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Database: UniProt
Entry: A0A4U0TTF0_9PEZI
LinkDB: A0A4U0TTF0_9PEZI
Original site: A0A4U0TTF0_9PEZI 
ID   A0A4U0TTF0_9PEZI        Unreviewed;       451 AA.
AC   A0A4U0TTF0;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=B0A50_05392 {ECO:0000313|EMBL:TKA25531.1};
OS   Salinomyces thailandica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Salinomyces.
OX   NCBI_TaxID=706561 {ECO:0000313|EMBL:TKA25531.1, ECO:0000313|Proteomes:UP000308549};
RN   [1] {ECO:0000313|EMBL:TKA25531.1, ECO:0000313|Proteomes:UP000308549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 6315 {ECO:0000313|EMBL:TKA25531.1,
RC   ECO:0000313|Proteomes:UP000308549};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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:TKA25531.1}.
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DR   EMBL; NAJL01000034; TKA25531.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U0TTF0; -.
DR   Proteomes; UP000308549; 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:UP000308549};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          48..151
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          194..370
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   451 AA;  48557 MW;  F17A0DAE54535813 CRC64;
     MLSRSAVRSA ARQAWQQQRR GLAAPASGSF QYQTGEAHGV KIASRDIPGP VGSLAIVSKA
     GTRFQHLPGL AEGLNRYAFK NTERRTSLRI QRESELLGAA LQSHHTRENL VVGAKFLRDD
     LPYFVELLAE VATMTKYRAH VMSEEVLPLV QLDQKTYLAN TLEMAVNSAY GVAFHRGLGV
     PLKPASSTPI SKYLTVENLE EYAACAYATP NFALVGNGVE HSELSKWVNE FFGDVSSQAP
     HALGGEQTKY YGGEERISHA GGNSLVLAFP GSSAPTGAFY KPEASVLAAL LGGQSTIKWT
     PGFSLLSNAT QDAPNMHIVT KSNIFSDAGL LTIEMNGSAN DIRRTAGKVV DALKACSENI
     SDEQFQKAKA LAKFKELEHG QLPQAAMELT GAGLVQGNKA YQIDEVAKNL DSVTVDKVKQ
     FAKEALENKA SVSAVGDLYV LPYAEEIGLK V
//
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