ID A0A0M0K3K7_9EUKA Unreviewed; 291 AA.
AC A0A0M0K3K7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Ubiquinone biosynthesis protein {ECO:0000256|RuleBase:RU366063};
GN ORFNames=Ctob_009144 {ECO:0000313|EMBL:KOO32943.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO32943.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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|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:KOO32943.1}.
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DR EMBL; JWZX01001643; KOO32943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0K3K7; -.
DR OrthoDB; 10272at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000037460; 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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Ubiquinone {ECO:0000313|EMBL:KOO32943.1};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688,
KW ECO:0000256|RuleBase:RU366063}.
FT DOMAIN 226..267
FT /note="COQ9 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08511"
FT REGION 54..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 291 AA; 30861 MW; 3AD95E3B1B880040 CRC64;
MLLRAPLRST RLLHAPTVLA SRLAAGRMTR FTVAPSELQR RAYGSKAPID GDAVAEGESK
AAAGEAAGVP QTEKRAPPTD AELRARVLES ALLEVATQGW TTGALAAGAA ACGLSPMAHG
LVLRGPIELV EHFHIKCDSE VSAELAARRE ELAGLEVHNR LLVAMQARLL KVGTYRSSWA
QALALRALPA NLPNTLRDAH ATAVMLLDAC GEDAKVPLLP GAVDPYVKLM SIGAIYGAAE
LHLLTDSSAD LSDTWTFLER EVEALRTMAR GTTSLPDISP SGLVLSLLMR R
//
