SDHF2_CRYNB
ID SDHF2_CRYNB Reviewed; 175 AA.
AC P0CR33; D3NQ36; Q55ZP1; Q5KP03;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 41.
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=CNBA4490;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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. 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAEY01000002; EAL23333.1; -; Genomic_DNA.
DR RefSeq; XP_777980.1; XM_772887.1.
DR AlphaFoldDB; P0CR33; -.
DR SMR; P0CR33; -.
DR EnsemblFungi; AAW41035; AAW41035; CNA04680.
DR EnsemblFungi; EAL23333; EAL23333; CNBA4490.
DR GeneID; 4933711; -.
DR KEGG; cnb:CNBA4490; -.
DR VEuPathDB; FungiDB:CNBA4490; -.
DR HOGENOM; CLU_103054_0_0_1; -.
DR Proteomes; UP000001435; Chromosome 1.
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.
FT CHAIN 1..175
FT /note="Succinate dehydrogenase assembly factor 2,
FT mitochondrial"
FT /id="PRO_0000410278"
FT REGION 42..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 175 AA; 20251 MW; 71777F9048E02C81 CRC64;
MSVLRALPRV ARVVRPAPPS LRSISTTNTI FKSPTADPFP LPFSDPELAH ANNSLPSNSE
EWPLPEPLDR TGEDEKTLRA RLIYQTRKRG TLETDLILST FARDELPNMD FEEMKQFDKL
LDEPDWDIFY WSVKKRDPPA RWKGTPLLEK LQKHAKNEGK VVRMMPELMQ KEPDL