ID   SDHF3_MAGO7             Reviewed;         136 AA.
AC   P0C146; A4REY4; G4NBP0;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Succinate dehydrogenase assembly factor 3, mitochondrial {ECO:0000250|UniProtKB:Q04401};
DE            Short=SDH assembly factor 3 {ECO:0000250|UniProtKB:Q04401};
DE            Short=SDHAF3 {ECO:0000250|UniProtKB:Q04401};
DE   Flags: Precursor;
GN   ORFNames=MGG_17437;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Plays an essential role in the assembly of succinate
CC       dehydrogenase (SDH), an enzyme complex (also referred to as respiratory
CC       complex II) that is a component of both the tricarboxylic acid (TCA)
CC       cycle and the mitochondrial electron transport chain, and which couples
CC       the oxidation of succinate to fumarate with the reduction of ubiquinone
CC       (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur
CC       protein subunit of the SDH catalytic dimer, protecting it from the
CC       deleterious effects of oxidants. May act together with SDHAF1.
CC       {ECO:0000250|UniProtKB:Q04401, ECO:0000250|UniProtKB:Q8SZ16}.
CC   -!- SUBUNIT: Interacts with the iron-sulfur protein subunit within the SDH
CC       catalytic dimer. {ECO:0000250|UniProtKB:Q04401}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q04401}.
CC   -!- SIMILARITY: Belongs to the complex I LYR family. SDHAF3 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CM001235; EHA48948.1; -; Genomic_DNA.
DR   RefSeq; XP_003718532.1; XM_003718484.1.
DR   AlphaFoldDB; P0C146; -.
DR   SMR; P0C146; -.
DR   STRING; 318829.MGG_17437T0; -.
DR   EnsemblFungi; MGG_17437T0; MGG_17437T0; MGG_17437.
DR   GeneID; 12984112; -.
DR   KEGG; mgr:MGG_17437; -.
DR   VEuPathDB; FungiDB:MGG_17437; -.
DR   eggNOG; KOG4100; Eukaryota.
DR   HOGENOM; CLU_102310_1_0_1; -.
DR   InParanoid; P0C146; -.
DR   OMA; LTEWQMY; -.
DR   OrthoDB; 1613308at2759; -.
DR   Proteomes; UP000009058; Chromosome 5.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IEA:InterPro.
DR   InterPro; IPR008381; SDHAF3/Sdh7.
DR   PANTHER; PTHR13137; PTHR13137; 1.
PE   3: Inferred from homology;
KW   Chaperone; Gluconeogenesis; Mitochondrion; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..136
FT                   /note="Succinate dehydrogenase assembly factor 3,
FT                   mitochondrial"
FT                   /id="PRO_0000042749"
SQ   SEQUENCE   136 AA;  15381 MW;  4C54B9414930B8D1 CRC64;
     MRASMVRRMA AAASSSASSS LRPAPLALLP PIPLYRRLLR AHRKHLPAEM RLLGDEYLKS
     EFRAHRNIDN PAHLIGFLTE WQLYAQQVEG ESWLGEKIDQ AKVEKLSEQQ VGQLYELMMA
     IKSRREGGEG EGQESP