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Database: UniProt
Entry: A0A3L6S9V4_PANMI
LinkDB: A0A3L6S9V4_PANMI
Original site: A0A3L6S9V4_PANMI 
ID   A0A3L6S9V4_PANMI        Unreviewed;       587 AA.
AC   A0A3L6S9V4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Monocopper oxidase-like protein SKU5 {ECO:0000313|EMBL:RLN17807.1};
GN   ORFNames=C2845_PM02G25930 {ECO:0000313|EMBL:RLN17807.1};
OS   Panicum miliaceum (Proso millet) (Broomcorn millet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX   NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN17807.1, ECO:0000313|Proteomes:UP000275267};
RN   [1] {ECO:0000313|Proteomes:UP000275267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA   Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA   Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA   Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT   "The genome of broomcorn millet.";
RL   Nat. Commun. 10:436-436(2019).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
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:RLN17807.1}.
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DR   EMBL; PQIB02000005; RLN17807.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L6S9V4; -.
DR   STRING; 4540.A0A3L6S9V4; -.
DR   Proteomes; UP000275267; Chromosome 2.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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   PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR   PANTHER; PTHR11709:SF58; SKU5 SIMILAR 3; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..587
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018216518"
FT   DOMAIN          31..144
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          157..311
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          396..531
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   587 AA;  65172 MW;  8D9F332AA1AE291F CRC64;
     MPPLLLLLLL LAASPAPARA GDPYAYYDWE VSYVSAQPLG VKQKVIGING QFPGPPLNVT
     TNWNVVVNVR NALDEPLLLT WNGVQQRKTA WQDGVLGTNC AIPAGWNWTY TFQVKDQVGS
     FFYFPSTPLH RAAGGYGAIT INNRDVIPIP FGFPDGDITL FIGDWYNRGH KELRRALDGG
     NLLGAPDGVL INGLGPYQYN ESVVPPGIVY ERINGEPGKT YRFRVHNVGV STSLNFRIQN
     HNLLLVETEG SYTSQQNYTN LDIHVGQSYS FLVTMDQNAS TDYYVVASAR FVDAVVVDKL
     TGVAILHYSN SQGPASGPLP DPPNDQYDTA FSINQARSIR WNVTASGARP NPQGSFHYGD
     ITVTDVYLLQ SRPPELIDGK LRSTLNEISY IAPSTPLVLA QLFNVPGVYK LDFPNHPMNR
     LPKVDTSIIN GTYKGFMEII FQNNATTVQS YHLDGYAFFV VGMDYGLWTE NSRGTYNKWD
     GVARSTIQVF PGAWTAILVF LDNAGIWNLR VQNLDTWYLG QEVYINVVNP EDNSSTLPDN
     AIFCGALSSL QKEQSHRFVY SEASLVAPWR NTVSLLFLLA SFTIWLQ
//
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