DHX36_BOVIN
ID DHX36_BOVIN Reviewed; 1010 AA.
AC Q05B79;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=ATP-dependent DNA/RNA helicase DHX36 {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9H2U1};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9H2U1};
DE AltName: Full=DEAD/H box polypeptide 36 {ECO:0000250|UniProtKB:Q9H2U1};
DE AltName: Full=DEAH-box protein 36 {ECO:0000305};
DE AltName: Full=G4-resolvase-1 {ECO:0000250|UniProtKB:Q9H2U1};
DE Short=G4R1 {ECO:0000250|UniProtKB:Q9H2U1};
DE AltName: Full=MLE-like protein 1 {ECO:0000250|UniProtKB:Q9H2U1};
DE AltName: Full=RNA helicase associated with AU-rich element protein {ECO:0000250|UniProtKB:Q9H2U1};
GN Name=DHX36 {ECO:0000250|UniProtKB:Q9H2U1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 56-1010 IN COMPLEXES WITH
RP MYC-PROMOTER G4-DNA-CONTAINING STRUCTURE; ATP AND MAGNESIUM ION, FUNCTION,
RP G4-DNA-BINDING, G4-RNA-BINDING, ATP-BINDING, MAGNESIUM-BINDING SITES,
RP REGION DSM MOTIF, REGION RECA-LIKE DOMAINS, REGION WH DOMAIN, REGION
RP OB-FOLD-LIKE SUBDOMAINS, AND MUTAGENESIS OF ARG-63; ILE-65; TYR-69; LYS-76;
RP ASN-77 AND LYS-78.
RX PubMed=29899445; DOI=10.1038/s41586-018-0209-9;
RA Chen M.C., Tippana R., Demeshkina N.A., Murat P., Balasubramanian S.,
RA Myong S., Ferre-D'Amare A.R.;
RT "Structural basis of G-quadruplex unfolding by the DEAH/RHA helicase
RT DHX36.";
RL Nature 558:465-469(2018).
CC -!- FUNCTION: Multifunctional ATP-dependent helicase that unwinds G-
CC quadruplex (G4) structures (PubMed:29899445). Plays a role in many
CC biological processes such as genomic integrity, gene expression
CC regulations and as a sensor to initiate antiviral responses (By
CC similarity). G4 structures correspond to helical structures containing
CC guanine tetrads (PubMed:29899445). Binds with high affinity to and
CC unwinds G4 structures that are formed in nucleic acids (G4-ADN and G4-
CC RNA) (PubMed:29899445) (By similarity). Plays a role in genomic
CC integrity. Converts the G4-RNA structure present in telomerase RNA
CC template component (TREC) into a double-stranded RNA to promote P1
CC helix formation that acts as a template boundary ensuring accurate
CC reverse transcription (By similarity). Plays a role in transcriptional
CC regulation. Resolves G4-DNA structures in promoters of genes, such as
CC YY1, KIT/c-kit and ALPL and positively regulates their expression (By
CC similarity). Plays a role in post-transcriptional regulation. Unwinds a
CC G4-RNA structure located in the 3'-UTR polyadenylation site of the pre-
CC mRNA TP53 and stimulates TP53 pre-mRNA 3'-end processing in response to
CC ultraviolet (UV)-induced DNA damage (By similarity). Binds to the
CC precursor-microRNA-134 (pre-miR-134) terminal loop and regulates its
CC transport into the synapto-dendritic compartment (By similarity).
CC Involved in the pre-miR-134-dependent inhibition of target gene
CC expression and the control of dendritic spine size (By similarity).
CC Plays a role in the regulation of cytoplasmic mRNA translation and mRNA
CC stability (By similarity). Binds to both G4-RNA structures and
CC alternative non-quadruplex-forming sequence within the 3'-UTR of the
CC PITX1 mRNA regulating negatively PITX1 protein expression (By
CC similarity). Binds to both G4-RNA structure in the 5'-UTR and AU-rich
CC elements (AREs) localized in the 3'-UTR of NKX2-5 mRNA to either
CC stimulate protein translation or induce mRNA decay in an ELAVL1-
CC dependent manner, respectively (By similarity). Binds also to ARE
CC sequences present in several mRNAs mediating exosome-mediated 3'-5'
CC mRNA degradation (By similarity). Involved in cytoplasmic urokinase-
CC type plasminogen activator (uPA) mRNA decay (By similarity). Component
CC of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of
CC viral double-stranded RNA (dsRNA) and plays a role in the activation of
CC a cascade of antiviral responses including the induction of pro-
CC inflammatory cytokines via the adapter molecule TICAM1 (By similarity).
CC Required for the early embryonic development and hematopoiesis.
CC Involved in the regulation of cardioblast differentiation and
CC proliferation during heart development. Involved in spermatogonia
CC differentiation. May play a role in ossification (By similarity).
CC {ECO:0000250|UniProtKB:D4A2Z8, ECO:0000250|UniProtKB:Q8VHK9,
CC ECO:0000250|UniProtKB:Q9H2U1, ECO:0000269|PubMed:29899445}.
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=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q9H2U1};
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:Q9H2U1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:29899445};
CC -!- ACTIVITY REGULATION: ATPase activity is enhanced in the presence of
CC homomeric poly(U) RNAs, but not by double-stranded DNA (dsDNA), double-
CC stranded RNA (dsRNA) and tRNA. {ECO:0000250|UniProtKB:Q9H2U1}.
CC -!- SUBUNIT: Found in a multi-helicase-TICAM1 complex at least composed of
CC DHX36, DDX1, DDX21 and TICAM1; this complex exists in resting cells
CC with or without dsRNA poly(I:C) ligand stimulation. Interacts (via C-
CC terminus) with TICAM1 (via TIR domain). Interacts (via C-terminus) with
CC DDX21; this interaction serves as bridges to TICAM1 (By similarity).
CC Interacts with TERT; this interaction is dependent on the ability of
CC DHX36 to bind to the G-quadruplex RNA (G4-RNA) structure present in the
CC telomerase RNA template component (TERC). Interacts with DKC1; this
CC interaction is dependent on the ability of DHX36 to bind to the G4-RNA
CC structure present in TERC. Interacts with PARN; this interaction
CC stimulates PARN to enhance uPA mRNA decay. Interacts with EXOSC3; this
CC interaction occurs in a RNase-insensitive manner. Interacts with
CC EXOSC10; this interaction occurs in a RNase-insensitive manner.
CC Interacts with ILF3; this interaction occurs in a RNA-dependent manner.
CC Interacts with ELAVL1; this interaction occurs in an RNA-dependent
CC manner. Interacts with DDX5; this interaction occurs in a RNA-dependent
CC manner. Interacts with DDX17; this interaction occurs in a RNA-
CC dependent manner. Interacts with HDAC1; this interaction occurs in a
CC RNA-dependent manner (By similarity). Interacts with HDAC3; this
CC interaction occurs in a RNA-dependent manner (By similarity). Interacts
CC with HDAC4 (By similarity). Interacts with AGO1. Interacts with AGO2
CC (By similarity). Interacts with ERCC6 (By similarity).
CC {ECO:0000250|UniProtKB:Q8VHK9, ECO:0000250|UniProtKB:Q9H2U1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8VHK9}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q9H2U1}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9H2U1}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q9H2U1}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q8VHK9}. Perikaryon
CC {ECO:0000250|UniProtKB:D4A2Z8}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:D4A2Z8}. Cell projection, axon
CC {ECO:0000250|UniProtKB:D4A2Z8}. Note=Predominantly localized in the
CC nucleus. Colocalizes with SRSF2 in nuclear speckles. Colocalizes with
CC DDX5 in nucleolar caps upon transcription inhibition. Accumulates and
CC colocalized with TIA1 in cytoplasmic stress granules (SGs) in an
CC arsenite-, heat shock- and RNA-binding-dependent manner. Shuttles into
CC and out of SGs in an ATPase-dependent manner (By similarity).
CC Colocalizes in the cytosol with the multi-helicase-TICAM1 complex that
CC translocates to the mitochondria upon poly(I:C) stimulation (By
CC similarity). {ECO:0000250|UniProtKB:Q8VHK9,
CC ECO:0000250|UniProtKB:Q9H2U1}.
CC -!- DOMAIN: The DHX36-specific motif (DSM) form folds into a DNA-binding-
CC induced alpha-helix that together with the oligonucleotide and
CC oligosaccharide-binding-fold-like (OB-fold-like) subdomain bind to Myc-
CC promoter G4-DNA-containing structure in an ATP-dependent manner. Upon
CC G4-DNA-binding, DHX36 pulls on DSM in the 3'-direction, inducing
CC rearrangement of the RecA-like 1 and 2 and the degenerate-winged-helix
CC (WH) regions; these rearrangements are probably responsible for the
CC ATP-independent repetitive G4-DNA unfolding activity, one residue at a
CC time. Upon resolving of G4-DNA into separate nucleotide strands, and
CC ATP hydrolysis, the apoprotein of DHX36 seems incompatible with G4-DNA-
CC binding (PubMed:29899445). The N-terminus is necessary for its
CC recruitment to cytoplasmic stress granules (SGs) upon arsenite-induced
CC treatment (By similarity). {ECO:0000250|UniProtKB:Q9H2U1,
CC ECO:0000269|PubMed:29899445}.
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DR EMBL; DAAA02002573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02002574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC122652; AAI22653.1; -; mRNA.
DR RefSeq; NP_001073720.1; NM_001080251.1.
DR PDB; 5VHA; X-ray; 2.23 A; A=150-1010.
DR PDB; 5VHC; X-ray; 2.49 A; D=150-1010.
DR PDB; 5VHD; X-ray; 2.55 A; D=150-1010.
DR PDB; 5VHE; X-ray; 3.79 A; A=56-1010.
DR PDBsum; 5VHA; -.
DR PDBsum; 5VHC; -.
DR PDBsum; 5VHD; -.
DR PDBsum; 5VHE; -.
DR AlphaFoldDB; Q05B79; -.
DR SMR; Q05B79; -.
DR STRING; 9913.ENSBTAP00000008082; -.
DR PaxDb; Q05B79; -.
DR PRIDE; Q05B79; -.
DR Ensembl; ENSBTAT00000008082; ENSBTAP00000008082; ENSBTAG00000006142.
DR GeneID; 509583; -.
DR KEGG; bta:509583; -.
DR CTD; 170506; -.
DR VEuPathDB; HostDB:ENSBTAG00000006142; -.
DR VGNC; VGNC:28054; DHX36.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000156903; -.
DR HOGENOM; CLU_001832_1_4_1; -.
DR InParanoid; Q05B79; -.
DR OMA; GKMILMS; -.
DR OrthoDB; 278674at2759; -.
DR TreeFam; TF324744; -.
DR Reactome; R-BTA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000006142; Expressed in spermatid and 107 other tissues.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB.
DR GO; GO:0002151; F:G-quadruplex RNA binding; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
DR GO; GO:0070883; F:pre-miRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0070034; F:telomerase RNA binding; ISS:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1903843; P:cellular response to arsenite ion; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISS:UniProtKB.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:1901534; P:positive regulation of hematopoietic progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IEA:Ensembl.
DR GO; GO:1904582; P:positive regulation of intracellular mRNA localization; ISS:UniProtKB.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; IEA:Ensembl.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
DR GO; GO:0010501; P:RNA secondary structure unwinding; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0090669; P:telomerase RNA stabilization; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Antiviral defense; ATP-binding;
KW Cell projection; Chromosome; Cytoplasm; Developmental protein;
KW Differentiation; DNA-binding; Helicase; Hydrolase; Immunity;
KW Innate immunity; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; RNA-binding; Telomere; Transcription; Transcription regulation;
KW Translation regulation; Transport.
FT CHAIN 1..1010
FT /note="ATP-dependent DNA/RNA helicase DHX36"
FT /id="PRO_0000445444"
FT DOMAIN 219..389
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 479..649
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..202
FT /note="Necessary for nuclear and nucleolar caps
FT localizations"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT REGION 1..107
FT /note="Required for the pre-miR-134 transport"
FT /evidence="ECO:0000250|UniProtKB:D4A2Z8"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..54
FT /note="Required for recruitment to cytoplasmic stress
FT granules"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT REGION 56..108
FT /note="Required for G4-DNA- and G4-RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT REGION 56..78
FT /note="DSM (DHX36-specific motif)"
FT /evidence="ECO:0000269|PubMed:29899445"
FT REGION 109..388
FT /note="RecA-like domain 1"
FT /evidence="ECO:0000269|PubMed:29899445"
FT REGION 267..319
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000269|PubMed:29899445"
FT REGION 389..630
FT /note="RecA-like domain 2"
FT /evidence="ECO:0000269|PubMed:29899445"
FT REGION 500..559
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000269|PubMed:29899445"
FT REGION 631..700
FT /note="WH domain"
FT /evidence="ECO:0000269|PubMed:29899445"
FT REGION 640..699
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000269|PubMed:29899445"
FT REGION 843..907
FT /note="OB-fold-like subdomains"
FT /evidence="ECO:0000269|PubMed:29899445"
FT REGION 851..862
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000269|PubMed:29899445"
FT REGION 872..902
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000269|PubMed:29899445"
FT MOTIF 336..339
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 519..530
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT BINDING 235..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29899445,
FT ECO:0007744|PDB:5VHC, ECO:0007744|PDB:5VHD"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:29899445,
FT ECO:0007744|PDB:5VHC"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:29899445,
FT ECO:0007744|PDB:5VHC"
FT BINDING 559
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29899445,
FT ECO:0007744|PDB:5VHD"
FT BINDING 604..607
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29899445,
FT ECO:0007744|PDB:5VHC, ECO:0007744|PDB:5VHD"
FT MOD_RES 949
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT MUTAGEN 63
FT /note="R->A: Decreases G4-DNA-binding; when associated with
FT A-65."
FT /evidence="ECO:0000269|PubMed:29899445"
FT MUTAGEN 65
FT /note="I->A: Decreases G4-DNA-binding; when associated with
FT A-63."
FT /evidence="ECO:0000269|PubMed:29899445"
FT MUTAGEN 69
FT /note="Y->A: Decreases strongly G4-DNA-binding."
FT /evidence="ECO:0000269|PubMed:29899445"
FT MUTAGEN 76
FT /note="K->G: Decreases G4-DNA-binding; when associated with
FT G-77 and G-78."
FT /evidence="ECO:0000269|PubMed:29899445"
FT MUTAGEN 77
FT /note="N->G: Decreases G4-DNA-binding; when associated with
FT G-76 and G-78."
FT /evidence="ECO:0000269|PubMed:29899445"
FT MUTAGEN 78
FT /note="K->G: Decreases G4-DNA-binding; when associated with
FT G-76 and G-77."
FT /evidence="ECO:0000269|PubMed:29899445"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 343..355
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 373..379
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 400..407
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 433..453
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 458..466
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 474..487
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 514..517
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 521..526
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:5VHC"
FT STRAND 547..552
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 565..570
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 572..580
FT /evidence="ECO:0007829|PDB:5VHA"
FT TURN 581..584
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 585..592
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 595..604
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 605..609
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 611..617
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 619..622
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 639..647
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 653..659
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 666..678
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 690..696
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 702..713
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 717..727
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 740..751
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 757..773
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 776..785
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 790..809
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 812..816
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 821..823
FT /evidence="ECO:0007829|PDB:5VHA"
FT TURN 825..828
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 830..841
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 845..849
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 852..855
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 860..862
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 864..866
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 868..871
FT /evidence="ECO:0007829|PDB:5VHD"
FT STRAND 875..879
FT /evidence="ECO:0007829|PDB:5VHC"
FT STRAND 884..890
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 895..898
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 904..906
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 909..915
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 919..923
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 925..932
FT /evidence="ECO:0007829|PDB:5VHA"
FT TURN 933..935
FT /evidence="ECO:0007829|PDB:5VHA"
FT STRAND 936..938
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 943..964
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 971..973
FT /evidence="ECO:0007829|PDB:5VHA"
FT HELIX 977..989
FT /evidence="ECO:0007829|PDB:5VHA"
SQ SEQUENCE 1010 AA; 114826 MW; 8205792C016B1018 CRC64;
MSYDYHQNWG RDGGPRSSGG GYGGSYGGSH GGGHGGNRGS GGGGGGGGGR GGRGRHPGHL
KGREIGLWYA KKQGQKNKEA ERQERAVVHM DERREEQIVQ LLHSVQTKND KDEEAQISWF
APEDHGYGTE APAENKPNSV KNVEHQEKKM INQEKRPFRI RDKYIDRDSE YLLQENEPDA
TLDQQLLEDL QKKKTDLRYI EMQRFREKLP SYGMQKELVN MIDNHQVTVI SGETGCGKTT
QVTQFILDNY IERGKGSACR IVCTQPRRIS AISVAERVAA ERAESCGNGN STGYQIRLQS
RLPRKQGSIL YCTTGIILQW LQSDPHLSSV SHIVLDEIHE RNLQSDVLMT VVKDLLSYRP
DLKVVLMSAT LNAEKFSEYF GNCPMIHIPG FTFPVVEYLL EDIIEKIRYV PEQKEHRSQF
KKGFMQGHVN RQEKEEKEAI YKERWPGYLR ELRQRYSAST VDVVEMMDDE KVDLNLIAAL
IRYIVLEEED GAILVFLPGW DNISTLHDLL MSQVMFKSDK FIIIPLHSLM PTVNQTQVFK
RTPPGVRKIV IATNIAETSI TIDDVVYVID GGKIKETHFD TQNNISTMSA EWVSKANAKQ
RKGRAGRVQP GHCYHLYNSL RASLLDDYQL PEILRTPLEE LCLQIKILRL GGIAHFLSRL
MDPPSNEAVL LSIKHLMELN ALDKQEELTP LGVHLARLPV EPHIGKMILF GALFCCLDPV
LTIAASLSFK DPFVIPLGKE KVADARRKEL AKDTKSDHLT VVNAFKGWEK AKQRGFRYEK
DYCWEYFLSS NTLQMLHNMK GQFAEHLLGA GFVSSRNPQD PESNINSDNE KIIKAVICAG
LYPKVAKIRL NLGKKRKMVK VYTKTDGVVA IHPKSVNVEQ TEFNYNWLIY HLKMRTSSIY
LYDCTEVSPY CLLFFGGDIS IQKDNDQETI AVDEWIIFQS PARIAHLVKE LRKELDILLQ
EKIESPHPVD WKDTKSRDCA VLSAIIDLIK TQEKATPRNL PPRFQDGYYS
