ID A0A135TYL8_9PEZI Unreviewed; 256 AA.
AC A0A135TYL8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Ubiquinone biosynthesis protein {ECO:0000256|RuleBase:RU366063};
GN ORFNames=CSIM01_13086 {ECO:0000313|EMBL:KXH53240.1};
OS Colletotrichum simmondsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH53240.1, ECO:0000313|Proteomes:UP000070328};
RN [1] {ECO:0000313|EMBL:KXH53240.1, ECO:0000313|Proteomes:UP000070328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS122122 {ECO:0000313|EMBL:KXH53240.1,
RC ECO:0000313|Proteomes:UP000070328};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipid-binding protein involved in the biosynthesis of
CC coenzyme Q, also named ubiquinone, an essential lipid-soluble electron
CC transporter for aerobic cellular respiration.
CC {ECO:0000256|RuleBase:RU366063}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004749, ECO:0000256|RuleBase:RU366063}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU366063}.
CC -!- SIMILARITY: Belongs to the COQ9 family. {ECO:0000256|ARBA:ARBA00010766,
CC ECO:0000256|RuleBase:RU366063}.
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:KXH53240.1}.
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DR EMBL; JFBX01000023; KXH53240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135TYL8; -.
DR OrthoDB; 10272at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000070328; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.357.10; Tetracycline Repressor, domain 2; 1.
DR InterPro; IPR013718; COQ9_C.
DR InterPro; IPR048674; COQ9_HTH.
DR InterPro; IPR012762; Ubiq_biosynth_COQ9.
DR NCBIfam; TIGR02396; diverge_rpsU; 1.
DR PANTHER; PTHR21427; UBIQUINONE BIOSYNTHESIS PROTEIN COQ9, MITOCHONDRIAL; 1.
DR PANTHER; PTHR21427:SF19; UBIQUINONE BIOSYNTHESIS PROTEIN COQ9, MITOCHONDRIAL; 1.
DR Pfam; PF08511; COQ9; 1.
DR Pfam; PF21392; COQ9_N; 1.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121,
KW ECO:0000256|RuleBase:RU366063};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU366063};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688,
KW ECO:0000256|RuleBase:RU366063}.
FT DOMAIN 51..75
FT /note="Ubiquinone biosynthesis protein COQ9 HTH"
FT /evidence="ECO:0000259|Pfam:PF21392"
FT DOMAIN 157..227
FT /note="COQ9 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08511"
SQ SEQUENCE 256 AA; 28464 MW; D4D44D607BB76551 CRC64;
MSVPCRPTAS LAFRSLRQCP RASAIAPRTT RAYHSYDHPD PITTFHPHES TILSAAYKHV
PEYGFSQKAL ALGAKDTGYL DISTSVLLDG PFSLIRYHLV TKREGLANKE KELFGESSQV
GISEKVELLT WERLLENKTV IDRWQEALAV MAQPSYVPAS LKELAKLVDE IWFLSGDTAV
DPSWYTKRAS LSMIYASSEL FMTNDKSAGF KDTRDFLRRR LSEVKEAGGV MGSLGQWVGF
TASAGVNVLR SKGIRI
//
