ID   SDHF2_ASPTN             Reviewed;         295 AA.
AC   Q0CSY3;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 65.
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   ORFNames=ATEG_03201;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476597; EAU36475.1; -; Genomic_DNA.
DR   RefSeq; XP_001212379.1; XM_001212379.1.
DR   AlphaFoldDB; Q0CSY3; -.
DR   SMR; Q0CSY3; -.
DR   STRING; 341663.Q0CSY3; -.
DR   EnsemblFungi; EAU36475; EAU36475; ATEG_03201.
DR   GeneID; 4317901; -.
DR   VEuPathDB; FungiDB:ATEG_03201; -.
DR   eggNOG; KOG3326; Eukaryota.
DR   HOGENOM; CLU_943336_0_0_1; -.
DR   OMA; NTERMTG; -.
DR   OrthoDB; 1492851at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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:0018293; P:protein-FAD linkage; ISS:UniProtKB.
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..295
FT                   /note="Succinate dehydrogenase assembly factor 2,
FT                   mitochondrial"
FT                   /id="PRO_0000383188"
FT   REGION          35..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  32924 MW;  3ADEE8305DFEE1B9 CRC64;
     MSVSRMIPRL VRASASPMAV PTAFRRSFGS SVVCAKDNDG PRGPSTPSTA PEYRQNQTSK
     PPNQFMPNST STMTNDYPKV GEKASPPELL NSVDPNYRPA DPYSGKVQHF TGGRQEPGAQ
     KPELGLGEME GITFKVEPLQ RSGEDTTTMR ARLLYQSRKR GILESDLLLS TFADVYLAKM
     NHEQLQEYDR FLDENDWDIY YWATQDAPEE GTPAEDTPTE TWQRTGAKSG EWRQTIGAFK
     AAYRPVPTRW ADSEVLRLLR EHVRDNSATG FHAAKNKKTG GSGLGRMPNI QVFDS