ID A0A0D2GEN2_9EURO Unreviewed; 458 AA.
AC A0A0D2GEN2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=Z517_05870 {ECO:0000313|EMBL:KIW79258.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW79258.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW79258.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW79258.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN846972; KIW79258.1; -; Genomic_DNA.
DR RefSeq; XP_013283066.1; XM_013427612.1.
DR AlphaFoldDB; A0A0D2GEN2; -.
DR STRING; 1442368.A0A0D2GEN2; -.
DR GeneID; 25305360; -.
DR VEuPathDB; FungiDB:Z517_05870; -.
DR HOGENOM; CLU_009902_0_1_1; -.
DR OrthoDB; 1330839at2759; -.
DR Proteomes; UP000053029; 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:UP000053029};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 52..156
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 201..375
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 458 AA; 48386 MW; 70F4F7D9B5FEFDB4 CRC64;
MASPASLGSR ALRASSRHIP VTSLQRRGLA AAASGSFQYE TGEASGVKFA SRDLPGATTT
LTVVAKAGTR YQPLPGYSDA LEKFAFKSTT KRSTLRITRE AELLGGELSA YHSRENLVLR
AKFLREDLPY FTELLGEVIS KTRYTTHELN EEVIHVMKLA QKGLLGSPLS LALNSVHGVA
FHRGLGEPLY ATSSVPIIQY LDAEDVAKFS DSAYVKGNIA VVANGASHAE FSKWVGEFFQ
DTPAGSKLNS PASKYYGGEE RIAHGSGNVL IIGFQGSSSF TAGSSYKPEI AVLASLLGGE
SSIKWSPGFS LLSKAAHDFP QVQVSTQHAA YSDAGLLYIT FTGNAAQIAK ASENAVNTLK
KIAAGEVAEE DIKKATALAK FRALEAGQQT QAGLEATGNG LIEGGKPFQI DEIGSSIDKV
SSDKVKAAAK SLLESKASVS AVGDLFRLPF ASEIGLTV
//
