ID   F8QNK6_NEIMD            Unreviewed;       146 AA.
AC   F8QNK6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Cu,Zn superoxide dismutase {ECO:0000313|EMBL:ADJ66728.1};
DE   Flags: Fragment;
GN   Name=sodC {ECO:0000313|EMBL:ADJ66728.1};
OS   Neisseria meningitidis serogroup A.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=65699 {ECO:0000313|EMBL:ADJ66728.1};
RN   [1] {ECO:0000313|EMBL:ADJ66728.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M12746 {ECO:0000313|EMBL:ADJ66728.1};
RA   Dolan J.M., Hatcher C.P., Theodore M.J., Satterfield D., Linscott K.,
RA   Bach M., Wang X., Harcourt B.H., Mayer L.W.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADJ66728.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M12746 {ECO:0000313|EMBL:ADJ66728.1};
RX   PubMed=21573213; DOI=10.1371/journal.pone.0019361;
RA   Dolan Thomas J., Hatcher C.P., Satterfield D.A., Theodore M.J., Bach M.C.,
RA   Linscott K.B., Zhao X., Wang X., Mair R., Schmink S., Arnold K.E.,
RA   Stephens D.S., Harrison L.H., Hollick R.A., Andrade A.L.,
RA   Lamaro-Cardoso J., de Lemos A.P., Gritzfeld J., Gordon S., Soysal A.,
RA   Bakir M., Sharma D., Jain S., Satola S.W., Messonnier N.E., Mayer L.W.;
RT   "sodC-Based Real-Time PCR for Detection of Neisseria meningitidis.";
RL   PLoS ONE 6:E19361-E19361(2011).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
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; GQ365738; ADJ66728.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8QNK6; -.
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; IPR018152; SOD_Cu/Zn_BS.
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; PS00087; SOD_CU_ZN_1; 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          32..146
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          65..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADJ66728.1"
FT   NON_TER         146
FT                   /evidence="ECO:0000313|EMBL:ADJ66728.1"
SQ   SEQUENCE   146 AA;  15591 MW;  B4F4C7673512A22E CRC64;
     AQAHEHNTIP KGASIEVKVQ QLDPVNGNKD VGTVTITESN YGLVFTPDLQ GLSEGLHGFH
     IHENPSCEPK EKEGKLTAGL GAGGHWDPKG AKQHGYPWQD DAHLGDLPAL TVLHDGTATN
     PVLAPRLKHL DDVRGHSIMI HTGGDN
//