ID A0A200QGE6_9MAGN Unreviewed; 541 AA.
AC A0A200QGE6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:OVA09457.1};
GN ORFNames=BVC80_7767g6 {ECO:0000313|EMBL:OVA09457.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA09457.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA09457.1, 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:OVA09457.1};
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 -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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:OVA09457.1}.
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DR EMBL; MVGT01002069; OVA09457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200QGE6; -.
DR STRING; 56857.A0A200QGE6; -.
DR InParanoid; A0A200QGE6; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13846; CuRO_1_AAO_like_1; 1.
DR CDD; cd13872; CuRO_2_AAO_like_1; 1.
DR CDD; cd13894; CuRO_3_AAO_like_1; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034273; CuRO_1_AAO-like.
DR InterPro; IPR034271; CuRO_2_AO-like.
DR InterPro; IPR034275; CuRO_3_AO-like.
DR PANTHER; PTHR11709:SF90; L-ASCORBATE OXIDASE; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..541
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012239279"
FT DOMAIN 33..146
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 159..296
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 376..511
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 541 AA; 60180 MW; E741A623862F05E5 CRC64;
MGENRVLCSL FLCFFVISCV NGEDPYRFFS WTVTYGDIYP LGVKQQGILI NGQFPGPQID
SVTNDNLIIS VLNNLTEPFL LSWNGLQQRR NSWQDGVYGT NCPIPPGVNF TYILQVKDQI
GSFFYYPSLA FHKAAGGFGG ITISSRPRIP VPFPPPAGDF TILAGDWFKA NHTDLKAILD
GGHNLPFPDG LLINGRGWNG NTFTVDQGKT YRFRISNVGL TTSINFRIQG HKMKLVEVEG
SHTLQNTYSS LDIHLGQSYS VLVTMDQPGQ DYYIVVSSRF TNPVLTTTSI LHYSNSAGKV
SGPPPGGPTI QIDWSLNQAR SIRWNLTASG PRPNPQGSYH YGLINTTRTI RLANSAPIIS
DKQRYAVNSV SFIPADTPLK IADYFNISGV FYPGSISDNP TGGGGYLQTS VMAADFRAYV
EIVFENSEDT VQSWHIDGYS FFVVGMDGGQ WSPASRLSYN LRDTAARCTV QVYPKSWSAI
YMALDNVGMW NIRSENWARQ YLGQQFYLRV FSPARSWRDE YPIPKNALLC GRASGRKTRP
L
//