DDX21_MOUSE
ID DDX21_MOUSE Reviewed; 851 AA.
AC Q9JIK5; Q3TVJ3; Q9WV45;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Nucleolar RNA helicase 2 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9NR30};
DE AltName: Full=DEAD box protein 21;
DE AltName: Full=Gu-alpha;
DE AltName: Full=Nucleolar RNA helicase Gu;
DE AltName: Full=Nucleolar RNA helicase II;
DE AltName: Full=RH II/Gu;
GN Name=Ddx21;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=10860663; DOI=10.1006/geno.2000.6209;
RA Valdez B.C., Wang W.;
RT "Mouse RNA helicase II/Gu: cDNA and genomic sequences, chromosomal
RT localization, and regulation of expression.";
RL Genomics 66:184-194(2000).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Valdez B.C.;
RL Submitted (APR-2001) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-144; SER-181;
RP SER-192; SER-218; SER-243 AND SER-244, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-155, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-236 AND SER-245, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, INTERACTION WITH TICAM1; DDX1 AND DHX36, IDENTIFICATION IN A
RP COMPLEX WITH DDX1; DHX36 AND TICAM1, SUBUNIT, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21703541; DOI=10.1016/j.immuni.2011.03.027;
RA Zhang Z., Kim T., Bao M., Facchinetti V., Jung S.Y., Ghaffari A.A., Qin J.,
RA Cheng G., Liu Y.J.;
RT "DDX1, DDX21, and DHX36 helicases form a complex with the adaptor molecule
RT TRIF to sense dsRNA in dendritic cells.";
RL Immunity 34:866-878(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP INTERACTION WITH WDR43.
RX PubMed=31128943; DOI=10.1016/j.molcel.2019.05.007;
RA Bi X., Xu Y., Li T., Li X., Li W., Shao W., Wang K., Zhan G., Wu Z.,
RA Liu W., Lu J.Y., Wang L., Zhao J., Wu J., Na J., Li G., Li P., Shen X.;
RT "RNA Targets Ribogenesis Factor WDR43 to Chromatin for Transcription and
RT Pluripotency Control.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: RNA helicase that acts as a sensor of the transcriptional
CC status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA
CC (rRNA) processing and transcription from polymerase II (Pol II) (By
CC similarity). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at
CC lower extent, mRNAs (By similarity). In the nucleolus, localizes to
CC rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes
CC rRNA transcription, processing and modification (By similarity).
CC Required for rRNA 2'-O-methylation, possibly by promoting the
CC recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-
CC ribosomal complexes (By similarity). In the nucleoplasm, binds 7SK RNA
CC and is recruited to the promoters of Pol II-transcribed genes: acts by
CC facilitating the release of P-TEFb from inhibitory 7SK snRNP in a
CC manner that is dependent on its helicase activity, thereby promoting
CC transcription of its target genes (By similarity). Functions as
CC cofactor for JUN-activated transcription: required for phosphorylation
CC of JUN at 'Ser-77' (By similarity). Can unwind double-stranded RNA
CC (helicase) and can fold or introduce a secondary structure to a single-
CC stranded RNA (foldase) (By similarity). Together with SIRT7, required
CC to prevent R-loop-associated DNA damage and transcription-associated
CC genomic instability: deacetylation by SIRT7 activates the helicase
CC activity, thereby overcoming R-loop-mediated stalling of RNA
CC polymerases (By similarity). Involved in rRNA processing. May bind to
CC specific miRNA hairpins (By similarity). Component of a multi-helicase-
CC TICAM1 complex that acts as a cytoplasmic sensor of viral double-
CC stranded RNA (dsRNA) and plays a role in the activation of a cascade of
CC antiviral responses including the induction of pro-inflammatory
CC cytokines via the adapter molecule TICAM1 (PubMed:21703541).
CC {ECO:0000250|UniProtKB:Q9NR30, ECO:0000269|PubMed:21703541}.
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 Evidence={ECO:0000250|UniProtKB:Q9NR30};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q9NR30};
CC -!- ACTIVITY REGULATION: Acetylation inhibits the helicase activity.
CC {ECO:0000250|UniProtKB:Q9NR30}.
CC -!- SUBUNIT: Homodimer; homodimerizes via its N-terminus (PubMed:21703541).
CC Found in a multi-helicase-TICAM1 complex at least composed of DHX36,
CC DDX1, DDX21 and TICAM1; this complex exists in resting cells with or
CC without poly(I:C) RNA ligand stimulation (PubMed:21703541). Interacts
CC (via C-terminus) with TICAM1 (via TIR domain) (PubMed:21703541).
CC Interacts with DHX36 (via C-terminus); this interaction serves as
CC bridges to TICAM1 (PubMed:21703541). Interacts (via C-terminus) with
CC DDX1 (via B30.2/SPRY domain); this interaction serves as bridges to
CC TICAM1 (PubMed:21703541). Component of the B-WICH complex, at least
CC composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6,
CC MYBBP1A and DDX21. Interacts with C1QBP. Interacts with JUN. Interacts
CC with WDR46. Interacts with MCM3AP (By similarity). Interacts with WDR43
CC (PubMed:31128943). {ECO:0000250|UniProtKB:Q9NR30,
CC ECO:0000269|PubMed:21703541, ECO:0000269|PubMed:31128943}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9NR30}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9NR30}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:21703541}. Mitochondrion
CC {ECO:0000303|PubMed:21703541}. Note=Present both in nucleolus and
CC nucleoplasm. Interaction with JUN promotes translocation from the
CC nucleolus to the nucleoplasm. Interaction with WDR46 is required for
CC localization to the nucleolus. Colocalizes in the cytosol with DDX1,
CC DHX36 and TICAM1 (PubMed:21703541). The multi-helicase-TICAM1 complex
CC may translocate to the mitochondria upon poly(I:C) RNA ligand
CC stimulation (PubMed:21703541). {ECO:0000250|UniProtKB:Q9NR30,
CC ECO:0000269|PubMed:21703541}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and testis. Expressed at
CC lower level in brain, lungs, and skeletal muscle.
CC {ECO:0000269|PubMed:10860663}.
CC -!- DOMAIN: The helicase and foldase activities reside in two separate
CC domains, the helicase in the N-terminus and the foldase in the C-
CC terminus. {ECO:0000250|UniProtKB:Q9NR30}.
CC -!- DOMAIN: The 3 X 5 AA repeats seem to be critical for the RNA folding
CC activity. {ECO:0000250}.
CC -!- PTM: Acetylation by CREBBP/CBP inhibits the helicase activity.
CC Deacetylation by SIRT7 promotes the helicase activity and overcomes R-
CC loop-mediated stalling of RNA polymerases.
CC {ECO:0000250|UniProtKB:Q9NR30}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC subfamily. {ECO:0000305}.
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DR EMBL; AF220365; AAF61690.1; -; Genomic_DNA.
DR EMBL; AF159131; AAD43959.3; -; mRNA.
DR EMBL; AK160095; BAE35625.1; -; mRNA.
DR EMBL; CH466553; EDL32086.1; -; Genomic_DNA.
DR EMBL; BC043655; AAH43655.1; -; mRNA.
DR CCDS; CCDS23891.1; -.
DR RefSeq; NP_062426.2; NM_019553.2.
DR PDB; 3ZIN; X-ray; 2.00 A; B/C=839-851.
DR PDBsum; 3ZIN; -.
DR AlphaFoldDB; Q9JIK5; -.
DR SMR; Q9JIK5; -.
DR BioGRID; 207838; 14.
DR ComplexPortal; CPX-1133; B-WICH chromatin remodelling complex.
DR CORUM; Q9JIK5; -.
DR DIP; DIP-48574N; -.
DR IntAct; Q9JIK5; 5.
DR MINT; Q9JIK5; -.
DR STRING; 10090.ENSMUSP00000042691; -.
DR iPTMnet; Q9JIK5; -.
DR PhosphoSitePlus; Q9JIK5; -.
DR SwissPalm; Q9JIK5; -.
DR EPD; Q9JIK5; -.
DR jPOST; Q9JIK5; -.
DR MaxQB; Q9JIK5; -.
DR PaxDb; Q9JIK5; -.
DR PeptideAtlas; Q9JIK5; -.
DR PRIDE; Q9JIK5; -.
DR ProteomicsDB; 279324; -.
DR Antibodypedia; 14684; 273 antibodies from 26 providers.
DR DNASU; 56200; -.
DR Ensembl; ENSMUST00000045866; ENSMUSP00000042691; ENSMUSG00000020075.
DR GeneID; 56200; -.
DR KEGG; mmu:56200; -.
DR UCSC; uc007fhn.1; mouse.
DR CTD; 9188; -.
DR MGI; MGI:1860494; Ddx21.
DR VEuPathDB; HostDB:ENSMUSG00000020075; -.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00940000155043; -.
DR HOGENOM; CLU_003041_20_0_1; -.
DR InParanoid; Q9JIK5; -.
DR OMA; RTFQPIY; -.
DR OrthoDB; 1139373at2759; -.
DR PhylomeDB; Q9JIK5; -.
DR TreeFam; TF328622; -.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 56200; 26 hits in 76 CRISPR screens.
DR ChiTaRS; Ddx21; mouse.
DR PRO; PR:Q9JIK5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9JIK5; protein.
DR Bgee; ENSMUSG00000020075; Expressed in epiblast (generic) and 275 other tissues.
DR Genevisible; Q9JIK5; MM.
DR GO; GO:0110016; C:B-WICH complex; ISO:MGI.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:MGI.
DR GO; GO:0097322; F:7SK snRNA binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:MGI.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; IMP:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:MGI.
DR GO; GO:0062176; P:R-loop disassembly; ISS:UniProtKB.
DR GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
DR GO; GO:0009615; P:response to virus; IMP:MGI.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR IDEAL; IID50235; -.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR012562; GUCT.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08152; GUCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54928; SSF54928; 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 3D-structure; Acetylation; Antiviral defense; ATP-binding; Cytoplasm;
KW Helicase; Hydrolase; Immunity; Innate immunity; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; rRNA processing; Transcription.
FT CHAIN 1..851
FT /note="Nucleolar RNA helicase 2"
FT /id="PRO_0000055028"
FT REPEAT 117..153
FT /note="1-1"
FT REPEAT 154..190
FT /note="1-2"
FT REPEAT 191..227
FT /note="1-3"
FT DOMAIN 289..468
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 501..645
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REPEAT 807..811
FT /note="2-1"
FT REPEAT 817..823
FT /note="2-2"
FT REPEAT 829..833
FT /note="2-3"
FT REGION 1..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..227
FT /note="3 X 37 AA tandem repeats"
FT REGION 783..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..833
FT /note="3 X 5 AA repeats"
FT MOTIF 258..286
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 411..414
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 21..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR30"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR30"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 134
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR30"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR30"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR30"
FT MOD_RES 672
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR30"
FT MOD_RES 847
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR30"
FT CONFLICT 1..46
FT /note="Missing (in Ref. 1; AAF61690)"
FT /evidence="ECO:0000305"
FT CONFLICT 790
FT /note="P -> Q (in Ref. 1; AAD43959)"
FT /evidence="ECO:0000305"
FT HELIX 845..849
FT /evidence="ECO:0007829|PDB:3ZIN"
SQ SEQUENCE 851 AA; 93551 MW; 7066986F4CA0DCD7 CRC64;
MPGKLRSGAK LGSDGAEESM ETLPKPSEKK TRKEKTKSKT EEATEGMEEA VSSKAKKTNK
KGPSEDDVDP PKSRKAKKQE EEPQDDTAST SKTSKKKKEP LEKQADSETK EIITEEPSEE
EADMPKPKKM KKGKEANGDA GEKSPKLKNG LSQPSEEEAD IPKPKKMKKG KEANGDAGEK
SPKLKNGLSQ PSEEEVDIPK PKKMKKGKEA SGDAGEKSPR LKDGLSQPSE PKSNSSDAPG
EESSSETEKE IPVEQKEGAF SNFPISEETV KLLKARGVNF LFPIQAKTFH HVYSGKDLIA
QARTGTGKTF SFAIPLIEKL QGGLQERKRG RAPQVLVLAP TRELANQVSK DFSDITKKLS
VACFYGGTPY GGQIERMRSG IDILVGTPGR IKDHLQNGKL DLTKLKHVVL DEVDQMLDMG
FADQVEEILC VAYKKDSEDN PQTLLFSATC PHWVFNVAKK YMKSTYEQVD LIGKKTQKAA
ITVEHLAIKC HWTERAAVIG DVIRVYSGHQ GRTIIFCETK KDAQELSQNT CIKQDAQSLH
GDIPQKQREI TLKGFRNGNF GVLVATNVAA RGLDIPEVDL VVQSCPPKDV ESYIHRSGRT
GRAGRTGVCI CFYQNKEEYQ LAQVEQKAGI KFKRIGVPSA TEIIKASSKD AIRLLDSVPP
TAISHFKQSA EKLIEEKGAV EALAAALAHI SGATSVDQRS LINSQAGFVT MILRCSIEMP
NISYAWKELK EQLGESIDAK VKGMVFLKGK LGVCFDVRTE AVTEIQEKWH DSRRWQLTVA
TEQPELEGPP DGYRGRMGQR DGSRGAFRGQ RGGSRNFRGQ GQRGGSRNFR GQRPGGGNRG
QKRSFSKAFG Q
