ID F2PWH9_TRIEC Unreviewed; 303 AA.
AC F2PWH9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Fe superoxide dismutase {ECO:0000313|EMBL:EGE06247.1};
GN ORFNames=TEQG_05252 {ECO:0000313|EMBL:EGE06247.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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}.
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DR EMBL; DS995746; EGE06247.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PWH9; -.
DR VEuPathDB; FungiDB:TEQG_05252; -.
DR eggNOG; KOG0876; Eukaryota.
DR HOGENOM; CLU_057349_1_0_1; -.
DR Proteomes; UP000009169; 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;
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; 33714 MW; 46B80D763FA80751 CRC64;
MLFQRSIRQQ AGLLASASRC TLRPQVQSRS FHRVPQLTHG 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
//
