ID A0A5Q4BJU7_9PEZI Unreviewed; 456 AA.
AC A0A5Q4BJU7;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 9.
DE RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial {ECO:0000256|ARBA:ARBA00040751};
DE AltName: Full=Core protein II {ECO:0000256|ARBA:ARBA00041372};
GN Name=Qcr-2 {ECO:0000313|EMBL:TQN66917.1};
GN ORFNames=CSHISOI_08523 {ECO:0000313|EMBL:TQN66917.1};
OS Colletotrichum shisoi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=2078593 {ECO:0000313|EMBL:TQN66917.1, ECO:0000313|Proteomes:UP000326340};
RN [1] {ECO:0000313|EMBL:TQN66917.1, ECO:0000313|Proteomes:UP000326340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-2018a {ECO:0000313|EMBL:TQN66917.1,
RC ECO:0000313|Proteomes:UP000326340};
RX PubMed=31527702;
RA Gan P., Tsushima A., Hiroyama R., Narusaka M., Takano Y., Narusaka Y.,
RA Kawaradani M., Damm U., Shirasu K.;
RT "Colletotrichum shisoi sp. nov., an anthracnose pathogen of Perilla
RT frutescens in Japan: molecular phylogenetic, morphological and genomic
RT evidence.";
RL Sci. Rep. 9:13349-13349(2019).
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:TQN66917.1}.
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DR EMBL; PUHP01001051; TQN66917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q4BJU7; -.
DR Proteomes; UP000326340; 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:UP000326340};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 49..181
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 204..375
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 456 AA; 47364 MW; 6D692FA605E06D2D CRC64;
MISRPSLTRP AQQALRHSSC ARTISGRRFA SAAAGSGAFE TSDVGGVKVA ARDSQGPTTK
LAIVAKAGTR YQPLPGLAVG LESFAFKNTS KRSGLRIVRE SELLGSQLTA YHTREALVLE
ASFFRDDLPY FTELLAEVVS QTKYTTHEFH EEVQPVLRLK QSATSAAALA LDSAHSVAFH
SGLGSPANLT PSIPIQPYLS EFAVSEFAQA AYAKPNIALV ADGASAANVS KWAEQFFKSV
PSASSGKLAL NTAATKYYGG EQRTYSPSGN SLVIAFPGAT NGQTSPELAV LAALLGGKSS
IKWSPGFSLI NKAVGPAPGL STSTVNLSYS DAGLLSVQFS GPASAIRTAA QEAVKALKSI
SEGTVSKEDL TKAIAKAKFD ALEATEKRSG SILLAGSGLV HNGKPINAAE VANSIGSVTA
EKLKTATKTI LEGKASVAAV GDLYALPYAE ELGLRV
//
