ID E1ZWN9_CAMFO Unreviewed; 525 AA.
AC E1ZWN9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Ubiquinone biosynthesis protein {ECO:0000256|RuleBase:RU366063};
GN ORFNames=EAG_01133 {ECO:0000313|EMBL:EFN74397.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN74397.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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 EMBL; GL434869; EFN74397.1; -; Genomic_DNA.
DR AlphaFoldDB; E1ZWN9; -.
DR STRING; 104421.E1ZWN9; -.
DR InParanoid; E1ZWN9; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000311; 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 InterPro; IPR013877; YAP-bd/ALF4/Glomulin.
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.
DR Pfam; PF08568; Kinetochor_Ybp2; 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:UP000000311};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Ubiquinone {ECO:0000313|EMBL:EFN74397.1};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688,
KW ECO:0000256|RuleBase:RU366063}.
FT DOMAIN 297..327
FT /note="Ubiquinone biosynthesis protein COQ9 HTH"
FT /evidence="ECO:0000259|Pfam:PF21392"
FT DOMAIN 415..483
FT /note="COQ9 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08511"
SQ SEQUENCE 525 AA; 60626 MW; EE5EB00311498E98 CRC64;
MSQIFVKRFT GFLEDHKPEE ALRLFTTESN KVIEDSVSEI VSITATYLTE SNLQSEQELF
ECCKNVLNVI AKKCNPMETV LEFLEQIECL NNDIKFCAIL EPLGICMMKM QDKSKAIEWC
INTIKSYIED LTSLHDADSD RIVNVYRRII LFLEPLVQEV FLGKNLELML KKICNLPYGS
SSDLVEISDE VITVLNLLRF LFIRDKHNET GIWNITDMLE NDYLNPLREG IDLCRAHWKV
KIKDLEQQKK NYNKIHDYSF RHLWTSRALL SDQSENDNNK KKEPQQFIHE ETDEEYEKNI
KTKILCASLK FVPEMGWSKQ AISAGAESIG YPGVIHGLFP NGGAALVLHF YSMSNHKLNQ
MLEKETLAIE TDPSNPRKMP EQQIHDAIET RLRMVIPYKK TWSQALAIMT LPPNVPTALA
NLLTLIDDIC YYAGDRSVDI NWYTRRMILA TIYKATELYM LQDTSEDHKK TWLFLDRRIK
DALHVYAMLS SSAKSSPDET LSYVTEMATS VFVTARNIVG LSWNR
//