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Database: UniProt
Entry: G4HIU2_9BACL
LinkDB: G4HIU2_9BACL
Original site: G4HIU2_9BACL 
ID   G4HIU2_9BACL            Unreviewed;       249 AA.
AC   G4HIU2;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Superoxide dismutase copper/zinc binding {ECO:0000313|EMBL:EHB62660.1};
GN   ORFNames=PaelaDRAFT_3903 {ECO:0000313|EMBL:EHB62660.1};
OS   Paenibacillus lactis 154.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB62660.1, ECO:0000313|Proteomes:UP000003891};
RN   [1] {ECO:0000313|EMBL:EHB62660.1, ECO:0000313|Proteomes:UP000003891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=154 {ECO:0000313|EMBL:EHB62660.1,
RC   ECO:0000313|Proteomes:UP000003891};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA   Allgaier M., Woyke T.J.;
RT   "The draft genome of Paenibacillus lactis 154.";
RL   Submitted (SEP-2011) 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}.
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DR   EMBL; AGIP01000009; EHB62660.1; -; Genomic_DNA.
DR   RefSeq; WP_007131067.1; NZ_AGIP01000009.1.
DR   AlphaFoldDB; G4HIU2; -.
DR   STRING; 743719.PaelaDRAFT_3903; -.
DR   GeneID; 48308531; -.
DR   PATRIC; fig|743719.3.peg.3960; -.
DR   eggNOG; COG2032; Bacteria.
DR   OrthoDB; 9792957at2; -.
DR   Proteomes; UP000003891; 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   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          120..247
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          49..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  25994 MW;  83E137527DCD914C CRC64;
     MKKKTNKLKY MAGAFLAGAL LLIGILIAAN PEGTLSAIKH TTSKISDYVN GKDNSTADGP
     LAKQGTATSD PNMPAGRNGV SARMDSEPVN QPVYWSEASR KESMGHPVVK LYNAAGEPIG
     SATLEQIHDG VKVKITASGL TPGKHGFHVH ENPIQDGDFK SAGAHFNPTH KHHGLENPQG
     SHVGDMPNLV VGADGTVEAE TIIQHGTLEK GQPNSVLGRS LIIHAGEDDN VTDPAGNSGD
     RVAGGNIPE
//
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