ID A0A200R7R5_9MAGN Unreviewed; 590 AA.
AC A0A200R7R5;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Tyrosinase {ECO:0000313|EMBL:OVA18745.1};
GN ORFNames=BVC80_1831g313 {ECO:0000313|EMBL:OVA18745.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA18745.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA18745.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA18745.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
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:OVA18745.1}.
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DR EMBL; MVGT01000435; OVA18745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200R7R5; -.
DR STRING; 56857.A0A200R7R5; -.
DR InParanoid; A0A200R7R5; -.
DR OrthoDB; 4070889at2759; -.
DR Proteomes; UP000195402; 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 Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR022740; Polyphenol_oxidase_C.
DR InterPro; IPR022739; Polyphenol_oxidase_cen.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF76; TYROSINASE; 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 PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..590
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013052460"
FT DOMAIN 341..352
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 590 AA; 67518 MW; 6EC7B404AAB9345A CRC64;
MDAKRWVCLV LFAFFFLGLS SDLIPRDSQQ VQVVSFMSEV KITILGIVYG AWPSMESSTL
NQQSSTTDEQ NNPPSIVVLS PNLTTCHRSL SDADVPVYCC PPKRESEEPF IDFQFPDTSI
PVRVRKPAHL ADADYIAKYN KAIAIMKSLP YSDPRSWLRQ ANMHCIYCTG AYNQQHSNSL
LKIHRSWMFF PWHRMMIYFH ERILGSLIGD ENFALPFWNW DAPEGMFIPD MYTNGSFVDT
QRDSSHLPPQ VADINYDYVE SGLGTEDQIA TNVAFMYNQM VSGAKKTELF MGCSYKAGED
GFCDGPGTIE LAPHNALHTW VGSNLNPERE NLGAFYSAAR DPVFYAHHSN IDRLWEAWKG
LRNYKPEIVD PEWLDSYFFF HNEKSQLVRI KIRDVLDITK LRYTYEKVEN VWLNARPKPS
VPPKIARHIL KMRENENQLL QDSNQAVVTP DLGGRTLDTT IRVKVHRPKT NRSKTEKEEE
EEVLVVYGIE IKKDMYVKFD VYINAVDETI IGPESREFAG TFVNMKRGVR LVMNKGDAVV
KRKTILKLGI SELLDDLEAD GDESIWVTLV PRGGTCVNTT VDGVRIEYMR
//