ID M3JVR0_CANMX Unreviewed; 374 AA.
AC M3JVR0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=G210_3286 {ECO:0000313|EMBL:EMG46469.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG46469.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG46469.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG46469.1}.
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DR EMBL; AOGT01001998; EMG46469.1; -; Genomic_DNA.
DR AlphaFoldDB; M3JVR0; -.
DR STRING; 1245528.M3JVR0; -.
DR eggNOG; KOG2583; Eukaryota.
DR HOGENOM; CLU_009902_0_1_1; -.
DR OMA; YKYQDAG; -.
DR OrthoDB; 1330839at2759; -.
DR Proteomes; UP000011777; 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:UP000011777};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 19..161
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 167..324
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 374 AA; 39481 MW; 90B3D9DFBE262FA5 CRC64;
MLSRASIRAY STIPNSIKVA SKESASDLTR LSVVINNAGA RNGKLGVSHL LSKFAFLNNG
AKSALRLTRE SELLGGSIEG QVTRDALILK TSFLQQDLPY YVEALGNVVS NTQFTPHEFN
EVVLPAAKTE AALAEADSSF KGLEKLHEIT FRKGLGNPLY YHESTPVTVD EVADFAKEQF
TGENISILAE GAIEEDLTKF VAESGFCYLP ASSSNGVKAL PAQSFTGKEA RIPSAGASSA
LIGIPVKPAD FGKYEVLSVA IGNTTLPNSS SPLSQIPGAT SHLYKYQDAG LFVISVTGEA
SQVAQGIKQA KSIAESVSAS QLSDAVKTAE LSVALQSSVE APLSIKVSAE KAPISEFNYV
ATGDLNVLPY ADEL
//
