ID   SDHF2_YARLI             Reviewed;         145 AA.
AC   Q6C202;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Succinate dehydrogenase assembly factor 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03057};
DE            Short=SDH assembly factor 2 {ECO:0000255|HAMAP-Rule:MF_03057};
DE            Short=SDHAF2 {ECO:0000255|HAMAP-Rule:MF_03057};
GN   OrderedLocusNames=YALI0F11957g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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. Required for flavinylation (covalent
CC       attachment of FAD) of the flavoprotein subunit of the SDH catalytic
CC       dimer. {ECO:0000255|HAMAP-Rule:MF_03057}.
CC   -!- SUBUNIT: Interacts with the flavoprotein subunit within the SDH
CC       catalytic dimer. {ECO:0000255|HAMAP-Rule:MF_03057}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03057}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       Rule:MF_03057}.
CC   -!- SIMILARITY: Belongs to the SDHAF2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03057}.
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DR   EMBL; CR382132; CAG78117.1; -; Genomic_DNA.
DR   RefSeq; XP_505310.1; XM_505310.1.
DR   AlphaFoldDB; Q6C202; -.
DR   SMR; Q6C202; -.
DR   STRING; 4952.CAG78117; -.
DR   EnsemblFungi; CAG78117; CAG78117; YALI0_F11957g.
DR   GeneID; 2908266; -.
DR   KEGG; yli:YALI0F11957g; -.
DR   VEuPathDB; FungiDB:YALI0_F11957g; -.
DR   HOGENOM; CLU_103054_0_1_1; -.
DR   InParanoid; Q6C202; -.
DR   OMA; YGKPQNP; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISS:UniProtKB.
DR   GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IBA:GO_Central.
DR   GO; GO:0018293; P:protein-FAD linkage; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 1.10.150.250; -; 1.
DR   HAMAP; MF_03057; SDHAF2; 1.
DR   InterPro; IPR005631; SDH.
DR   InterPro; IPR036714; SDH_sf.
DR   InterPro; IPR028882; SDHAF2.
DR   Pfam; PF03937; Sdh5; 1.
DR   SUPFAM; SSF109910; SSF109910; 1.
PE   3: Inferred from homology;
KW   Chaperone; Mitochondrion; Reference proteome.
FT   CHAIN           1..145
FT                   /note="Succinate dehydrogenase assembly factor 2,
FT                   mitochondrial"
FT                   /id="PRO_0000383200"
SQ   SEQUENCE   145 AA;  17142 MW;  46DC7D3D2F112F00 CRC64;
     MLRLVRSSRA FHTSLIRAGT QANINPVAGK TADEVDVKIE PIPRHGEETE TKRARLLYQS
     RKRGILETDL LLSRYAKLYL KDMTREELEE YDKLLDEPDW DIFYWATRND NIKPCPERWA
     KSPVMEKLRE LAENKEREVL RMPDL