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QCR2_ASHGO
ID   QCR2_ASHGO              Reviewed;         366 AA.
AC   Q75CW5;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial;
DE   AltName: Full=Complex III subunit 2;
DE   AltName: Full=Core protein II;
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 2;
DE   Flags: Precursor;
GN   Name=QCR2; OrderedLocusNames=ACL199C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 19; 108; 110; 269; 274; 281;
RP   283; 297; 313-314; 323; 330 AND 346.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC       multisubunit transmembrane complex that is part of the mitochondrial
CC       electron transport chain which drives oxidative phosphorylation. The
CC       respiratory chain contains 3 multisubunit complexes succinate
CC       dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC       (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC       (complex IV, CIV), that cooperate to transfer electrons derived from
CC       NADH and succinate to molecular oxygen, creating an electrochemical
CC       gradient over the inner membrane that drives transmembrane transport
CC       and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC       transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC       translocation of protons across the mitochondrial inner membrane, with
CC       protons being carried across the membrane as hydrogens on the quinol.
CC       In the process called Q cycle, 2 protons are consumed from the matrix,
CC       4 protons are released into the intermembrane space and 2 electrons are
CC       passed to cytochrome c. {ECO:0000250|UniProtKB:P07257}.
CC   -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC       (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC       composed of 3 respiratory subunits cytochrome b, cytochrome c1 and
CC       Rieske protein, 2 core protein subunits, and additional low-molecular
CC       weight protein subunits. The complex exists as an obligatory dimer and
CC       forms supercomplexes (SCs) in the inner mitochondrial membrane with
CC       cytochrome c oxidase (complex IV, CIV). {ECO:0000250|UniProtKB:P07257}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P07257}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P07257}; Matrix side
CC       {ECO:0000250|UniProtKB:P07257}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Does not seem to have a protease activity as it lack the zinc-
CC       binding site. {ECO:0000305}.
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DR   EMBL; AE016816; AAS51029.2; -; Genomic_DNA.
DR   RefSeq; NP_983205.2; NM_208558.2.
DR   AlphaFoldDB; Q75CW5; -.
DR   SMR; Q75CW5; -.
DR   STRING; 33169.AAS51029; -.
DR   EnsemblFungi; AAS51029; AAS51029; AGOS_ACL199C.
DR   GeneID; 4619325; -.
DR   KEGG; ago:AGOS_ACL199C; -.
DR   eggNOG; KOG2583; Eukaryota.
DR   HOGENOM; CLU_009902_0_1_1; -.
DR   InParanoid; Q75CW5; -.
DR   OMA; YKYQDAG; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0030061; C:mitochondrial crista; IEA:EnsemblFungi.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:EnsemblFungi.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:EnsemblFungi.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Respiratory chain; Transit peptide; Transport.
FT   TRANSIT         1..15
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           16..366
FT                   /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT                   /id="PRO_0000026794"
SQ   SEQUENCE   366 AA;  39229 MW;  B0A46B5B605A15D0 CRC64;
     MLSQRLQCSK QFARHLSVAA KDGSGKVSTL SVQVQGGSRY ATKDGVAHLL SRFNFHNTGN
     KSALRLVRES ELLGGRFQST VDREHITLSA TFLKEDLPYF VNALADVLYK TSFRPHELAE
     SVLPAATRDA AVARACPVAA AEEALYSVTY RHGLGKPVLY DGVEKVTLED IKAYADKVYT
     KENVTVLGQG INEADLKRFV NDSLLASLPS GTSLAGSGNA KTHSGEARLR HAGSSVAAIA
     VPVAKADFAT YEVLARYLTS DLYALSPLVH KAKLDKYTDG GLFSLYVKSA EAAKAAADIK
     KVVADLKAGK DISVARKYAA LQLAVENDSA ASPVSLKLEN AKDFKLGKFN YVAVGDVSNL
     PFADEL
 
 
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