GenomeNet

Database: UniProt
Entry: K7KJM5_SOYBN
LinkDB: K7KJM5_SOYBN
Original site: K7KJM5_SOYBN 
ID   K7KJM5_SOYBN            Unreviewed;       601 AA.
AC   K7KJM5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00498};
GN   Name=100802763 {ECO:0000313|EnsemblPlants:KRH62648};
GN   ORFNames=GLYMA_04G121700 {ECO:0000313|EMBL:KRH62648.1};
OS   Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH62648};
RN   [1] {ECO:0000313|EMBL:KRH62648.1, ECO:0000313|EnsemblPlants:KRH62648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH62648};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH62648.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH62648}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH62648};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH62648.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH62648.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM000837; KRH62648.1; -; Genomic_DNA.
DR   RefSeq; XP_003522849.1; XM_003522801.3.
DR   AlphaFoldDB; K7KJM5; -.
DR   SMR; K7KJM5; -.
DR   STRING; 3847.K7KJM5; -.
DR   PaxDb; 3847-GLYMA04G14361-1; -.
DR   EnsemblPlants; KRH62648; KRH62648; GLYMA_04G121700.
DR   GeneID; 100802763; -.
DR   Gramene; KRH62648; KRH62648; GLYMA_04G121700.
DR   KEGG; gmx:100802763; -.
DR   eggNOG; ENOG502QVBP; Eukaryota.
DR   HOGENOM; CLU_029668_1_0_1; -.
DR   InParanoid; K7KJM5; -.
DR   OMA; AQQAKVH; -.
DR   OrthoDB; 1026651at2759; -.
DR   Proteomes; UP000008827; 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; 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; 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:UP000008827};
KW   Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT   DOMAIN          359..370
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
FT   REGION          20..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         182
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         203
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         212
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
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         336
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         366
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   DISULFID        106..121
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT   DISULFID        120..183
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT   CROSSLNK        186..203
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ   SEQUENCE   601 AA;  67205 MW;  1A5384F2F62A2C1A CRC64;
     MASISPISFV SAINNVSSNS SNSPSSLHHP FSQIQSAKYR KPKRHHHIPR VTCSDNQKPN
     TSGELVLPHR RNILLGLGGL CGAAATLNNI PFANAAPILG PDLTTCVQAE LPEGVEPTNC
     CPPISTNIID FKFPPSNQPL RVRSAAHLVN KDYLAKYEKA VNLMKNLPSD DPRSFAQQAK
     VHCAYCDGGY HQLGFPDLDL EVHFSWLFFP YHRWYLYFHE RILASLINDP TFALPFWNWD
     APGGMQLPSM YADPKSPLYD SLRNANHQPP TLVNLDFTIE DPNAEANIST NLTTMYRQLV
     SNAKTPTLFF GNPYRAGDQP NPGGGSVEST PHGPVHAWTG DINHPTMEDM GNLYAAARDP
     IFYCHHSNVD RMWSIWKTLG GKRRDLTDPD WLESAFLFYD ENKNLVRVKT KDCLDTRKLG
     YVYQDVDIPW LKSKPTPLRS RAQKVELTPL FGGVAAAHAA ETSRNVKFPL VLDSVVSTVV
     KRPKKSRSKK EKEEKEEILV VEGIEFESST GVKFDVFIND EDDKLVKPDN TEFAGSFVSV
     PHSHEHHKNN KKIVTCLRLG LTDLLEELGA EDDDSVLVTL VPKYGKGRVN IRGIKIDFVS
     D
//
DBGET integrated database retrieval system