ID C4Y9V3_CLAL4 Unreviewed; 372 AA.
AC C4Y9V3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial {ECO:0000256|ARBA:ARBA00040751};
DE AltName: Full=Complex III subunit 2 {ECO:0000256|ARBA:ARBA00041778};
DE AltName: Full=Core protein II {ECO:0000256|ARBA:ARBA00041372};
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 2 {ECO:0000256|ARBA:ARBA00042707};
GN ORFNames=CLUG_05174 {ECO:0000313|EMBL:EEQ41045.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ41045.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ41045.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ41045.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004443}; Matrix side
CC {ECO:0000256|ARBA:ARBA00004443}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC {ECO:0000256|ARBA:ARBA00038146}.
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DR EMBL; CH408081; EEQ41045.1; -; Genomic_DNA.
DR RefSeq; XP_002615158.1; XM_002615112.1.
DR AlphaFoldDB; C4Y9V3; -.
DR STRING; 306902.C4Y9V3; -.
DR GeneID; 8495362; -.
DR KEGG; clu:CLUG_05174; -.
DR VEuPathDB; FungiDB:CLUG_05174; -.
DR HOGENOM; CLU_009902_0_1_1; -.
DR InParanoid; C4Y9V3; -.
DR OMA; YKYQDAG; -.
DR OrthoDB; 1330839at2759; -.
DR Proteomes; UP000007703; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF209; CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 21..158
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 164..314
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 372 AA; 38494 MW; 033445CE3B5AD750 CRC64;
MLSRVSARAY SSAPVKLVAR DASGSLSSIS LVVNNSGSKA GKSGVAHLLS KFAFLNTETK
SALRFTRESE LLGGQFSSHV TRDAIVLNAK FLKQDLPYYV EALANTIAKP QFRPHEFTEV
VVPVAKAEAA SAAASNAFVG LEALHALSFR KGLGNPLYYN PASSVSYEDV TEFAAHAYTA
GNVSLVASGV NEADLAGFVA ESAFSDLSAS AASAVPVKSF TGKETRITAA GESFAAIAVP
VAKADFAKYE VLSAAVGTSV LAGVDSPLAK IPGADSKLYQ YQDAGLFVVS VSGDAASVAQ
GIKNAKKAVE AVSASSLSAS LKAAELSVAL QESFEFPREI KISADSAKGV KLGEFNYVAV
GNTDVLPYAD EL
//
