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Database: UniProt
Entry: F1L517_ASCSU
LinkDB: F1L517_ASCSU
Original site: F1L517_ASCSU 
ID   F1L517_ASCSU            Unreviewed;       364 AA.
AC   F1L517;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Ubiquinone biosynthesis monooxygenase coq-6 {ECO:0000313|EMBL:ADY45221.1};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY45221.1};
RN   [1] {ECO:0000313|EMBL:ADY45221.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the UbiH/COQ6 family.
CC       {ECO:0000256|ARBA:ARBA00005349}.
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DR   EMBL; JI171488; ADY45221.1; -; mRNA.
DR   AlphaFoldDB; F1L517; -.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR010971; UbiH/COQ6.
DR   NCBIfam; TIGR01988; Ubi-OHases; 1.
DR   PANTHER; PTHR43876; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43876:SF7; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   2: Evidence at transcript level;
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:ADY45221.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Ubiquinone {ECO:0000313|EMBL:ADY45221.1}.
FT   DOMAIN          26..288
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   364 AA;  40298 MW;  7F2D43633032E204 CRC64;
     MSLLSYWTTH LAISARYYSS NANLFYDVVI VGGGMVGNAM ACSMGLSKKL SSKKILLLES
     GDLKPLTKTP IYSNRVSAIS PPSVTFFKKL GIWEKLEKYR VKRVDRLEVI DSCSRSTIRF
     EQPNPSNEIA YIVENDAIIA FLIDRIREQC NNVEIKTNTK VDNCTIPNSL AKLANLKLND
     GTDVSTSLII GADGVKSQIR QSFDVDYTAW EYGQKGVVAT LQVQAEDNNS TAWQRFSKYG
     PIALLPLSAN LSSLVWTTSD EHAEYLLSLT PEHFVDELNY YLTTDASQSP ITNQVLSLAE
     GVLNSLCGTK PTGVPIPTNG DRIAIGYSSC FPSWIRARAL ICGSTCRAYR RCGTSYSSTC
     WTRR
//
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