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Database: UniProt/TrEMBL
Entry: A1B2I8_PARDP
LinkDB: A1B2I8_PARDP
Original site: A1B2I8_PARDP 
ID   A1B2I8_PARDP            Unreviewed;       165 AA.
AC   A1B2I8;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   03-MAY-2023, entry version 105.
DE   SubName: Full=Superoxide dismutase, copper/zinc binding protein {ECO:0000313|EMBL:ABL69732.1};
GN   OrderedLocusNames=Pden_1634 {ECO:0000313|EMBL:ABL69732.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL69732.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457}.
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DR   EMBL; CP000489; ABL69732.1; -; Genomic_DNA.
DR   RefSeq; WP_011747931.1; NC_008686.1.
DR   AlphaFoldDB; A1B2I8; -.
DR   STRING; 318586.Pden_1634; -.
DR   EnsemblBacteria; ABL69732; ABL69732; Pden_1634.
DR   GeneID; 75501116; -.
DR   KEGG; pde:Pden_1634; -.
DR   eggNOG; COG2032; Bacteria.
DR   HOGENOM; CLU_056632_8_1_5; -.
DR   OMA; KWVAFHV; -.
DR   OrthoDB; 5431326at2; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003:SF71; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..165
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002632256"
FT   DOMAIN          35..164
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          72..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   165 AA;  16864 MW;  E150D14427C6D063 CRC64;
     MRNHLVALGF ALLPISAHAQ DAKATFLDQE GQEAGSAALT ATPSGVLIEV EATGLPASNW
     VAFHIHETGS CDHGTGHESA GGHFNPSGAP HGVLSEGGPH AGDMPNIWVD AEGTARAQVF
     NPMVTLADGD NGIKGRALMI HAGPDDYQTQ PTGAAGDRLA CAVIE
//
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