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Database: UniProt
Entry: V9FMP1_PHYPR
LinkDB: V9FMP1_PHYPR
Original site: V9FMP1_PHYPR 
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
//
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