ID A0A314YMJ2_PRUYE Unreviewed; 329 AA.
AC A0A314YMJ2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Superoxide dismutase copper chaperone {ECO:0000256|ARBA:ARBA00032899};
GN ORFNames=Pyn_09362 {ECO:0000313|EMBL:PQQ09142.1};
OS Prunus yedoensis var. nudiflora.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=2094558 {ECO:0000313|EMBL:PQQ09142.1, ECO:0000313|Proteomes:UP000250321};
RN [1] {ECO:0000313|EMBL:PQQ09142.1, ECO:0000313|Proteomes:UP000250321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jeju island {ECO:0000313|Proteomes:UP000250321};
RC TISSUE=Leaf {ECO:0000313|EMBL:PQQ09142.1};
RA Baek S., Kim J.-H., Choi K., Kim G.-B., Cho A., Jang H., Shin C.-H.,
RA Yu H.-J., Mun J.-H.;
RT "Draft genome of wild Prunus yedoensis var. nudiflora.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: In the C-terminal section; belongs to the Cu-Zn superoxide
CC dismutase family. {ECO:0000256|ARBA:ARBA00025798}.
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:PQQ09142.1}.
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DR EMBL; PJQY01000640; PQQ09142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A314YMJ2; -.
DR STRING; 2094558.A0A314YMJ2; -.
DR Proteomes; UP000250321; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003:SF86; COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Reference proteome {ECO:0000313|Proteomes:UP000250321};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..329
FT /note="Superoxide dismutase copper chaperone"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016437721"
FT DOMAIN 97..160
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 329 AA; 34706 MW; 58CAB3E366710AAF CRC64;
MAFLRSVATT TAIAASALPA AFALSPLSSS SSSSSSPSQS FRFPKPQNLS FLFSTPSLNP
NRSCLATSFT NSPSAIHMDA PTSEQKPSHQ SDAALPELLT EYMVDMKCEG CVNSVKNKLQ
TVDGVKSVEV DLNSQVVRIL GSTPVKTMTE ALEQTGRKAR LIGQGIPEDF LVSAAVAEFK
GPDIFGVVRL AQVNMELARI EANFSGLPPG KHGWSINEFG DVTEGAASTG KVFNPSKEEA
NEPLGDLGTL DADENGNAFF SGVKEKLRVA DLIGRSLVVY GTADKSDSGI KAAVIARSAG
VGKNYKKLCT CDGTTIWEAT GNDFVTSKV
//