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Database: UniProt
Entry: A0A494ZUB3_9BACI
LinkDB: A0A494ZUB3_9BACI
Original site: A0A494ZUB3_9BACI 
ID   A0A494ZUB3_9BACI        Unreviewed;       196 AA.
AC   A0A494ZUB3;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Superoxide dismutase family protein {ECO:0000313|EMBL:RKQ29582.1};
GN   ORFNames=D8M06_17475 {ECO:0000313|EMBL:RKQ29582.1};
OS   Oceanobacillus halophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=930130 {ECO:0000313|EMBL:RKQ29582.1, ECO:0000313|Proteomes:UP000269301};
RN   [1] {ECO:0000313|EMBL:RKQ29582.1, ECO:0000313|Proteomes:UP000269301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23996 {ECO:0000313|EMBL:RKQ29582.1,
RC   ECO:0000313|Proteomes:UP000269301};
RX   PubMed=26869142; DOI=.1099/ijsem.0.000952;
RA   Amoozegar M.A., Bagheri M., Makhdoumi A., Nikou M.M., Fazeli S.A.S.,
RA   Schumann P., Sproer C., Sanchez-Porro C., Ventosa A.;
RT   "Oceanobacillus halophilus sp. nov., a novel moderately halophilic
RT   bacterium from a hypersaline lake.";
RL   Int. J. Syst. Evol. Microbiol. 66:1317-1322(2016).
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:RKQ29582.1}.
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DR   EMBL; RBZP01000023; RKQ29582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494ZUB3; -.
DR   OrthoDB; 9792957at2; -.
DR   Proteomes; UP000269301; 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; 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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269301};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..196
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019774546"
FT   DOMAIN          38..168
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          165..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   196 AA;  20585 MW;  C2F2CB2DC1A15457 CRC64;
     MRVMFLILMI FVLSACNGGA DETTRTVEMY NAAGDMVGNA TLNEMPDGVQ IKLKLEGLSP
     GFHGIHVHEF SSCEGPDFQS AGNHLDPEGN EHGLMHPKGS HLGDLPNIEA DAGGLVDAEL
     MLAGATLTDG KQSILRGDGT SLVVHESQDD GVSQPAGDSG VRIICGEIKA DPNADSKSSA
     EETPSDPTET NENQDE
//
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