ID A0A2D0SD66_ICTPU Unreviewed; 642 AA.
AC A0A2D0SD66;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
GN Name=dus3l {ECO:0000313|RefSeq:XP_017340667.1,
GN ECO:0000313|RefSeq:XP_017340668.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017340668.1};
RN [1] {ECO:0000313|RefSeq:XP_017340667.1, ECO:0000313|RefSeq:XP_017340668.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017340667.1,
RC ECO:0000313|RefSeq:XP_017340668.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_017340667.1; XM_017485178.2.
DR RefSeq; XP_017340668.1; XM_017485179.3.
DR RefSeq; XP_017340669.1; XM_017485180.1.
DR Ensembl; ENSIPUT00000006040; ENSIPUP00000005775; ENSIPUG00000004025.
DR GeneID; 108274798; -.
DR CTD; 56931; -.
DR OMA; WSYIAEC; -.
DR OrthoDB; 275918at2759; -.
DR Proteomes; UP000221080; Chromosome 14.
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 Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 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; 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 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 103..133
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 146..171
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 103..133
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 146..171
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 46..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 73223 MW; 3F0B1D104B862985 CRC64;
MEGGDVNSAE GSTIQTTDRG EAALKTQYIT NKENFYEFLA TGFKSEKAED EKASAEVPID
GAEEQSREPE TKKRKVDGDE QTKDKKKRRG QNKSRPHLKP HSYEAQRLCP SLIQESERKC
FYGEKCKFIH DVADYMSTKP EDLGDTCYLY DTFGRCPYGV TCRFAKAHTG PDYKNLVNEE
LRKSLDRTET VRNSLDKELQ RRLRKKQVSF KSSENFLKSI SAGKKQHGKS SMSENTPNEL
RQEEEVSQSE TRQEGPAAEL KTEESQTKPP PVKTIGPLTD DDIIKLRPCE KKQVDFRDKL
YLAPLTTCGN LPFRRVCKRF GADITCGEMA MCTNLLQGQT SEWALLKRHH TEDVFGVQLE
GCFPDSMTRC AELLNHNIDV DFVDINSGCP IDLVYKKGGG CGLMTRANKF EQIVRGMNSV
LDVPLTVKIR TGVQQNCNIA HKLIPELKKW GVSMITLHGR SREQRYTKLA DWSYIDTCSK
LAAPVPLFGN GDVLSYEDAM RARETGVSGI MVARGALIKP WLFTEIKEQR QWDISSSERL
QILRDFTHFG LEHWGSDTQG VEKTRNFLLE WLSFTCRYIP VGLLERVQKI NERPPYYLGR
DYLETLMASQ HVDDWIRISE MLLGPVPKNF SFLPKHKANA YK
//
