ID H9GJF4_ANOCA Unreviewed; 608 AA.
AC H9GJF4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00012376};
DE EC=1.3.1.89 {ECO:0000256|ARBA:ARBA00012376};
GN Name=dus3l {ECO:0000313|Ensembl:ENSACAP00000012701.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000012701.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000012701.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000012701.3};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000012701.3}
RP IDENTIFICATION.
RG Ensembl;
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 -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005451}.
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DR RefSeq; XP_008121235.1; XM_008123028.2.
DR AlphaFoldDB; H9GJF4; -.
DR STRING; 28377.ENSACAP00000012701; -.
DR Ensembl; ENSACAT00000012957.4; ENSACAP00000012701.3; ENSACAG00000012955.4.
DR GeneID; 100553540; -.
DR KEGG; acs:100553540; -.
DR CTD; 56931; -.
DR eggNOG; KOG2333; Eukaryota.
DR GeneTree; ENSGT00550000075134; -.
DR HOGENOM; CLU_013299_7_0_1; -.
DR InParanoid; H9GJF4; -.
DR OrthoDB; 275918at2759; -.
DR TreeFam; TF105726; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000012955; Expressed in hindlimb bud and 12 other cell types or tissues.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000001646}.
FT DOMAIN 257..499
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 67669 MW; FC38B5C9B93CBFAD CRC64;
MKASQSTSTG AKVSSSLDPG KDPSEGKDGG PNNAETPKSL EPGAPPTKLL KLSSAKPEAS
KGPAVCLKNV KQKNVVCFTG EKCLFGAMCP WQHDLEKYIA TKLPDIGDCC ILFSLFGKCR
FGITCRFGGA HLGSNFQNLV NDELWAVHKG KSAVKNQHLD KAAAALKEFP FHKSSVYLQC
IVKAASMLGI PNVDSKCHLP PVIPSLMPSL AHPKSLASRA GSENLAQKTV GVLTDEDLIR
LRPCEKKKLD FRGKLYLSPL AKWGNLPFRR ICKRFGADIT CSEVISSQDL CQGDLEKCAE
FFHRHESEDF FGIQVEGSAP EHMVKCAEFL NERIQVDFVD INAEGPVLFE KGSGSALMMH
PNTFENIVRG MDYVSNVPIT VKLRSGISLD ENLAHTLIPD LHRWGAAMVT LHGRVKESTF
RSPADWNYIS HCAQIAKPMP LFGCGDIFSF EDVLKAKQTG VSGVMIGRGA LVKPWIFTEI
KEMRHWDISA QERLDMLKEF TDYGLEYWGT DTNGVEKTRA ALVQWLQFLS RYIPVALLEH
QPPKFGNKPP NSLSGDYLEV LMSSRKTKDM VKISEMFLGP VSSDFNFSWI QYMNSYELQQ
DRRQMYML
//
