65214 MW; 4E9C160954B1B26B CRC64;
MNTPSKLLPL FFALILFLIL SISLLNTDFS LFTAIKIICR RTYKPSHGLA TTSNQRDRNI
DHSSSISRAI SPNISECFPA GLPSNAITDT DCCPSKPSFS KLIDFKDFAS PNATPRVRRP
FHLLDEEYIA KFEKGIALMK GLPDDDPRSF IQQAKVHCAY CNGAYHLYHP FQDTKLDIHR
SWFFFPFHRW YIYFFERILG NLIGDPDFAL PFWNWDSIEA MHMPSCFTNP NSSLFHELRN
QKHLPPHVID LNYAAGNVDV PSHQQVLYNL ATMYKQMVLA STTELFMGSP FRLGDNPHPG
IGSVEAAPHN TVHTWVGGAD TPHHEDMGTF YTAARDPIFY GHHSNLDRMW AIWKTLGEGR
REYSDQDWLD SEFFFYDENA DFVRVKVRDC IDTKNLGYVY QDVDLAWLRT PPTSRKSKLL
RQKKKAQVLS WKPRKLPLVL DSITSVIVKR PKKLRSREEK EEEEEVLVIE GIEFGSDKYV
KFDVHVDDDE ERLSDPDETE FVGSFVHLYH GHGHNISTSF KVGLSKVLEN LEAEEDDDVL
VTLVPRVGKG EVTLGNIKIE FIPREPKD
//
