ID   A0A3S4RRT7_MYCCI        Unreviewed;       287 AA.
AC   A0A3S4RRT7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Cu/Zn superoxide dismutase {ECO:0000313|EMBL:VEG50771.1};
DE            EC=1.15.1.1 {ECO:0000313|EMBL:VEG50771.1};
GN   Name=sodC_2 {ECO:0000313|EMBL:VEG50771.1};
GN   ORFNames=NCTC10485_05091 {ECO:0000313|EMBL:VEG50771.1};
OS   Mycolicibacterium chitae (Mycobacterium chitae).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1792 {ECO:0000313|EMBL:VEG50771.1, ECO:0000313|Proteomes:UP000282551};
RN   [1] {ECO:0000313|EMBL:VEG50771.1, ECO:0000313|Proteomes:UP000282551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10485 {ECO:0000313|EMBL:VEG50771.1,
RC   ECO:0000313|Proteomes:UP000282551};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
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DR   EMBL; LR134355; VEG50771.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S4RRT7; -.
DR   OrthoDB; 9792957at2; -.
DR   Proteomes; UP000282551; Chromosome 1.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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:SF105; SUPEROXIDE DISMUTASE [CU-ZN]; 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.
PE   4: Predicted;
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Oxidoreductase {ECO:0000313|EMBL:VEG50771.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282551};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..287
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018522441"
FT   DOMAIN          74..208
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          30..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   287 AA;  28965 MW;  6B1F20D08F80DC99 CRC64;
     MQNHTHTVAA ALAVPVAFAF LAGCAQGEQA ADETTSPTTS PAPSGDTLST ELQTADGRSV
     ANVDIEFVDD YATITLETTE AGILTPGFHA FHIHAVGLCE PNSVAPGGGE PGDFLSAGGH
     LHGPDNHAAI GDLTPIDVRS DGSARLVATT DSFTIDDLRG PQGSALMIHE GPDNFANIPP
     RYTSNGVPGP DAETLATGDA GSRVACGVLA PASTTPAGTT ETATVTETTA MVPPPPGPAT
     TTEMPPVETT TPTETTAPTE TTTSPTTTTE TTAETTPPAE GEELPAE
//