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Database: UniProt
Entry: A0A0J7ID90_9FLAO
LinkDB: A0A0J7ID90_9FLAO
Original site: A0A0J7ID90_9FLAO 
ID   A0A0J7ID90_9FLAO        Unreviewed;       167 AA.
AC   A0A0J7ID90;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Superoxide dismutase {ECO:0000313|EMBL:KMQ64177.1};
GN   ORFNames=ACM40_04215 {ECO:0000313|EMBL:KMQ64177.1};
OS   Chryseobacterium sp. BLS98.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=885586 {ECO:0000313|EMBL:KMQ64177.1, ECO:0000313|Proteomes:UP000036030};
RN   [1] {ECO:0000313|EMBL:KMQ64177.1, ECO:0000313|Proteomes:UP000036030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BLS98 {ECO:0000313|EMBL:KMQ64177.1,
RC   ECO:0000313|Proteomes:UP000036030};
RA   Pipes S.E., Miller J.R., Newman J.D.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KMQ64177.1}.
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DR   EMBL; LFNF01000001; KMQ64177.1; -; Genomic_DNA.
DR   RefSeq; WP_048501736.1; NZ_LFNF01000001.1.
DR   AlphaFoldDB; A0A0J7ID90; -.
DR   STRING; 885586.ACM40_04215; -.
DR   PATRIC; fig|885586.5.peg.859; -.
DR   OrthoDB; 9792957at2; -.
DR   Proteomes; UP000036030; 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   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..167
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005288334"
FT   DOMAIN          37..166
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   167 AA;  17358 MW;  075303B4851C5CE3 CRC64;
     MKGQTLALLA GCAFLAASCC TTKTYTVNAK SGTQTGGTAK FTQKGEEVTM KLEVTNLTPG
     IHAVHIHEKG DCSAADGTST GGHWNPAKDD HGKWGAEHFH MGDIGNLTAD ASGKAVLTFK
     TTKWCLGCTD ESKNIIGKGL IVHAAADDFH TQPTGNAGGR VGCVEIK
//
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