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Database: UniProt
Entry: V4NUQ2_9CAUL
LinkDB: V4NUQ2_9CAUL
Original site: V4NUQ2_9CAUL 
ID   V4NUQ2_9CAUL            Unreviewed;       173 AA.
AC   V4NUQ2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Superoxide dismutase copper/zinc binding domain-containing protein {ECO:0000259|Pfam:PF00080};
GN   ORFNames=AEYBE204_18920 {ECO:0000313|EMBL:ESQ76950.1};
OS   Asticcacaulis sp. YBE204.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282363 {ECO:0000313|EMBL:ESQ76950.1, ECO:0000313|Proteomes:UP000017808};
RN   [1] {ECO:0000313|EMBL:ESQ76950.1, ECO:0000313|Proteomes:UP000017808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YBE204 {ECO:0000313|EMBL:ESQ76950.1,
RC   ECO:0000313|Proteomes:UP000017808};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
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:ESQ76950.1}.
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DR   EMBL; AWGF01000021; ESQ76950.1; -; Genomic_DNA.
DR   RefSeq; WP_023464033.1; NZ_AWGF01000021.1.
DR   AlphaFoldDB; V4NUQ2; -.
DR   STRING; 1282363.AEYBE204_18920; -.
DR   PATRIC; fig|1282363.3.peg.3667; -.
DR   OrthoDB; 5431326at2; -.
DR   Proteomes; UP000017808; 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; 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:UP000017808};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..173
FT                   /note="Superoxide dismutase copper/zinc binding domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004724081"
FT   DOMAIN          35..171
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   173 AA;  17205 MW;  1D3F342CAFDE298B CRC64;
     MRAVLLSGLL ATALASAACA ATPGTLTGND GKAIGTVTVT PAPKGVILKI DAAGLPEGWH
     GVHFHAKGDC GDTAKFQNSG GHVHDSAAAL THGLLNPASN DSGDLTNIYV HKDGTVKAEI
     YSSFVVAEAK DGSALPALKD ADGTAVVIHA SADDYTTQPI GGAGARIACA VLP
//
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