ID U6GQJ3_EIMAC Unreviewed; 783 AA.
AC U6GQJ3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00012376};
DE EC=1.3.1.89 {ECO:0000256|ARBA:ARBA00012376};
GN ORFNames=EAH_00028200 {ECO:0000313|EMBL:CDI82470.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI82470.1};
RN [1] {ECO:0000313|EMBL:CDI82470.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI82470.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDI82470.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI82470.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(47) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(47) in tRNA; Xref=Rhea:RHEA:53364, Rhea:RHEA-COMP:13539,
CC Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89;
CC Evidence={ECO:0000256|ARBA:ARBA00033625};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53366;
CC Evidence={ECO:0000256|ARBA:ARBA00033625};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(47) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(47) in tRNA; Xref=Rhea:RHEA:53360, Rhea:RHEA-COMP:13539,
CC Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89;
CC Evidence={ECO:0000256|ARBA:ARBA00033656};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53362;
CC Evidence={ECO:0000256|ARBA:ARBA00033656};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA +
CC H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00033653};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000256|ARBA:ARBA00033653};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA +
CC H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00033638};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000256|ARBA:ARBA00033638};
CC -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005451}.
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DR EMBL; HG672419; CDI82470.1; -; Genomic_DNA.
DR RefSeq; XP_013248133.1; XM_013392679.1.
DR AlphaFoldDB; U6GQJ3; -.
DR EnsemblProtists; CDI82470; CDI82470; EAH_00028200.
DR GeneID; 25270890; -.
DR VEuPathDB; ToxoDB:EAH_00028200; -.
DR OMA; NIACPLD; -.
DR OrthoDB; 275918at2759; -.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR PANTHER; PTHR45846; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR PANTHER; PTHR45846:SF1; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR Pfam; PF01207; Dus; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 3: Inferred from homology;
FT DOMAIN 609..764
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT REGION 170..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 83232 MW; 986C9B6A2FC09C77 CRC64;
MATTPLQPSL EGRKDGSAGA AAGLMSIYTT ASATCDGPAL PSFVRFNESH LPSAFPPVFL
AAHAAFCLKD GEAPQVPDYL AACSSAPSSN GNASSALKPL EYSSVHKNDE SVIPSESNIN
QKITPCSHYP ATKPLQRKAL RRTVDFLRQQ NFDFSSLNSS ILMDYGVTRE ASAASTPSSG
TNAAESREKE GEQRQQQAAA KAPLSLPLCN KGESDAPGAA QKDPSEPSSS NSVATDAAAG
AADASVAAAT QQNCSKFAHH GAAQDLGNPL LDSSEDTNSG IAEAPAAVAA REVLSEPSAC
KKRRGLNTAA LRHKNLEQVT NECAASGAFC LSQAACGACD VANCTKDHDV AAFMKARPED
LKGECIFFSR SGLCPFGCCC RFAGSHVDAN GVNLNREGRQ VTLLDLQKYK EEHKSDEMNI
ITTQSVLPMA TRRKRSCKRN KQAAVTTAAT GNENSMQVAS NHSNPSASSS SPLTSLNPLE
SKPPKVETEA GEGGPAQSEA PAAPAAAAAA APAGAAAAVA TARGVGAVDI LPVDDLSREE
RRRRFTQQIR GKTFLAPLTT VGNLPFRRLC TRLGADVTVS EMAVAQSLVE AKASELCLLR
FGKLINETNI QCDFVDLNIA CPLDQLHRKF KAGSIMLEKP AAVESVVKSL MDASPNLPVT
LKVRTAHYGK KHQLHNVIGK LSRCGVSAIF AHGRTAQQRY SKSADWDYLS SCKQHMPEDV
LLIGCGDILS SAEYEYRKAS ANMDALMIGR GALIKPWIFT EIKEERIWDI SAPERFELLR
WVV
//
