ID   H1VMQ0_COLHI            Unreviewed;       305 AA.
AC   H1VMQ0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Superoxide dismutase {ECO:0000313|EMBL:CCF41504.1};
GN   ORFNames=CH063_02608 {ECO:0000313|EMBL:CCF41504.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF41504.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(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; CACQ02004735; CCF41504.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1VMQ0; -.
DR   STRING; 759273.H1VMQ0; -.
DR   EnsemblFungi; CCF41504; CCF41504; CH063_02608.
DR   VEuPathDB; FungiDB:CH63R_00719; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   HOGENOM; CLU_057349_1_0_1; -.
DR   Proteomes; UP000007174; 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..184
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   DOMAIN          217..272
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   REGION          285..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  33656 MW;  134FC8E501822072 CRC64;
     MFARLRIPRV GATFAAAASA PARTAVQMQQ QRSLHYVPQL AYEFKQGVPG LLSADGYDMA
     WNQYMTLILD KLNALTAGTD LEQRDVKQIL LASAQDPSQA PVFNHASMAH NTHFFFKNIT
     PNPKPIPQSL AAELTHSFSS IETLRREIIL TASAMFGPGF VWLVKAGHQD YRILTTYLAG
     SPYPGAHWRL QGTDMNTVGN AGSASYFFQR NAAAQRPGQK PPGALDVVPL LCLNTWEHTW
     LRDYGLGVGG VGGKKAFAEA WWEVIDWEAV KNTADIPTRP NFMRGKGFGK IRGTSQRGEE
     ESPHE
//