ID A0A1V6SHJ8_9EURO Unreviewed; 291 AA.
AC A0A1V6SHJ8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Ubiquinone biosynthesis protein {ECO:0000256|RuleBase:RU366063};
GN ORFNames=PENFLA_c048G07454 {ECO:0000313|EMBL:OQE13416.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE13416.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE13416.1}.
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DR EMBL; MLQL01000048; OQE13416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6SHJ8; -.
DR STRING; 254877.A0A1V6SHJ8; -.
DR OrthoDB; 10272at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000191342; 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:UP000191342};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688,
KW ECO:0000256|RuleBase:RU366063}.
FT DOMAIN 193..262
FT /note="COQ9 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08511"
FT REGION 30..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 291 AA; 32087 MW; B977219E23EEA475 CRC64;
MAYFARTLPK RVLTPSLPQS IRQTRAIATT TLQSTPTRPA QTTPRTSKPR QLPHRTYHSA
LHSRLPDHSY TNSQTAILTS ALAHVPAHGF TATALTLGAR DAGFLDVSVQ LLPRAEFDLI
LFWLASRRGL LRGQVEEGGL FRRIAAEKGK DVHELSVEER VRGLILERLR MNAEVKGVWQ
DALAQMSLLA NIPLSLTELH ALASDILTLS GDDAVDATWY TRRLAVSAIY ASAEVVMTRD
PTPDLVETEA FVERRFEDRK AIADKLTGIG QCAGFGWNTA IGLGRSWGLK I
//
