ID V9FMP1_PHYPR Unreviewed; 360 AA.
AC V9FMP1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Ubiquinone biosynthesis protein {ECO:0000256|RuleBase:RU366063};
GN ORFNames=F443_04191 {ECO:0000313|EMBL:ETI52729.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI52729.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI52729.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI52729.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) 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:ETI52729.1}.
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DR EMBL; ANIZ01000769; ETI52729.1; -; Genomic_DNA.
DR AlphaFoldDB; V9FMP1; -.
DR EnsemblProtists; ETI52729; ETI52729; F443_04191.
DR eggNOG; KOG2969; Eukaryota.
DR OrthoDB; 10272at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000018721; 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 Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688,
KW ECO:0000256|RuleBase:RU366063}.
FT DOMAIN 73..96
FT /note="Ubiquinone biosynthesis protein COQ9 HTH"
FT /evidence="ECO:0000259|Pfam:PF21392"
FT DOMAIN 180..250
FT /note="COQ9 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08511"
SQ SEQUENCE 360 AA; 38483 MW; C27EA0DC06295533 CRC64;
MLLAIMASRS LIRRSAHLAT AVTSKRTVAH AASVSAIRQS FHTTPRIRLH STQITAASEE
SPKTEPQVDP EQLILAKAMG HVVAHGWTIE ALAAGATDLG YPSVAHGMFS RGAVELVEYF
MDSCLAKLRE TLIVNTEKLQ AMTVAERLKF GVRARLEMLE PVLATWPQGM AIGALPQNAP
STAKRLAMLS DEIWYFAGDK STDLSWYTKR AILTGIYAST ELFMLNDKSP NFQDTWAFLD
RRVDETIQLG ELPQNLNDVA GMASIGLQSV FSAVTSLAGP LAGQIISNSP LSQVPNPISA
VGSVVPPSVV SAVASGMPFN SPASAGPAGH DAMAFKSKDL DEINAELEKL GGADASERRS
//