DUS3L_HUMAN
ID DUS3L_HUMAN Reviewed; 650 AA.
AC Q96G46; Q96HM5; Q9BSU4; Q9H877; Q9NPR1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like {ECO:0000305};
DE EC=1.3.1.89 {ECO:0000250|UniProtKB:Q06053};
DE AltName: Full=mRNA-dihydrouridine synthase DUS3L {ECO:0000305};
DE EC=1.3.1.- {ECO:0000250|UniProtKB:Q06053};
DE AltName: Full=tRNA-dihydrouridine synthase 3-like {ECO:0000305};
GN Name=DUS3L {ECO:0000303|PubMed:34556860, ECO:0000312|HGNC:HGNC:26920};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP GLY-185.
RC TISSUE=Pancreas, Placenta, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-650 (ISOFORM 2).
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273 AND SER-276, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-416, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [17]
RP FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF CYS-396.
RX PubMed=34556860; DOI=10.1038/s41589-021-00874-8;
RA Dai W., Li A., Yu N.J., Nguyen T., Leach R.W., Wuehr M., Kleiner R.E.;
RT "Activity-based RNA-modifying enzyme probing reveals DUS3L-mediated
RT dihydrouridylation.";
RL Nat. Chem. Biol. 17:1178-1187(2021).
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base,
CC in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs
CC (lncRNAs) (PubMed:34556860). Mainly modifies the uridine in position 47
CC (U47) in the D-loop of most cytoplasmic tRNAs (PubMed:34556860). Also
CC able to mediate the formation of dihydrouridine in some mRNAs, thereby
CC regulating their translation (PubMed:34556860).
CC {ECO:0000269|PubMed:34556860}.
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:0000250|UniProtKB:Q06053};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53366;
CC Evidence={ECO:0000250|UniProtKB:Q06053};
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:0000250|UniProtKB:Q06053};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53362;
CC Evidence={ECO:0000250|UniProtKB:Q06053};
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:0000250|UniProtKB:Q9UTH9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000250|UniProtKB:Q9UTH9};
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:0000250|UniProtKB:Q9UTH9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000250|UniProtKB:Q9UTH9};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC -!- INTERACTION:
CC Q96G46; Q96CV9: OPTN; NbExp=3; IntAct=EBI-5458011, EBI-748974;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96G46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96G46-2; Sequence=VSP_019971, VSP_019972;
CC Name=3;
CC IsoId=Q96G46-3; Sequence=VSP_019970;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily. {ECO:0000305}.
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DR EMBL; AK023958; BAB14740.1; -; mRNA.
DR EMBL; AC011499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004549; AAH04549.1; -; mRNA.
DR EMBL; BC008362; AAH08362.1; -; mRNA.
DR EMBL; BC009973; AAH09973.1; -; mRNA.
DR EMBL; AL365411; CAB96955.1; -; mRNA.
DR CCDS; CCDS32880.1; -. [Q96G46-1]
DR CCDS; CCDS54202.1; -. [Q96G46-3]
DR RefSeq; NP_001155091.1; NM_001161619.1. [Q96G46-3]
DR RefSeq; NP_064560.2; NM_020175.2. [Q96G46-1]
DR AlphaFoldDB; Q96G46; -.
DR SMR; Q96G46; -.
DR BioGRID; 121258; 51.
DR IntAct; Q96G46; 10.
DR STRING; 9606.ENSP00000311977; -.
DR GlyGen; Q96G46; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96G46; -.
DR PhosphoSitePlus; Q96G46; -.
DR BioMuta; DUS3L; -.
DR DMDM; 110808212; -.
DR EPD; Q96G46; -.
DR jPOST; Q96G46; -.
DR MassIVE; Q96G46; -.
DR MaxQB; Q96G46; -.
DR PaxDb; Q96G46; -.
DR PeptideAtlas; Q96G46; -.
DR PRIDE; Q96G46; -.
DR ProteomicsDB; 76593; -. [Q96G46-1]
DR ProteomicsDB; 76594; -. [Q96G46-2]
DR ProteomicsDB; 76595; -. [Q96G46-3]
DR Antibodypedia; 23988; 102 antibodies from 18 providers.
DR DNASU; 56931; -.
DR Ensembl; ENST00000309061.12; ENSP00000311977.5; ENSG00000141994.16. [Q96G46-1]
DR Ensembl; ENST00000320699.12; ENSP00000315558.7; ENSG00000141994.16. [Q96G46-3]
DR GeneID; 56931; -.
DR KEGG; hsa:56931; -.
DR MANE-Select; ENST00000309061.12; ENSP00000311977.5; NM_020175.3; NP_064560.2.
DR UCSC; uc002mdc.4; human. [Q96G46-1]
DR CTD; 56931; -.
DR DisGeNET; 56931; -.
DR GeneCards; DUS3L; -.
DR HGNC; HGNC:26920; DUS3L.
DR HPA; ENSG00000141994; Low tissue specificity.
DR neXtProt; NX_Q96G46; -.
DR OpenTargets; ENSG00000141994; -.
DR PharmGKB; PA142671938; -.
DR VEuPathDB; HostDB:ENSG00000141994; -.
DR eggNOG; KOG2333; Eukaryota.
DR GeneTree; ENSGT00550000075134; -.
DR HOGENOM; CLU_013299_0_2_1; -.
DR InParanoid; Q96G46; -.
DR OMA; IAANKPW; -.
DR PhylomeDB; Q96G46; -.
DR TreeFam; TF105726; -.
DR PathwayCommons; Q96G46; -.
DR SignaLink; Q96G46; -.
DR BioGRID-ORCS; 56931; 23 hits in 1079 CRISPR screens.
DR ChiTaRS; DUS3L; human.
DR GenomeRNAi; 56931; -.
DR Pharos; Q96G46; Tdark.
DR PRO; PR:Q96G46; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96G46; protein.
DR Bgee; ENSG00000141994; Expressed in right testis and 133 other tissues.
DR ExpressionAtlas; Q96G46; baseline and differential.
DR Genevisible; Q96G46; HS.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106414; F:mRNA dihydrouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IDA:UniProtKB.
DR GO; GO:0002943; P:tRNA dihydrouridine synthesis; IDA:UniProtKB.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF01207; Dus; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR PROSITE; PS01136; UPF0034; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Flavoprotein; FMN; Isopeptide bond;
KW Metal-binding; mRNA processing; NAD; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Repeat; tRNA processing; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..650
FT /note="tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like"
FT /id="PRO_0000247342"
FT ZN_FING 118..148
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 156..186
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:34556860"
FT BINDING 311..313
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 365
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 435
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 465
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 497..499
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 520..521
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XI1"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 59..300
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019970"
FT VAR_SEQ 464..482
FT /note="LHGRSREQRYTKLADWQYI -> VGLGTPRALGPRGRPRVPS (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_019971"
FT VAR_SEQ 483..650
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_019972"
FT VARIANT 185
FT /note="R -> G (in dbSNP:rs2436487)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027092"
FT VARIANT 609
FT /note="D -> N (in dbSNP:rs12977803)"
FT /id="VAR_027093"
FT MUTAGEN 396
FT /note="C->A: Abolished synthesis of dihydrouridine."
FT /evidence="ECO:0000269|PubMed:34556860"
FT CONFLICT 134
FT /note="K -> N (in Ref. 1; BAB14740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 72594 MW; B785373796AB88E0 CRC64;
MAEGTAEAPL ENGGGGDSGA GALERGVAPI KRQYLTTKEQ FHQFLEAKGQ EKTCRETEVG
DPAGNELAEP EAKRIRLEDG QTADGQTEEA AEPGEQLQTQ KRARGQNKGR PHVKPTNYDK
NRLCPSLIQE SAAKCFFGDR CRFLHDVGRY LETKPADLGP RCVLFETFGR CPYGVTCRFA
GAHLRPEGQN LVQEELAARG TQPPSIRNGL DKALQQQLRK REVRFERAEQ ALRRFSQGPT
PAAAVPEGTA AEGAPRQENC GAQQVPAGPG TSTPPSSPVR TCGPLTDEDV VRLRPCEKKR
LDIRGKLYLA PLTTCGNLPF RRICKRFGAD VTCGEMAVCT NLLQGQMSEW ALLKRHQCED
IFGVQLEGAF PDTMTKCAEL LSRTVEVDFV DINVGCPIDL VYKKGGGCAL MNRSTKFQQI
VRGMNQVLDV PLTVKIRTGV QERVNLAHRL LPELRDWGVA LVTLHGRSRE QRYTKLADWQ
YIEECVQAAS PMPLFGNGDI LSFEDANRAM QTGVTGIMIA RGALLKPWLF TEIKEQRHWD
ISSSERLDIL RDFTNYGLEH WGSDTQGVEK TRRFLLEWLS FLCRYVPVGL LERLPQRINE
RPPYYLGRDY LETLMASQKA ADWIRISEML LGPVPPSFAF LPKHKANAYK
