ID   QCR2_CRYNH              Reviewed;         434 AA.
AC   J9VPD8;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial {ECO:0000303|PubMed:32518190};
DE   Flags: Precursor;
GN   Name=QCR2 {ECO:0000303|PubMed:32518190};
GN   ORFNames=CNAG_05179 {ECO:0000312|EMBL:AFR94444.1};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000312|Proteomes:UP000010091};
RN   [1] {ECO:0000312|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA   Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA   Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA   Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA   Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA   Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA   Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
RN   [2] {ECO:0000305}
RP   INTERACTION WITH MRJ1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=32518190; DOI=10.1128/mbio.01127-20;
RA   Horianopoulos L.C., Hu G., Caza M., Schmitt K., Overby P., Johnson J.D.,
RA   Valerius O., Braus G.H., Kronstad J.W.;
RT   "The Novel J-Domain Protein Mrj1 Is Required for Mitochondrial Respiration
RT   and Virulence in Cryptococcus neoformans.";
RL   MBio 11:E01127-E01127(2020).
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 10 subunits. The complex is composed of 3 respiratory
CC       subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein
CC       (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular
CC       weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (By
CC       similarity). The complex exists as an obligatory dimer and forms
CC       supercomplexes (SCs) in the inner mitochondrial membrane with a monomer
CC       or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2
CC       different assemblies (supercomplexes III(2)IV and III(2)IV(2)) (By
CC       similarity). Interacts with MRJ1 (PubMed:32518190).
CC       {ECO:0000250|UniProtKB:P07257, ECO:0000269|PubMed:32518190}.
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 protease activity as it lacks the zinc-
CC       binding sites. {ECO:0000305}.
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DR   EMBL; CP003823; AFR94444.1; -; Genomic_DNA.
DR   RefSeq; XP_012048763.1; XM_012193373.1.
DR   AlphaFoldDB; J9VPD8; -.
DR   SMR; J9VPD8; -.
DR   EnsemblFungi; AFR94444; AFR94444; CNAG_05179.
DR   GeneID; 23888519; -.
DR   VEuPathDB; FungiDB:CNAG_05179; -.
DR   HOGENOM; CLU_009902_0_1_1; -.
DR   Proteomes; UP000010091; Chromosome 4.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; TAS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; TAS:UniProtKB.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IPI:UniProtKB.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
PE   1: Evidence at protein level;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Respiratory chain; Transit peptide; Transport.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..434
FT                   /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000451744"
SQ   SEQUENCE   434 AA;  44542 MW;  219FE9145F8D9450 CRC64;
     MYSLNRLPRS AAFKSSANLL RRNASTTSAG GVNVVGFENK GPAATSSLTV AIKAGSRYET
     TPGVAHVLKS FAYKATASAS ALRTAREAEL YGGVLSAALT REHLLLSAEF LRGDEEHFLN
     VLASVLSSSQ FYRHELSELV LPVVEAETIS SQAIPSTIAL DLAHSLAFRR GLGNSLYANK
     NYPVSIDDVK SFGEAAFAKS NIAVIGTGVS TEALAKAVSN AFGAGTSSGS KLSTPKANYY
     GGETRVPLDI HAPATATPTM VIAFGTSSPA SADLKVLKHL LGGETSVKWT PGASPLAQAA
     DKIPGASAKA FLLPYSDAAL FGVVLSAPTS AETKTLAQEV ASIVKNAGEF KEEEVKRAVA
     KATFEDAAST ETLSGFVAAA GPAALVGSVP EAQSFSGVSA SSISKAAGEL LKGKPTVVSI
     GNISVLPYAD ELGL