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Database: UniProt
Entry: Q28141
LinkDB: Q28141
Original site: Q28141 
ID   DHX9_BOVIN              Reviewed;        1287 AA.
AC   Q28141;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-OCT-2019, entry version 142.
DE   RecName: Full=ATP-dependent RNA helicase A {ECO:0000250|UniProtKB:Q08211};
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:Q08211};
DE   AltName: Full=DEAH box protein 9 {ECO:0000250|UniProtKB:O70133};
DE   AltName: Full=Nuclear DNA helicase II {ECO:0000250|UniProtKB:Q08211};
DE            Short=NDH II {ECO:0000250|UniProtKB:Q08211};
GN   Name=DHX9 {ECO:0000250|UniProtKB:Q08211};
GN   Synonyms=DDX9 {ECO:0000250|UniProtKB:Q08211}, NDH2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thymus;
RX   PubMed=7608213; DOI=10.1074/jbc.270.27.16422;
RA   Zhang S., Maacke H., Grosse F.;
RT   "Molecular cloning of the gene encoding nuclear DNA helicase II. A
RT   bovine homologue of human RNA helicase A and Drosophila Mle protein.";
RL   J. Biol. Chem. 270:16422-16427(1995).
RN   [2]
RP   FUNCTION AS AN ATP-DEPENDENT HELICASE, DNA-BINDING, AND RNA-BINDING.
RX   PubMed=7511411; DOI=10.1021/bi00179a016;
RA   Zhang S., Grosse F.;
RT   "Nuclear DNA helicase II unwinds both DNA and RNA.";
RL   Biochemistry 33:3906-3912(1994).
CC   -!- FUNCTION: Multifunctional ATP-dependent nucleic acid helicase that
CC       unwinds DNA and RNA in a 3' to 5' direction and that plays
CC       important roles in many processes, such as DNA replication,
CC       transcriptional activation, post-transcriptional RNA regulation,
CC       mRNA translation and RNA-mediated gene silencing (PubMed:7511411).
CC       Requires a 3'-single-stranded tail as entry site for acid nuclei
CC       unwinding activities as well as the binding and hydrolyzing of any
CC       of the four ribo- or deoxyribo-nucleotide triphosphates (NTPs)
CC       (PubMed:7511411). Unwinds numerous nucleic acid substrates such as
CC       double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA
CC       forks composed of either partially complementary DNA duplexes or
CC       DNA:RNA hybrids, respectively, and also DNA and RNA displacement
CC       loops (D- and R-loops), triplex-helical DNA (H-DNA) structure and
CC       DNA and RNA-based G-quadruplexes (PubMed:7511411). Binds dsDNA,
CC       single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing
CC       RNA (PubMed:7511411). Binds also to circular dsDNA or dsRNA of
CC       either linear and/or circular forms and stimulates the relaxation
CC       of supercoiled DNAs catalyzed by topoisomerase TOP2A. Plays a role
CC       in DNA replication at origins of replication and cell cycle
CC       progression. Plays a role as a transcriptional coactivator acting
CC       as a bridging factor between polymerase II holoenzyme and
CC       transcription factors or cofactors, such as BRCA1, CREBBP, RELA
CC       and SMN1. Binds to the CDKN2A promoter. Plays several roles in
CC       post-transcriptional regulation of gene expression. In cooperation
CC       with NUP98, promotes pre-mRNA alternative splicing activities of a
CC       subset of genes. As component of a large PER complex, is involved
CC       in the negative regulation of 3' transcriptional termination of
CC       circadian target genes such as PER1 and NR1D1 and the control of
CC       the circadian rhythms. Acts also as a nuclear resolvase that is
CC       able to bind and neutralize harmful massive secondary double-
CC       stranded RNA structures formed by inverted-repeat Alu
CC       retrotransposon elements that are inserted and transcribed as
CC       parts of genes during the process of gene transposition. Involved
CC       in the positive regulation of nuclear export of constitutive
CC       transport element (CTE)-containing unspliced mRNA. Component of
CC       the coding region determinant (CRD)-mediated complex that promotes
CC       cytoplasmic MYC mRNA stability. Plays a role in mRNA translation.
CC       Positively regulates translation of selected mRNAs through its
CC       binding to post-transcriptional control element (PCE) in the 5'-
CC       untranslated region (UTR). Involved with LARP6 in the translation
CC       stimulation of type I collagen mRNAs for CO1A1 and CO1A2 through
CC       binding of a specific stem-loop structure in their 5'-UTRs.
CC       Stimulates LIN28A-dependent mRNA translation probably by
CC       facilitating ribonucleoprotein remodeling during the process of
CC       translation. Plays also a role as a small interfering (siRNA)-
CC       loading factor involved in the RNA-induced silencing complex
CC       (RISC) loading complex (RLC) assembly, and hence functions in the
CC       RISC-mediated gene silencing process. Binds preferentially to
CC       short double-stranded RNA, such as those produced during rotavirus
CC       intestinal infection. This interaction may mediate NLRP9
CC       inflammasome activation and trigger inflammatory response,
CC       including IL18 release and pyroptosis. Finally, mediates the
CC       attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to
CC       actin filaments in the nucleus. {ECO:0000250|UniProtKB:Q08211}.
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:Q08211};
CC   -!- SUBUNIT: Component of the coding region determinant (CRD)-mediated
CC       complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1.
CC       Identified in a mRNP complex, at least composed of DHX9, DDX3X,
CC       ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2,
CC       SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule
CC       complex containing untranslated mRNAs. The large PER complex
CC       involved in the repression of transcriptional termination is
CC       composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A
CC       (active). Associates (via DRBM domains) with the RISC complex;
CC       this association occurs in a small interfering (siRNA)-dependent
CC       manner. Associates with the SMN complex; this association induces
CC       recruitment of DHX9 to the RNA polymerase II. Associates with
CC       polysomes in a LIN28A-dependent manner. Interacts (via C-terminus)
CC       with ACTB; this interaction is direct and mediates the attachment
CC       to nuclear ribonucleoprotein complexes. Interacts with ADAR
CC       isoform 1; this interaction occurs in a RNA-independent manner.
CC       Interacts (via DRBM domains) with AGO2 (via middle region); this
CC       interaction promotes active RISC assembly by promoting the
CC       association of siRNA with AGO2. Interacts (via NTD domain) with
CC       AKAP8L (via N-terminus). Interacts with BRCA1 (via C-terminus);
CC       this interaction is direct and links BRCA1 to the RNA polymerase
CC       II holoenzyme. Interacts (via N-terminus) with CREBBP; this
CC       interaction mediates association with RNA polymerase II holoenzyme
CC       and stimulates CREB-dependent transcriptional activation.
CC       Interacts (via N-terminus) with EIF2AK2/PKR; this interaction is
CC       dependent upon the activation of the kinase. Interacts (via DRBM
CC       domains) with DICER1. Interacts with H2AFX; this interaction is
CC       direct, requires phosphorylation of histone H2AFX by PRKDC and
CC       promotes binding of DHX9 to transcriptionally stalled sites on
CC       chromosomal DNA in response to genotoxic stress. Interacts with
CC       HNRNPC; this interaction is direct, enhanced probably by their
CC       concomitant binding to RNA and mediates the attachment to actin
CC       filaments. Interacts (via NTD domain) with PRMT1. Interacts with
CC       IGF2BP1. Interacts with IGF2BP2, IGF2BP3. Interacts (via DRBM
CC       domains) with ILF3; this interaction occurs in a RNA-independent
CC       manner. Interacts with Importin alpha/Importin beta receptor.
CC       Interacts with LARP6 (via C-terminus); this interaction occurs in
CC       a mRNA-independent manner. Interacts (via N- and C-terminus) with
CC       LIN28A (via C-terminus); this interaction occurs in a RNA-
CC       independent manner. Interacts with LMX1B. Interacts (via helicase
CC       C-terminal domain, HA2 and OB-fold regions) with MAVS (via CARD
CC       domain); this interaction occurs in both resting and double-
CC       stranded RNA poly(I:C)-induced cells. Interacts with MBD2; this
CC       interaction stimulates transcriptional activation in a CREB-
CC       dependent manner. Interacts (via H2A and OB-fold regions) with
CC       MYD88 (via TIR domain); this interaction is direct. Interacts with
CC       NLRP9 upon rotavirus infection; this interaction may trigger NLRP9
CC       inflammasome activation and inflammatory response. Interacts (via
CC       DRBM, OB-fold and RGG regions) with NUP98 (via N-terminus); this
CC       interaction occurs in a RNA-dependent manner and stimulates DHX9-
CC       mediated ATPase activity and regulates transcription and splicing
CC       of a subset of genes. Interacts (via N-terminus) with NXF1 (via N-
CC       terminus); this interaction is direct and negatively regulates
CC       NXF1-mediated nuclear export of constitutive transport element
CC       (CTE)-containing cellular mRNAs. Interacts with RELA; this
CC       interaction is direct and activates NF-kappa-B-mediated
CC       transcription. Interacts (via MTAD region) with RNA polymerase II
CC       holoenzyme; this interaction stimulates transcription activation
CC       in a CREB-dependent manner. Interacts (via RGG region) with SMN1;
CC       this interaction links SMN1 to the RNA polymerase II holoenzyme
CC       (ref.8). Interacts with SP7. Interacts (via DRBM domains) with
CC       TARBP2 (via DRBM first and second domains); this interaction
CC       occurs in a small interfering (siRNA)-dependent manner. Interacts
CC       with TOP2A; this interaction occurs in a E2 enzyme UBE2I- and RNA-
CC       dependent manner, negatively regulates DHX9-mediated double-
CC       stranded DNA and RNA duplex helicase activity and stimulates
CC       TOP2A-mediated supercoiled DNA relaxation activity. Interacts (via
CC       DRBM domains and C-terminus) with WRN (via 3'-5' exonuclease
CC       domain); this interaction inhibits the DNA-dependent NTPase and
CC       DNA helicase activities of DHX9 and stimulates the 3'-5'
CC       exonuclease activity of WRN. Interacts with XRCC5; this
CC       interaction occurs in a RNA-dependent manner. Interacts with ZIC2
CC       (via C2H2-type domain 3). Interacts with MCM3AP (By similarity).
CC       {ECO:0000250|UniProtKB:Q08211}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08211}.
CC       Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q08211}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:Q08211}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q08211}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:Q08211}. Note=Nucleoplasmic shuttling
CC       protein. Its nuclear import involves the nucleocytoplasmic
CC       transport receptor Importin alpha/Importin beta receptor pathway
CC       in a Ran-dependent manner. In interphase, localizes in nuclear
CC       stress granules and at perichromatin fibrils and in cytoplasmic
CC       ribonucleoprotein granules. Colocalizes with WRN and H2AFX at
CC       centrosomes in a microtubule-dependent manner following DNA
CC       damaging agent treatment. Excluded from the mitotic nucleus as
CC       early as prophase and re-entered the nucleus at telophase.
CC       Recruited in diffuse and discrete intranuclear foci (GLFG-body) in
CC       a NUP98-dependent manner. Colocalizes with SP7 in the nucleus.
CC       Colocalizes with ACTB at nuclear actin filaments inside the
CC       nucleus or at the nuclear pore. Colocalizes with HNRNPC at nuclear
CC       ribonucleoprotein complex proteins in the nucleus. Localized in
CC       cytoplasmic mRNP granules containing untranslated mRNAs.
CC       {ECO:0000250|UniProtKB:Q08211}.
CC   -!- DOMAIN: DRBM domains cooperate for the binding to nucleic acid but
CC       not for unwinding helicase activity. The helicase-associated
CC       domain-2 (HA2) region is essential for the duplex RNA unwinding
CC       helicase activity. The minimal transactivation region (MTAD)
CC       mediates interaction with the RNA polymerase II holoenzyme and
CC       stimulates transcriptional activation in a CREB-dependent manner.
CC       The oligonucleotide- or oligosaccharide-binding (OB-fold) and the
CC       repeated arginine and glycine-glycine (RGG) regions are
CC       dispensable for both RNA-binding and unwinding helicase
CC       activities. The RGG region contains both nuclear localization
CC       signal (NLS) and nuclear export signal (NES) and is necessary and
CC       sufficient for nucleocytoplasmic shuttling in a RNA-independent
CC       manner. {ECO:0000250|UniProtKB:Q08211}.
CC   -!- PTM: Methylated. PRMT1-mediated methylation of undefined Arg
CC       residues in the nuclear transport domain (NTD) is required for
CC       nuclear import of DHX9. {ECO:0000250|UniProtKB:Q08211}.
CC   -!- PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-
CC       dependent manner. Phosphorylated by EIF2AK2/PKR; this
CC       phosphorylation reduces its association with double-stranded RNA.
CC       {ECO:0000250|UniProtKB:Q08211}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000305}.
DR   EMBL; X82829; CAA58036.1; -; mRNA.
DR   PIR; I46032; I46032.
DR   RefSeq; NP_776461.1; NM_174036.2.
DR   SMR; Q28141; -.
DR   BioGrid; 158477; 1.
DR   IntAct; Q28141; 2.
DR   STRING; 9913.ENSBTAP00000026409; -.
DR   PaxDb; Q28141; -.
DR   PeptideAtlas; Q28141; -.
DR   PRIDE; Q28141; -.
DR   Ensembl; ENSBTAT00000026409; ENSBTAP00000026409; ENSBTAG00000019821.
DR   GeneID; 281115; -.
DR   KEGG; bta:281115; -.
DR   CTD; 1660; -.
DR   VGNC; VGNC:28060; DHX9.
DR   eggNOG; KOG0920; Eukaryota.
DR   eggNOG; COG1643; LUCA.
DR   GeneTree; ENSGT00940000155924; -.
DR   HOGENOM; HOG000247063; -.
DR   InParanoid; Q28141; -.
DR   KO; K13184; -.
DR   OrthoDB; 278674at2759; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   ExpressionAtlas; Q28141; baseline.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR   GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005726; C:perichromatin fibrils; ISS:UniProtKB.
DR   GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR   GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0016442; C:RISC complex; ISS:UniProtKB.
DR   GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:UniProtKB.
DR   GO; GO:0033679; F:3'-5' DNA/RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0034458; F:3'-5' RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0003688; F:DNA replication origin binding; ISS:UniProtKB.
DR   GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0061676; F:importin-alpha family protein binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISS:UniProtKB.
DR   GO; GO:1905538; F:polysome binding; ISS:UniProtKB.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0001069; F:regulatory region RNA binding; IEA:Ensembl.
DR   GO; GO:1905172; F:RISC complex binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR   GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0001085; F:RNA polymerase II transcription factor binding; IEA:Ensembl.
DR   GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
DR   GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
DR   GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0035197; F:siRNA binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0045142; F:triplex DNA binding; ISS:UniProtKB.
DR   GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR   GO; GO:0070934; P:CRD-mediated mRNA stabilization; IEA:Ensembl.
DR   GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR   GO; GO:0039695; P:DNA-templated viral transcription; IEA:Ensembl.
DR   GO; GO:0044806; P:G-quadruplex DNA unwinding; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
DR   GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR   GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR   GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; ISS:UniProtKB.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR   GO; GO:2000637; P:positive regulation of gene silencing by miRNA; ISS:UniProtKB.
DR   GO; GO:1902741; P:positive regulation of interferon-alpha secretion; ISS:UniProtKB.
DR   GO; GO:0035549; P:positive regulation of interferon-beta secretion; ISS:UniProtKB.
DR   GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISS:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:1905698; P:positive regulation of polysome binding; ISS:UniProtKB.
DR   GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISS:UniProtKB.
DR   GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; ISS:UniProtKB.
DR   GO; GO:0050434; P:positive regulation of viral transcription; IEA:Ensembl.
DR   GO; GO:1904973; P:positive regulation of viral translation; IEA:Ensembl.
DR   GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IEA:Ensembl.
DR   GO; GO:2000765; P:regulation of cytoplasmic translation; ISS:UniProtKB.
DR   GO; GO:0050684; P:regulation of mRNA processing; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; ISS:UniProtKB.
DR   GO; GO:0070922; P:small RNA loading onto RISC; ISS:UniProtKB.
DR   GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; ISS:UniProtKB.
DR   CDD; cd00048; DSRM; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00035; dsrm; 2.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00358; DSRM; 2.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; ATP-binding; Biological rhythms;
KW   Complete proteome; Cytoplasm; Cytoskeleton; DNA replication;
KW   DNA-binding; Helicase; Hydrolase; Immunity; Inflammatory response;
KW   Innate immunity; Isopeptide bond; Manganese; Metal-binding;
KW   Methylation; mRNA processing; mRNA splicing; mRNA transport;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; RNA-binding; RNA-mediated gene silencing; Transcription;
KW   Transcription regulation; Transcription termination;
KW   Translation regulation; Transport; Ubl conjugation.
FT   CHAIN         1   1287       ATP-dependent RNA helicase A.
FT                                /FTId=PRO_0000055156.
FT   DOMAIN        3     71       DRBM 1. {ECO:0000250|UniProtKB:Q08211,
FT                                ECO:0000255|PROSITE-ProRule:PRU00266}.
FT   DOMAIN      177    249       DRBM 2. {ECO:0000250|UniProtKB:Q08211,
FT                                ECO:0000255|PROSITE-ProRule:PRU00266}.
FT   DOMAIN      395    561       Helicase ATP-binding.
FT                                {ECO:0000250|UniProtKB:Q08211,
FT                                ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      633    806       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     408    416       ATP. {ECO:0000250|UniProtKB:Q08211,
FT                                ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   REGION        1    247       Interaction with CREBBP.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION        5      9       siRNA-binding.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION       53     55       siRNA-binding.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      179    183       siRNA-binding.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      227    322       Interaction with BRCA1.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      231    233       siRNA-binding.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      252    661       Necessary for interaction with RNA
FT                                polymerase II holoenzyme.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      310    949       Necessary for interaction with H2AFX.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      328    377       MTAD. {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      395    806       Core helicase.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      828    916       HA2. {ECO:0000250|UniProtKB:Q08211}.
FT   REGION      955   1071       OB-fold. {ECO:0000250|UniProtKB:Q08211}.
FT   REGION     1147   1276       NTD region.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   REGION     1148   1287       RGG. {ECO:0000250|UniProtKB:Q08211}.
FT   MOTIF       508    511       DEIH box.
FT   MOTIF       583    592       Nuclear localization signal (NLS1).
FT                                {ECO:0000255}.
FT   MOTIF      1152   1170       Nuclear localization signal (NLS2).
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   METAL       415    415       Manganese.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   METAL       509    509       Manganese.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     125    125       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     143    143       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:O70133}.
FT   MOD_RES     143    143       N6-methyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     188    188       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     196    196       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     318    318       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     446    446       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES     503    503       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES    1021   1021       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES    1163   1163       Asymmetric dimethylarginine.
FT                                {ECO:0000250|UniProtKB:O70133}.
FT   MOD_RES    1172   1172       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q08211}.
FT   MOD_RES    1235   1235       Asymmetric dimethylarginine.
FT                                {ECO:0000250|UniProtKB:O70133}.
FT   MOD_RES    1251   1251       Asymmetric dimethylarginine.
FT                                {ECO:0000250|UniProtKB:O70133}.
FT   MOD_RES    1259   1259       Asymmetric dimethylarginine.
FT                                {ECO:0000250|UniProtKB:O70133}.
FT   MOD_RES    1266   1266       Asymmetric dimethylarginine.
FT                                {ECO:0000250|UniProtKB:O70133}.
FT   MOD_RES    1282   1282       Asymmetric dimethylarginine.
FT                                {ECO:0000250|UniProtKB:O70133}.
FT   CROSSLNK    694    694       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q08211}.
SQ   SEQUENCE   1287 AA;  141944 MW;  DC908095AB683ED4 CRC64;
     MGDVKNFLYA WCGKRKMTPS YEIRAVGNKN RQKFMCEVRV EGYNYTGMGN STNKKDAQSN
     AARDFVNYLV RINELKSEEV PAVGVAPPTP SATDSSDTTA EDGGVPGNLG GPLPPHLTLQ
     AENNSGGGGS GYVPTWDRGA NLKDYYSRKE EQEVQATLES EEVDLNAGLH GNWTLENAKA
     RLNQYFQKEK IQGEYKYTQV GPDHNRSFIA EMTIYIKQIG RRIFAREHGS NKKLAAQSCA
     LSLVRQLYHL GVIEPYSGLT KKKEGETVEP YKVNLSQDLE HQLQNIVQEL NLEIVPIPED
     PSVPVALNLG KLAQFEPSQR QNPVGVVPWS PPQSNWNPWT SSNIDEGPLA YATPEQISMD
     LKNELMYQLE QDRDLQAVLQ ERELLPVKKF ESEILEAISQ NPVVIIRGAT GCGKTTQVPQ
     FILDDCIQND RAAECNIVVT QPRRISAVSV AERVAYERGE EPGKSCGYSV RFESILPRPH
     ASIMFCTVGV LLRKLEAGIR GISHVIVDEI HERDINTDFL LVVLRDVVQA YPEVRIVLMS
     ATIDTSMFCE YFFNCPIIEV YGRTFPVQEY FLEDCIQMTH FVPPPKDKKK KDKDDDGGED
     DDANCNLICG DEYGAETRIS MAQLNEKETP FELIEALLLY IETLNVPGAV LVFLPGWNLI
     YTMQKHLEMN PHFGSHRYQI LPLHSQIPRE EQRKVFDPVP SGVTKIILST NIAETSITIN
     DVVYVIDSCK QKVKLFTAHN NMTNYATVWA SKTNLEQRKG RAGRVRPGFC FHLCSRARFE
     RLETHMTPEM FRTPLHEIAL SIKLLRLGGI GQFLAKAIEP PPLDAVIEAE HTLRELDALD
     ANDELTPLGR ILAKLPIEPR FGKMMIMGCI FYVGDAICTI SAATCFPEPF ISEGKRLGYI
     HRNFAGNRFS DHVALLSVFQ AWDDARMGGE EAEIRFCEHK RLNMATLRMT WEAKVQLKEI
     LINSGFPEEC LLTQVFTNTG PDNNLDVVIS LLAFGVYPNV CYHKEKRKIL TTEGRNALIH
     KSSVNCPFSS QDMKYPSPFF VFGEKIRTRA ISAKGMTLVT PLQLLLFASK KVQSDGQLVL
     VDDWIRLQIS HEAAACITAL RAAMEALVVE VTKQPGIISQ LDPVNERMLN TIRQISRPSA
     AGINLMIGTT RYGDGPRPPK MARYDNGSGY RRGGSSYSGG GYGLGGYGTG GYGGGGGYGG
     RGGYSGGGYG GGSNSFRGSY VGGGGGVGGG GGGFRGLSRG GYRGMSGGDY RGESGGGYRG
     SGGFQRGGGR GGYGGGYFGQ GRGGGGY
//
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