ID A0A1A9WI49_9MUSC Unreviewed; 338 AA.
AC A0A1A9WI49;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Ubiquinone biosynthesis protein {ECO:0000256|RuleBase:RU366063};
OS Glossina brevipalpis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI020660-PA, ECO:0000313|Proteomes:UP000091820};
RN [1] {ECO:0000313|Proteomes:UP000091820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GBRI020660-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI020660-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A1A9WI49; -.
DR STRING; 37001.A0A1A9WI49; -.
DR EnsemblMetazoa; GBRI020660-RA; GBRI020660-PA; GBRI020660.
DR VEuPathDB; VectorBase:GBRI020660; -.
DR OrthoDB; 10272at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000091820; 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 121..148
FT /note="Ubiquinone biosynthesis protein COQ9 HTH"
FT /evidence="ECO:0000259|Pfam:PF21392"
FT DOMAIN 233..302
FT /note="COQ9 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08511"
FT REGION 70..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 338 AA; 38573 MW; D70675E624910A8A CRC64;
MANLSSLCKF IQLPKLVNNK TGINFRTIYR SLSSSINQST YVNIPPADCK VRYTTKVTLQ
IQAQASHHRH LCSKNTNDPV KPGLDEFRER EEKKEEEFEQ REREKARAAS DDTNDAKINA
IRMKILEAAL PHVPTSGWTR ETIMLGAEEM GFPGVAHGMF PEGGFALVSY FIGKCNAELL
KQMKTETDNG RKAIHDPIEF LVDFVRIRLE MILPYKSQWP QAIALIALPQ NAATSLAQLL
TLVDDICYYS GDRSVDIEWY TRRIGLATVM KMTELYMLRD KSPQHINTWE FLENRLNEFS
QLQTILSQTE DVTKTFQNSL NSAFITARNM LGLGYNRP
//
