ID G0HFP9_CORVD Unreviewed; 206 AA.
AC G0HFP9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Superoxide dismutase {ECO:0000313|EMBL:AEK37302.1};
DE EC=1.15.1.1 {ECO:0000313|EMBL:AEK37302.1};
GN Name=sodC {ECO:0000313|EMBL:AEK37302.1};
GN OrderedLocusNames=CVAR_1949 {ECO:0000313|EMBL:AEK37302.1};
OS Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS NCIMB 30131) (Corynebacterium mooreparkense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK37302.1, ECO:0000313|Proteomes:UP000006659};
RN [1] {ECO:0000313|EMBL:AEK37302.1, ECO:0000313|Proteomes:UP000006659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC {ECO:0000313|Proteomes:UP000006659};
RX PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA Schroeder J., Maus I., Trost E., Tauch A.;
RT "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT from the surface of smear-ripened cheeses and insights into cheese ripening
RT and flavor generation.";
RL BMC Genomics 12:545-545(2011).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
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DR EMBL; CP002917; AEK37302.1; -; Genomic_DNA.
DR RefSeq; WP_014010458.1; NC_015859.1.
DR AlphaFoldDB; G0HFP9; -.
DR STRING; 858619.CVAR_1949; -.
DR KEGG; cva:CVAR_1949; -.
DR eggNOG; COG2032; Bacteria.
DR HOGENOM; CLU_056632_8_0_11; -.
DR Proteomes; UP000006659; Chromosome.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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: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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:AEK37302.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..206
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039711820"
FT DOMAIN 56..202
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
FT REGION 93..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 206 AA; 21092 MW; 3C0AAB44A600E896 CRC64;
MRLPTRSSAV AAAAATVLVL SACSSDDNDD GNTTDDASTT AYATADVTNA DGDALGTASV
SEDSFASDAT ELTVSFTGLE PGMYGMHIHT VGQCETDSES PDGSDTGDYL SSGGHMDSDD
HDHPSHGGDL PALLVKEDGT ASLTVSTDRV TKENLLDDDG SALIIHESPD NYGNIPERYA
PDGPDEDSLK TGDAGGRQAC GVFEAA
//
