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Database: UniProt
Entry: A0A0T5NUE4_9RHOB
LinkDB: A0A0T5NUE4_9RHOB
Original site: A0A0T5NUE4_9RHOB 
ID   A0A0T5NUE4_9RHOB        Unreviewed;       176 AA.
AC   A0A0T5NUE4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Superoxide dismutase {ECO:0000313|EMBL:KRS12255.1};
GN   ORFNames=XM53_11400 {ECO:0000313|EMBL:KRS12255.1};
OS   Roseovarius atlanticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1641875 {ECO:0000313|EMBL:KRS12255.1, ECO:0000313|Proteomes:UP000051295};
RN   [1] {ECO:0000313|EMBL:KRS12255.1, ECO:0000313|Proteomes:UP000051295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R12B {ECO:0000313|EMBL:KRS12255.1,
RC   ECO:0000313|Proteomes:UP000051295};
RA   Li G., Lai Q., Shao Z., Yan P.;
RT   "The draft genome sequence of Roseovarius sp.R12b.";
RL   Submitted (APR-2015) 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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457}.
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:KRS12255.1}.
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DR   EMBL; LAXJ01000010; KRS12255.1; -; Genomic_DNA.
DR   RefSeq; WP_057793401.1; NZ_LAXJ01000010.1.
DR   AlphaFoldDB; A0A0T5NUE4; -.
DR   STRING; 1641875.XM53_11400; -.
DR   PATRIC; fig|1641875.4.peg.63; -.
DR   OrthoDB; 5431326at2; -.
DR   Proteomes; UP000051295; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
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; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..176
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006663919"
FT   DOMAIN          44..171
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   176 AA;  17833 MW;  0E535802554729DD CRC64;
     MRFHPLAHTA FFAAATALAT APALADADQD KGFAAQVEGS EDAITGTVRI TPTASGVMRV
     SVDLEGVPAG PHGIHIHETG DCSASDFKSA GGHVAGDAKH GVSVEGGPHP GDLPNAEVGS
     DEKLVVTHFN ERLTADHLTD DDGAAFIVHS GADDYESQPA GDAGARIACG VFEPAS
//
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