DED1_YEAST
ID DED1_YEAST Reviewed; 604 AA.
AC P06634; D6W2R0;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=ATP-dependent RNA helicase DED1 {ECO:0000305};
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 1;
DE AltName: Full=Defines essential domain protein 1 {ECO:0000303|PubMed:3001645};
GN Name=DED1 {ECO:0000303|PubMed:3001645}; Synonyms=SPP81;
GN OrderedLocusNames=YOR204W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=A364A X H79-20.3;
RX PubMed=1996139; DOI=10.1038/349715a0;
RA Jamieson D.J., Rahe B., Pringle J., Beggs J.D.;
RT "A suppressor of a yeast splicing mutation (prp8-1) encodes a putative ATP-
RT dependent RNA helicase.";
RL Nature 349:715-717(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
RX PubMed=3001645; DOI=10.1093/nar/13.23.8587;
RA Struhl K.;
RT "Nucleotide sequence and transcriptional mapping of the yeast pet56-his3-
RT ded1 gene region.";
RL Nucleic Acids Res. 13:8587-8601(1985).
RN [5]
RP FUNCTION.
RX PubMed=7835345; DOI=10.1002/j.1460-2075.1995.tb07009.x;
RA Thuillier V., Stettler S., Sentenac A., Thuriaux P., Werner M.;
RT "A mutation in the C31 subunit of Saccharomyces cerevisiae RNA polymerase
RT III affects transcription initiation.";
RL EMBO J. 14:351-359(1995).
RN [6]
RP FUNCTION.
RX PubMed=9144215; DOI=10.1073/pnas.94.10.5201;
RA de la Cruz J., Iost I., Kressler D., Linder P.;
RT "The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent
RT translation in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5201-5206(1997).
RN [7]
RP FUNCTION, CELLULAR LOCATION, AND MUTAGENESIS OF GLY-108; GLY-368 AND
RP GLY-494.
RX PubMed=9045610; DOI=10.1126/science.275.5305.1468;
RA Chuang R.-Y., Weaver P.L., Liu Z., Chang T.-H.;
RT "Requirement of the DEAD-Box protein ded1p for messenger RNA translation.";
RL Science 275:1468-1471(1997).
RN [8]
RP FUNCTION, SINGLE STRAND AND DOUBLE STRAND RNA-BINDING, AND MUTAGENESIS OF
RP GLU-307.
RX PubMed=10364207; DOI=10.1074/jbc.274.25.17677;
RA Iost I., Dreyfus M., Linder P.;
RT "Ded1p, a DEAD-box protein required for translation initiation in
RT Saccharomyces cerevisiae, is an RNA helicase.";
RL J. Biol. Chem. 274:17677-17683(1999).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF LEU-237 AND GLU-317.
RX PubMed=11069307; DOI=10.1073/pnas.240460897;
RA Noueiry A.O., Chen J., Ahlquist P.;
RT "A mutant allele of essential, general translation initiation factor DED1
RT selectively inhibits translation of a viral mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12985-12990(2000).
RN [10]
RP FUNCTION.
RX PubMed=14671320; DOI=10.1073/pnas.2536857100;
RA Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M.,
RA Ahlquist P.;
RT "Systematic, genome-wide identification of host genes affecting replication
RT of a positive-strand RNA virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003).
RN [11]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, RNA-BINDING, AND MUTAGENESIS OF
RP PHE-144; PHE-162; THR-166; GLN-169 AND LYS-192.
RX PubMed=15201868; DOI=10.1038/sj.emboj.7600272;
RA Cordin O., Tanner N.K., Doere M., Linder P., Banroques J.;
RT "The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-
RT binding and helicase activity.";
RL EMBO J. 23:2478-2487(2004).
RN [12]
RP FUNCTION.
RX PubMed=14763975; DOI=10.1046/j.1365-2958.2003.03898.x;
RA Berthelot K., Muldoon M., Rajkowitsch L., Hughes J., McCarthy J.E.G.;
RT "Dynamics and processivity of 40S ribosome scanning on mRNA in yeast.";
RL Mol. Microbiol. 51:987-1001(2004).
RN [13]
RP FUNCTION, AND INTERACTION WITH THE L-A VIRUS GAG PROTEIN AND WITH L-A VIRUS
RP PARTICLES.
RX PubMed=15064363; DOI=10.1093/nar/gkh519;
RA Chong J.-L., Chuang R.-Y., Tung L., Chang T.-H.;
RT "Ded1p, a conserved DExD/H-box translation factor, can promote yeast L-A
RT virus negative-strand RNA synthesis in vitro.";
RL Nucleic Acids Res. 32:2031-2038(2004).
RN [14]
RP FUNCTION.
RX PubMed=16216083; DOI=10.1021/bi0508946;
RA Yang Q., Jankowsky E.;
RT "ATP- and ADP-dependent modulation of RNA unwinding and strand annealing
RT activities by the DEAD-box protein DED1.";
RL Biochemistry 44:13591-13601(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535; SER-539 AND SER-576, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535; SER-539; SER-543 AND
RP SER-572, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [17]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, RNA-BINDING, AND MUTAGENESIS OF
RP PHE-405 AND ARG-486.
RX PubMed=18332124; DOI=10.1128/mcb.01555-07;
RA Banroques J., Cordin O., Doere M., Linder P., Tanner N.K.;
RT "A conserved phenylalanine of motif IV in superfamily 2 helicases is
RT required for cooperative, ATP-dependent binding of RNA substrates in DEAD-
RT box proteins.";
RL Mol. Cell. Biol. 28:3359-3371(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-535; SER-539 AND
RP SER-543, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-218; SER-263;
RP SER-535; SER-539 AND SER-598, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [20]
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 [21]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-158, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [22]
RP METHYLATION AT ARG-62.
RX PubMed=23865587; DOI=10.1021/pr400556c;
RA Low J.K., Hart-Smith G., Erce M.A., Wilkins M.R.;
RT "Analysis of the proteome of Saccharomyces cerevisiae for methylarginine.";
RL J. Proteome Res. 12:3884-3899(2013).
RN [23]
RP METHYLATION AT ARG-51; ARG-62 AND ARG-578.
RX PubMed=26046779; DOI=10.1002/pmic.201500032;
RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O.,
RA Pears C., Schofield C.J., Kessler B.M.;
RT "Expanding the yeast protein arginine methylome.";
RL Proteomics 15:3232-3243(2015).
RN [24]
RP METHYLATION AT ARG-51; ARG-62; ARG-545 AND ARG-578, AND PHOSPHORYLATION AT
RP SER-539 AND SER-543.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
CC -!- FUNCTION: ATP-binding RNA helicase involved in translation initiation.
CC Remodels RNA in response to ADP and ATP concentrations by facilitating
CC disruption, but also formation of RNA duplexes. Has weak ATP-dependent
CC affinity for dsRNA, but strong ATP-dependent affinity for ssRNA. Acts
CC as a virus host factor involved in the replication of the MBV and the
CC L-A viruses by promoting the negative-strand RNA synthesis. May be
CC involved in recognition of the preinitiation complex and DNA binding of
CC the RNA polymerase III and play a role in mRNA splicing.
CC {ECO:0000269|PubMed:10364207, ECO:0000269|PubMed:11069307,
CC ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:14763975,
CC ECO:0000269|PubMed:15064363, ECO:0000269|PubMed:15201868,
CC ECO:0000269|PubMed:16216083, ECO:0000269|PubMed:18332124,
CC ECO:0000269|PubMed:1996139, ECO:0000269|PubMed:7835345,
CC ECO:0000269|PubMed:9045610, ECO:0000269|PubMed:9144215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 mM for ATP {ECO:0000269|PubMed:15201868,
CC ECO:0000269|PubMed:18332124};
CC -!- SUBUNIT: Interacts with the L-A virus GAG protein and the whole L-A
CC virus particles. {ECO:0000269|PubMed:15064363}.
CC -!- INTERACTION:
CC P06634; P24784: DBP1; NbExp=3; IntAct=EBI-5744, EBI-5596;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X57278; CAA40546.1; -; Genomic_DNA.
DR EMBL; Z75110; CAA99419.1; -; Genomic_DNA.
DR EMBL; X03245; CAA27004.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10976.1; -; Genomic_DNA.
DR PIR; S13653; S13653.
DR RefSeq; NP_014847.3; NM_001183623.3.
DR AlphaFoldDB; P06634; -.
DR SMR; P06634; -.
DR BioGRID; 34599; 630.
DR DIP; DIP-5820N; -.
DR IntAct; P06634; 91.
DR MINT; P06634; -.
DR STRING; 4932.YOR204W; -.
DR iPTMnet; P06634; -.
DR MaxQB; P06634; -.
DR PaxDb; P06634; -.
DR PRIDE; P06634; -.
DR EnsemblFungi; YOR204W_mRNA; YOR204W; YOR204W.
DR GeneID; 854379; -.
DR KEGG; sce:YOR204W; -.
DR SGD; S000005730; DED1.
DR VEuPathDB; FungiDB:YOR204W; -.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000168275; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; P06634; -.
DR OMA; IMRGQPV; -.
DR BioCyc; YEAST:G3O-33708-MON; -.
DR BRENDA; 3.6.4.13; 984.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR SABIO-RK; P06634; -.
DR PRO; PR:P06634; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P06634; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IPI:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR GO; GO:0033592; F:RNA strand annealing activity; IDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; IDA:SGD.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IDA:SGD.
DR GO; GO:0006413; P:translational initiation; IMP:SGD.
DR CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044763; Ded1/Dbp1_DEADc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Helicase; Hydrolase;
KW Initiation factor; Isopeptide bond; Methylation; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..604
FT /note="ATP-dependent RNA helicase DED1"
FT /id="PRO_0000055043"
FT DOMAIN 173..362
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 373..533
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..170
FT /note="Q motif"
FT MOTIF 306..309
FT /note="DEAD box"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 51
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 62
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:23865587"
FT MOD_RES 62
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956"
FT MOD_RES 545
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 545
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 578
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 158
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 108
FT /note="G->D: In DED1-120; impairs protein synthesis at 15
FT degrees Celsius; when associated with D-494."
FT /evidence="ECO:0000269|PubMed:9045610"
FT MUTAGEN 144
FT /note="F->A: Slow growth at 18 and 30 degrees Celsius and
FT no growth at 16 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:15201868"
FT MUTAGEN 144
FT /note="F->D,E: Lethal."
FT /evidence="ECO:0000269|PubMed:15201868"
FT MUTAGEN 162
FT /note="F->A: Lethal in vivo and inhibits ATPase and
FT helicase activities in vitro."
FT /evidence="ECO:0000269|PubMed:15201868"
FT MUTAGEN 162
FT /note="F->C: Slow growth at 18 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:15201868"
FT MUTAGEN 162
FT /note="F->L: Reduces RNA-helicase activity about 5-fold in
FT vitro."
FT /evidence="ECO:0000269|PubMed:15201868"
FT MUTAGEN 166
FT /note="T->A: Reduces RNA-helicase activity about 2.5-fold
FT in vitro."
FT /evidence="ECO:0000269|PubMed:15201868"
FT MUTAGEN 166
FT /note="T->S: Slow growth at 18 and 36 degrees Celsius in
FT vivo, and reduces RNA-helicase activity about 5-fold in
FT vitro."
FT /evidence="ECO:0000269|PubMed:15201868"
FT MUTAGEN 169
FT /note="Q->A,E: Lethal in vivo and impairs ATPase and RNA-
FT helicase activities in vitro."
FT /evidence="ECO:0000269|PubMed:15201868"
FT MUTAGEN 169
FT /note="Q->C,D,F,G,H,K,L,M,N,S,T: Lethal."
FT /evidence="ECO:0000269|PubMed:15201868"
FT MUTAGEN 192
FT /note="K->A: Impairs RNA-helicase activity in vitro."
FT /evidence="ECO:0000269|PubMed:15201868"
FT MUTAGEN 237
FT /note="L->M: In DED1-18; impairs BMV RNA synthesis; when
FT associated with D-317."
FT /evidence="ECO:0000269|PubMed:11069307"
FT MUTAGEN 307
FT /note="E->A: Lethal in vivo and impairs ATPase and RNA-
FT helicase activities in vitro."
FT /evidence="ECO:0000269|PubMed:10364207"
FT MUTAGEN 317
FT /note="E->D: In DED1-18; impairs BMV RNA synthesis; when
FT associated with M-237."
FT /evidence="ECO:0000269|PubMed:11069307"
FT MUTAGEN 368
FT /note="G->D: In DED1-199; impairs protein synthesis at 15
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9045610"
FT MUTAGEN 405
FT /note="F->Y,M,L,A,W: Reduces strongly ATPase activity and
FT strand displacement activity."
FT /evidence="ECO:0000269|PubMed:18332124"
FT MUTAGEN 486
FT /note="R->A: Reduces ATPase activity."
FT /evidence="ECO:0000269|PubMed:18332124"
FT MUTAGEN 494
FT /note="G->D: In DED1-120; impairs protein synthesis at 15
FT degrees Celsius; when associated with D-108."
FT /evidence="ECO:0000269|PubMed:9045610"
FT CONFLICT 37
FT /note="S -> M (in Ref. 2; CAA27004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 604 AA; 65553 MW; B6722D94C03BFA4B CRC64;
MAELSEQVQN LSINDNNENG YVPPHLRGKP RSARNNSSNY NNNNGGYNGG RGGGSFFSNN
RRGGYGNGGF FGGNNGGSRS NGRSGGRWID GKHVPAPRNE KAEIAIFGVP EDPNFQSSGI
NFDNYDDIPV DASGKDVPEP ITEFTSPPLD GLLLENIKLA RFTKPTPVQK YSVPIVANGR
DLMACAQTGS GKTGGFLFPV LSESFKTGPS PQPESQGSFY QRKAYPTAVI MAPTRELATQ
IFDEAKKFTY RSWVKACVVY GGSPIGNQLR EIERGCDLLV ATPGRLNDLL ERGKISLANV
KYLVLDEADR MLDMGFEPQI RHIVEDCDMT PVGERQTLMF SATFPADIQH LARDFLSDYI
FLSVGRVGST SENITQKVLY VENQDKKSAL LDLLSASTDG LTLIFVETKR MADQLTDFLI
MQNFRATAIH GDRTQSERER ALAAFRSGAA TLLVATAVAA RGLDIPNVTH VINYDLPSDV
DDYVHRIGRT GRAGNTGLAT AFFNSENSNI VKGLHEILTE ANQEVPSFLK DAMMSAPGSR
SNSRRGGFGR NNNRDYRKAG GASAGGWGSS RSRDNSFRGG SGWGSDSKSS GWGNSGGSNN
SSWW
