ID   A0A178EX17_TRIRU        Unreviewed;       303 AA.
AC   A0A178EX17;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Fe superoxide dismutase {ECO:0000313|EMBL:OAL64468.1};
GN   ORFNames=A7C99_3902 {ECO:0000313|EMBL:OAL64468.1};
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL64468.1, ECO:0000313|Proteomes:UP000243015};
RN   [1] {ECO:0000313|EMBL:OAL64468.1, ECO:0000313|Proteomes:UP000243015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA   Zhan P., Tao Y., Liu W.;
RT   "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a
CC       dedicated translation machinery responsible for the synthesis of
CC       mitochondrial genome-encoded proteins, including at least some of the
CC       essential transmembrane subunits of the mitochondrial respiratory
CC       chain. The mitoribosomes are attached to the mitochondrial inner
CC       membrane and translation products are cotranslationally integrated into
CC       the membrane. {ECO:0000256|ARBA:ARBA00037226}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAL64468.1}.
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DR   EMBL; LHPM01000015; OAL64468.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178EX17; -.
DR   VEuPathDB; FungiDB:TERG_04819; -.
DR   OrthoDB; 2055478at2759; -.
DR   Proteomes; UP000243015; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:InterPro.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR   Pfam; PF02777; Sod_Fe_C; 2.
DR   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000243015}.
FT   DOMAIN          128..186
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   DOMAIN          239..280
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   REGION          283..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  33740 MW;  43BC0C7636D17751 CRC64;
     MLFQRSIRQQ AGLLASASRC TLRPQVQSRS FHRVPQLTYG THFQEHGVPG VLSPEGYNLA
     WVQYQSYLVQ KLNMLTGGTA DENVGPGTLL IKYARQASMA SLFNYASMAH NNHFYFNCLS
     PETVPIPGKL EEAITESCSS VESLKEEFIA TANAMFGPGF VWLVKMKDTA QLKILATYIA
     GSPYPQAHFR RQPVDMATQT TGITGGENLE AVGRIASRTY GSMGPFAQQK YLAPGGADIH
     PILCVNTWEH VWLRDWGIGG KAGYLEAWWD KINWEEVAQN YKQAGPESSF DTSRKQKPFG
     SRY
//