ID A0A2U1NGK7_ARTAN Unreviewed; 588 AA.
AC A0A2U1NGK7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Cupredoxin {ECO:0000313|EMBL:PWA72644.1};
GN ORFNames=CTI12_AA267190 {ECO:0000313|EMBL:PWA72644.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA72644.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA72644.1, ECO:0000313|Proteomes:UP000245207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC TISSUE=Leaf {ECO:0000313|EMBL:PWA72644.1};
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
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:PWA72644.1}.
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DR EMBL; PKPP01002868; PWA72644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1NGK7; -.
DR STRING; 35608.A0A2U1NGK7; -.
DR Proteomes; UP000245207; 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 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 PANTHER; PTHR11709:SF537; CUPREDOXIN-RELATED; 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.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000245207};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..588
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015763543"
FT DOMAIN 35..149
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 161..315
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 399..535
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 588 AA; 65644 MW; 18235BDBD9E063F6 CRC64;
MAMANTPIFF SCIFLFCILS FTCAEDPTVS YKFEVSYITA SPLGVPQQVI AINGKFPGPT
INSTTNNNVV VNVRNKLDED LLLTWAGIQQ KRSSWQDGVL GTNCPIPPKW NWTYNFQVKD
QIGSYFYFPS LNLQRASGGF GSFIIKPRSV IPIPFDNPAD DITILIGDWY IRNHTALRKT
LDAGRDLGMP DGVLINGKGP YRYNDTLVPD GIDHETINVE PGKTYRIRVS NVGVSTSLNF
RIQSHNLLLA ESEGSYTVQQ NYTSLDIHVG QTYSFLITMD QNASSDYYIV ASARFVNEST
WQRVTGVGVL HYSNSKGKAS GPLPPPPQDQ YDTTYSMNQA RSIRWNVSAS GARPNPQGSF
KYGSINVTDV YILRNKPPVT IDGKRRATLS GISFVKPTTP IRLADEFKVK GAYKLDFPNE
PLTGPSRMET SVINGTYRGF MEVILQNNET KMHSYHMDGY AFFVVGMGYG EWTNDSRGTY
NKWDGIARTT TQVYPGAWTS ILISLDNVGV WNLRTENLDS WYLGQETYVR IVNPEKNNKT
ELPIPDNVLY CGALSRMQKP QDISSALKQH GSMVVLGLLM AMLSVLVL
//
