ID E9B342_LEIMU Unreviewed; 270 AA.
AC E9B342;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 22-FEB-2023, entry version 49.
DE RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN ORFNames=LMXM_31_2630 {ECO:0000313|EMBL:CBZ29658.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ29658.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|EMBL:CBZ29658.1, ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ29658.1,
RC ECO:0000313|Proteomes:UP000007259};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714}.
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DR EMBL; FR799584; CBZ29658.1; -; Genomic_DNA.
DR RefSeq; XP_003878110.1; XM_003878061.1.
DR AlphaFoldDB; E9B342; -.
DR GeneID; 13453703; -.
DR KEGG; lmi:LMXM_31_2630; -.
DR VEuPathDB; TriTrypDB:LmxM.31.2630; -.
DR OMA; YIANFWN; -.
DR OrthoDB; 117883at2759; -.
DR PhylomeDB; E9B342; -.
DR Proteomes; UP000007259; Chromosome 31.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR PANTHER; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR42769:SF2; SUPEROXIDE DISMUTASE; 1.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CBZ29658.1}.
FT DOMAIN 61..145
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 155..254
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
SQ SEQUENCE 270 AA; 32252 MW; 5EF40AA2756A8BF8 CRC64;
MHTPKADIQM GRFNFMDQYN EFRNRSGRVP DYYVDKYRKT YWRVDEYIRR SENYIQSQGF
FYLPTLEFPW YKGCMPLMSS YQIRVHYGRH HRAYVEKLNQ LIEGTPLYGM PLDELIVKSA
GDSQLKGVYS NAAQHYNHSF FWKCIQPYGS NIPPDLSAAV SAQYGSVEKF EKQFITAAQN
LFGSGWVYWV YDKKAGAFDI VSYGNAGCPL TNYEYTPLLC VDVWEHAYYI DYENKRPEYL
SKYFGVVDWQ WAERHWKRAT DQEYHEMKFW
//
