ID A0A093PIT8_9PASS Unreviewed; 657 AA.
AC A0A093PIT8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)] {ECO:0000256|RuleBase:RU291113};
DE EC=1.3.1.- {ECO:0000256|RuleBase:RU291113};
DE AltName: Full=tRNA-dihydrouridine synthase 3 {ECO:0000256|RuleBase:RU291113};
DE Flags: Fragment;
GN ORFNames=N305_10269 {ECO:0000313|EMBL:KFW76351.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW76351.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW76351.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW76351.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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 -!- 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}.
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DR EMBL; KL669410; KFW76351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093PIT8; -.
DR STRING; 328815.ENSMVIP00005027924; -.
DR Proteomes; UP000053258; 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 SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS01136; UPF0034; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
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:UP000053258};
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 102..132
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 145..170
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 102..132
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 145..170
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW76351.1"
FT NON_TER 657
FT /evidence="ECO:0000313|EMBL:KFW76351.1"
SQ SEQUENCE 657 AA; 73697 MW; D25D9CFF5F03D9FD CRC64;
RRFLTSKEEF HAFLRAGSEP GSQVGDEGKE EKKEEDEEKK EEQEEQVSSC QSEPPAKRVR
AEDLGQDEEN QEGAGADEKE LPERKRARGQ NKSRPCMKPN HYEQSRLCPS VTQGCPGKCF
YGPRCRFLHD VGEYLAGKPS DLGQRCVLFD TFGRCPYGVT CRFACAHLGD GHQNIVNAAL
AQQWEGKLLV RNNLSKDLQH QLRKRKFVFQ KAEEYLRGLK PRGGDGKGGK AMGEQEVSNC
AAPQEGLGDG DSHECPVLWE QGEDPKAEAL QSPSSRGDGV APSVPTVGPL TDEDVTKLRP
CEKKKLEIQG KLYLAPLTTC GNLPFRRICK RFGADVTCGE MAVCTNLLQG QSSEWALLKR
HHTEDIFGVQ LEGAFPDTMT KCAELLNRTI EVDFVDINVG CPIDLVYKKG GGCALMTRSN
KFEQIVRGMN SVLDVPLTVK IRTGVQEKIN VAHKIIPKIR EWGASMVTLH GRSREQRYTR
SADWEYIAEC AKIASPMPLF GNGDILSYED ANRAMEMGVS GIMIARQVFV GALIKPWLFT
EIKEQRHWDI SSGERFDILK DFTNYGLEHW GSDTQGVEKT RTLTAVPSHP RYIPVGLLEH
LPQRINERPP YYLGRDYLET LMASQNVDDW IRISELLLGP VPPSFTFLPK HKANSYR
//
