Database: RefSeq
Entry: XP_015649518
LinkDB: XP_015649518
Original site: XP_015649518 
LOCUS       XP_015649518             211 aa            linear   PLN 07-AUG-2018
DEFINITION  superoxide dismutase [Cu-Zn], chloroplastic [Oryza sativa Japonica
ACCESSION   XP_015649518
VERSION     XP_015649518.1
DBLINK      BioProject: PRJNA122
DBSOURCE    REFSEQ: accession XM_015794032.2
SOURCE      Oryza sativa Japonica Group (Japanese rice)
  ORGANISM  Oryza sativa Japonica Group
            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
            Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP
            clade; Oryzoideae; Oryzeae; Oryzinae; Oryza.
COMMENT     MODEL REFSEQ:  This record is predicted by automated computational
            analysis. This record is derived from a genomic sequence
            (NC_029263.1) annotated using gene prediction method: Gnomon,
            supported by mRNA and EST evidence.
            Also see:
                Documentation of NCBI's Annotation Process
            Annotation Provider         :: NCBI
            Annotation Status           :: Full annotation
            Annotation Name             :: Oryza sativa Japonica Group
                                           Annotation Release 102
            Annotation Version          :: 102
            Annotation Pipeline         :: NCBI eukaryotic genome annotation
            Annotation Software Version :: 8.1
            Annotation Method           :: Best-placed RefSeq; Gnomon
            Features Annotated          :: Gene; mRNA; CDS; ncRNA
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Oryza sativa Japonica Group"
     Protein         1..211
                     /product="superoxide dismutase [Cu-Zn], chloroplastic"
     Region          61..208
                     /note="Copper/zinc superoxide dismutase (SOD). superoxide
                     dismutases catalyse the conversion of superoxide radicals
                     to molecular oxygen. Three evolutionarily distinct
                     families of SODs are known, of which the
                     copper/zinc-binding family is one. Defects in the...;
     Site            order(63,65,75,77,107..109,170..171)
                     /note="E-class dimer interface [polypeptide binding]"
     Site            order(87,145)
                     /note="P-class dimer interface [polypeptide binding]"
     Site            order(103,105,120,137,140,177)
     Site            order(103,105,120,177)
                     /note="Cu2+ binding site [ion binding]"
     Site            order(120,128,137,140)
                     /note="Zn2+ binding site [ion binding]"
     CDS             1..211
        1 mqailaaama aqtllfsata ppaslfqsps sarpfhslrl aagpagaaaa ralvvadatk
       61 kavavlkgts qvegvvtltq ddqgpttvnv rvtgltpglh gfhlhefgdt tngcistgph
      121 fnpnnlthga pedevrhagd lgnivanaeg vaeativdkq iplsgpnsvv grafvvhele
      181 ddlgkgghel slstgnaggr lacgvvgltp l
DBGET integrated database retrieval system