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SDHF2_CANGA
ID   SDHF2_CANGA             Reviewed;         153 AA.
AC   Q6FQ93;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=CAGL0I08085g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380955; CAG60538.1; -; Genomic_DNA.
DR   RefSeq; XP_447601.1; XM_447601.1.
DR   AlphaFoldDB; Q6FQ93; -.
DR   SMR; Q6FQ93; -.
DR   STRING; 5478.XP_447601.1; -.
DR   EnsemblFungi; CAG60538; CAG60538; CAGL0I08085g.
DR   GeneID; 2889290; -.
DR   KEGG; cgr:CAGL0I08085g; -.
DR   CGD; CAL0130464; CAGL0I08085g.
DR   VEuPathDB; FungiDB:CAGL0I08085g; -.
DR   eggNOG; KOG3326; Eukaryota.
DR   HOGENOM; CLU_103054_0_1_1; -.
DR   InParanoid; Q6FQ93; -.
DR   OMA; YGKPQNP; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISS:UniProtKB.
DR   GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IEA:EnsemblFungi.
DR   GO; GO:0017013; P:protein flavinylation; IEA:EnsemblFungi.
DR   GO; GO:0018293; P:protein-FAD linkage; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:EnsemblFungi.
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..153
FT                   /note="Succinate dehydrogenase assembly factor 2,
FT                   mitochondrial"
FT                   /id="PRO_0000383190"
SQ   SEQUENCE   153 AA;  18203 MW;  7596EC3367897F54 CRC64;
     MLRITYKLPI ALRQQAFVAR KLVPTIKANY STNSDDDVVS RIKVHPIKRI NESIDKKRAR
     LIYQSRKRGI LETDLLLSGF AAKHLRSMTN EELDEYDALL NELDWDIYYW VTKNYKTSPV
     PERWKNSEIL KKLQDFSENK EKKILRMPDL ENY
 
 
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