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
//