ID I0YKY0_COCSC Unreviewed; 669 AA.
AC I0YKY0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00012376, ECO:0000256|RuleBase:RU291113};
DE EC=1.3.1.- {ECO:0000256|RuleBase:RU291113};
DE AltName: Full=tRNA-dihydrouridine synthase 3 {ECO:0000256|RuleBase:RU291113};
GN ORFNames=COCSUDRAFT_19841 {ECO:0000313|EMBL:EIE19049.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE19049.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE19049.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE19049.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
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 -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|RuleBase:RU291113};
CC -!- SIMILARITY: Belongs to the dus family. Dus3 subfamily.
CC {ECO:0000256|RuleBase:RU291113}.
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:EIE19049.1}.
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DR EMBL; AGSI01000020; EIE19049.1; -; Genomic_DNA.
DR RefSeq; XP_005643593.1; XM_005643536.1.
DR AlphaFoldDB; I0YKY0; -.
DR STRING; 574566.I0YKY0; -.
DR GeneID; 17036979; -.
DR KEGG; csl:COCSUDRAFT_19841; -.
DR eggNOG; KOG2333; Eukaryota.
DR OrthoDB; 275918at2759; -.
DR Proteomes; UP000007264; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:UniProtKB-UniRule.
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 InterPro; IPR018517; tRNA_hU_synthase_CS.
DR InterPro; IPR000571; Znf_CCCH.
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.
DR PROSITE; PS01136; UPF0034; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU291113};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|RuleBase:RU291113};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723,
KW ECO:0000256|RuleBase:RU291113}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU291113};
KW Reference proteome {ECO:0000313|Proteomes:UP000007264};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|RuleBase:RU291113};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723, ECO:0000256|RuleBase:RU291113};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723,
KW ECO:0000256|RuleBase:RU291113}.
FT DOMAIN 77..99
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 77..99
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 73537 MW; 88B61E007D457E14 CRC64;
MEKPEESAEA RMSRGLAPIK REYIRKAAPR GTIDDKIYKA EQQRNNGASK VASEKKSRRK
MKKAMHPKAS QFRAGDLCFN HARDQCPYGD KCKFNHDIVA YAAAKQPDLP GRCPSSAMPE
CPYGRCLHTC CLTFCSEHLQ NMHARMPDLP EPPTTNTLDK DLQGSLRRST YDFGRAQEVL
SNLGIKSSWR FGKDTGSKQK AQHPAPENNA PEDQNGHEHE DAQPEIGLQE PDPKRQKTDS
SAPADVSAAA ADASGAADVS IPADVSTAAA DASGACIGAE AAAEAGSAHA ETEATPPVRE
KRRIDFKGKL YLAPLTTVGN LPFRRVCKQL GADITCGEMA LATNLLQGQA SEWALLKRHP
SEDLFGVQVC GGYADSLARC AQLLEEHVDA DFVDVNMGCP IDLVCNRGAG SSLLNKPQRI
EQISRSMSSI LSCPLTIKVR KGYYDGDDNV HAWLPKAPSW GVSAATLHGR TRQQRYTKLA
DWEYIQSATA AAPGLQLIGN GDIMSFTEYN ERTVACPDLA TVMFARGALI KPWLFTEIKE
QRHWDISAGE RLDIFKRFCS HGLLHWGSDA RGVESTRRFL LEWMSFTHRY IPLELMEVVP
QRLHWRAPAY VGRSQLETLL ASESAADWVR ISEMLLGPVP ANFSFAPKHK ANAYANSEGG
MAFEAQAEG
//
