ID A0A5N6LXI7_9ASTR Unreviewed; 611 AA.
AC A0A5N6LXI7;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00497, ECO:0000259|PROSITE:PS00498};
GN ORFNames=E3N88_34240 {ECO:0000313|EMBL:KAD3066360.1};
OS Mikania micrantha.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Eupatorieae; Mikania.
OX NCBI_TaxID=192012 {ECO:0000313|EMBL:KAD3066360.1, ECO:0000313|Proteomes:UP000326396};
RN [1] {ECO:0000313|EMBL:KAD3066360.1, ECO:0000313|Proteomes:UP000326396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLD-2019 {ECO:0000313|EMBL:KAD3066360.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAD3066360.1};
RA Liu B.;
RT "Mikania micrantha, genome provides insights into the molecular mechanism
RT of rapid growth.";
RL Submitted (MAY-2019) 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 -!- 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:KAD3066360.1}.
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; SZYD01000017; KAD3066360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6LXI7; -.
DR Proteomes; UP000326396; Miscellaneous, Linkage group lg7.
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:SF97; TYROSINASE COPPER-BINDING DOMAIN-CONTAINING 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:UP000326396};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 206..223
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 373..384
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT BINDING 183
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 206
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 215
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
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 350
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 380
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 102..122
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 121..184
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 187..206
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 611 AA; 68355 MW; 69117C5BDACBE2BC CRC64;
MSSSSLLPLI SSFTSLPSTN TNRAINTKTN QAQGFRVSCN QTPDNHNDKK LVLPQAQKLV
IPNVDRRNLL VGLGGLYTAT NLTSMPSALA APITAPDITS ICKDAGAGVN DKENAVRTLK
CCPPSLGKPI KDFVFPTDKK VRMRWPAHTG TKEQVDKYRA AIQAMRDLPD DHPHSFVNQA
KIHCAYCNGG YTQVDSGFPD IDIQIHNSWL FFPFHRWYLY FYERILGKLI KDPDFALPFW
KWDEPAGMPI PEMFVPETID GKPNSLYDVY RDANHIKARI VDLDYDGKDK DIPDKQQVLC
NLSTVYRDLV RNGGDTLSFF GGVYVAGDDP VANGAQSVGS VEAGSHTAVH RWVGDPNQPN
NEDMGNFYSA GYDPAFYIHH SNVDRMWKLW KELSLPGHVD PTETDWLDAS YVFYDENEDL
VRVYNRDSVS LDKLKYNYIE NSKEVFPWRN SRPAKRNKSL QTATTSDVKK VDQIKFPVKL
DKILKVSVKR PAVNRSAEEK AKANEVLAIK GIRYDSGKFV KFDVFVNDKL KDGVFTTPCD
PEYAGGFAQI PHSGMKNMFM GSSARFGLTE LLEDTNTDGD EYATVTLVPR TGCEDLTVGN
IEIILVPVAA V
//
