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DHSD_NEUCR
ID   DHSD_NEUCR              Reviewed;         166 AA.
AC   Q7SGY6;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;
DE            Short=CybS;
DE   AltName: Full=Succinate-ubiquinone reductase membrane anchor subunit;
DE   Flags: Precursor;
GN   ORFNames=B18P24.060, NCU03031;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH)
CC       that is involved in complex II of the mitochondrial electron transport
CC       chain and is responsible for transferring electrons from succinate to
CC       ubiquinone (coenzyme Q). {ECO:0000250}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Forms part of complex II containing four subunits: a
CC       flavoprotein (FP), an iron-sulfur protein (IP) and a cytochrome b
CC       composed of a large and a small subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CybS family. {ECO:0000305}.
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DR   EMBL; BX842626; CAE76264.1; -; Genomic_DNA.
DR   EMBL; CM002236; EAA36181.1; -; Genomic_DNA.
DR   RefSeq; XP_965417.1; XM_960324.3.
DR   AlphaFoldDB; Q7SGY6; -.
DR   SMR; Q7SGY6; -.
DR   STRING; 5141.EFNCRP00000002361; -.
DR   EnsemblFungi; EAA36181; EAA36181; NCU03031.
DR   GeneID; 3881567; -.
DR   KEGG; ncr:NCU03031; -.
DR   VEuPathDB; FungiDB:NCU03031; -.
DR   HOGENOM; CLU_096618_0_1_1; -.
DR   InParanoid; Q7SGY6; -.
DR   OMA; SEGSYHW; -.
DR   UniPathway; UPA00223; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd03496; SQR_TypeC_CybS; 1.
DR   Gene3D; 1.20.1300.10; -; 1.
DR   InterPro; IPR007992; CybS.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   PANTHER; PTHR13337; PTHR13337; 1.
DR   SUPFAM; SSF81343; SSF81343; 1.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transmembrane; Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..166
FT                   /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT                   small subunit, mitochondrial"
FT                   /id="PRO_0000006494"
FT   TOPO_DOM        1..65
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..94
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..124
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..166
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   BINDING         106
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_note="ligand shared with large subunit"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /ligand_note="ligand shared with IP"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   166 AA;  17675 MW;  6C31DE98A6A85CA3 CRC64;
     MASVARSSAL LKQVAAQQSV AANGLRVAAF HTTSRKSLLP PPPQRIEGTV NDPVEVPPPS
     PSHGSYHWTF DRVVAAGLIP LTVAPFAAGS LNPTMDAVLA ATILIHSHTG FGNIIVDYVP
     SKRVPKARKV FTWGLNAATV LVGLALYEFE TTDVGLTETI KRVWKA
 
 
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