SDHF2_ASPFN
ID SDHF2_ASPFN Reviewed; 292 AA.
AC B8NT06;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=AFLA_051990;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963483; EED47145.1; -; Genomic_DNA.
DR RefSeq; XP_002383325.1; XM_002383284.1.
DR AlphaFoldDB; B8NT06; -.
DR SMR; B8NT06; -.
DR STRING; 5059.CADAFLAP00011190; -.
DR PRIDE; B8NT06; -.
DR EnsemblFungi; EED47145; EED47145; AFLA_051990.
DR VEuPathDB; FungiDB:AFLA_051990; -.
DR eggNOG; KOG3326; Eukaryota.
DR HOGENOM; CLU_943336_0_0_1; -.
DR OMA; NTERMTG; -.
DR Proteomes; UP000001875; 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.
FT CHAIN 1..292
FT /note="Succinate dehydrogenase assembly factor 2,
FT mitochondrial"
FT /id="PRO_0000383187"
FT REGION 27..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 292 AA; 32796 MW; C4789E516112F5DA CRC64;
MSAPRLIQRF ARPSLSPFFL RTTLARRSFG SSAIRPKDDN GRAPSTAPEH REYQTNRPPN
QHVPNTTSTM TRDFPKAGEK SVPPEFVSAA DPNYKPADPY PGKVEHFTGG RQETGAQKPE
LGVGEMEGIT FKVEPLKRTG EDVSTIRARL LYQSRKRGIL ESDLLLSTFA DVYLSKMNKE
QLQEYDRFLD ENDWDIYYWA TQDPPTEDNV AEDTPTETWK RTGAKSGEWA QTVGAYKAAY
RPVPSRWADS EVLRLLRQHV QDNSATGFHA AKSKKTGGAG LGRMPNVQVF DS
