ID J9G586_9SPIT Unreviewed; 479 AA.
AC J9G586;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=OXYTRI_16707 {ECO:0000313|EMBL:EJY85431.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY85431.1};
RN [1] {ECO:0000313|EMBL:EJY85431.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY85431.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
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}.
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:EJY85431.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMCR01003113; EJY85431.1; -; Genomic_DNA.
DR AlphaFoldDB; J9G586; -.
DR EnsemblProtists; EJY85431; EJY85431; OXYTRI_16707.
DR OrthoDB; 5473786at2759; -.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; 2.
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; 2.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 102..319
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 386..432
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 479 AA; 53643 MW; DDF4EBB97412963A CRC64;
MLVQKSSRNL LRPLISQVQC LRNFSTHFRP VKIPDSQKQH ADVLIVGGGI AGTSLACALA
SSDYFSSNDT SKDKLKRIVV LDHTKLPNIK SYQQEGGEAL KRIPEPRVIT LSPNSLRFLK
SIGVVQKCNQ RFITEFMNML VYEEMGNSYM KFGVKNRQQS ALIQLQESLM KSLLFKSEHS
QQVFEESQSH MGASIENNHL LAGLVERCNE SQKVQIIQKK VVEIYPAKDE HSHLKPIVKL
DDGSYIEADL LIGSDGEKSK VREEYGIHAN GYSYNQNGLV CTVKSIRPNT IAYQRFLRTG
PLALLPLWSD YSSIVWSCHP ELCQHLIDLP ESAFIDALNS ALQKSSDYSL VGGIFPPQKW
QSQQNKFEAP PIIEKLETKR YGFPLSLNLS NNLAANRMAL IGDAAHRVHP LAGQGMNIGI
TGVAFLANSI IKAKKCGYDI GNYDYVLSDY EKQEKVNAQM MVSSIELVKS SYSEMLLLI
//
