ID A0A445AXL4_ARAHY Unreviewed; 541 AA.
AC A0A445AXL4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=L-ascorbate oxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Ahy_B01g055976 {ECO:0000313|EMBL:RYR31185.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR31185.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR31185.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR31185.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:RYR31185.1}.
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DR EMBL; SDMP01000011; RYR31185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445AXL4; -.
DR STRING; 3818.A0A445AXL4; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000289738; Chromosome b01.
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:SF11; L-ASCORBATE OXIDASE HOMOLOG; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..541
FT /note="L-ascorbate oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019051399"
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..514
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 541 AA; 61112 MW; 77E0C95ADA2F2ECA CRC64;
MRPCILLFSS LILLLLSCSV NSEDPYRFFT WKVTYGDIYP LGVKQQGILI NGQFPGPHID
AVTNDNLVIS VYNYLREPFL ISWNGLQHRR NSWQDGVSGT NCPIPPGRNF TYNIQVKDQI
GSFFYFPSLG MHKAAGAFGA IRIWSRPKIP VPFPPPAGDF YILAGDWFKL DHHRLRRLLE
NGHNLPFPDG LLINGRGWNG NTFTVDQGKT YRFRISNVGL TTSINFRIQG HKMKLVEVEG
SHTLQNTYSS LDIHLGQSYS VLVTADQPPK DYYIVVSTRF TRRVLTTTSV LHYSNSHTGV
SGPVPGGPTT DIVSSVFQAR SIRWNLTASG PRPNPQGSYH YGMIIPTRTI MLANSAPYIN
GKQRFAVNSV SYVQPDTPLK LADYFNIGGV YWVGSMPTNP TGGNGYLQTA VMGANFHEFV
EIVFQNWEDT VQSWHIDGYS FFVVGFGSGQ WTVNSRGSYN LRDTVARCTT QVYPRSWTAI
YMPLDNVGMW NIRSENWARQ YLGQQFYLRV YTPSGSWRDE YPVPKNALLC GRATGRRTRP
F
//