ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. This enzyme cleaves double-stranded rRNA. It is involved in processing ribosomal RNA precursors. It is found even in minimal genones such as Mycoplasma genitalium and Buchnera aphidicola, and in some cases has been shown to be an essential gene. These bacterial proteins contain a double-stranded RNA binding motif (pfam00035) and a ribonuclease III domain (pfam00636). Eukaryotic homologs tend to be much longer proteins with additional domains, localized to the nucleus, and not included in this family. [Transcription, RNA processing]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445930775   24 LSKKIGIKFSKVEYYNTAFIHSSYKNENQEILEDNERLEFLGDSVLGLVAARSLFRKYPKANEGELSRIKSRIVSTPILN 103
Cdd:TIGR02191   1 LEKRLGYKFKNPELLEQALTHRSYANEHHKDVKNNERLEFLGDAVLGLVVAEYLFKNFPDASEGELSRLRAALVSEESLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445930775  104 SISEKLELSEYLLLGKGEKNSLGKGRRKLSANLFESLVGAIYLDQGFEIAEKFILRHLSEFVENPEKEESVRDYKTQLQE 183
Cdd:TIGR02191  81 EVARELGLGDFLLLGKGEEKSGGRRRDSILADAFEALIGAIYLDSGLEAARKFILKLLIPRIDAIIKEETLKDYKTALQE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 445930775  184 YSQKHFKILPIYRTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAKELYNRI 243
Cdd:TIGR02191 161 WAQARGKPLPEYRLIKEEGPDHDKEFTVEVSVNGEPYGEGKGKSKKEAEQNAAKAALEKL 220

Ribonuclease III family;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445930775    36 EYYNTAFIHSSYKNENqeilEDNERLEFLGDSVLGLVAARSLFRKYPKANEGELSRIKSRIVSTPILNSISEKLELSEYL 115
Cdd:smart00535   1 SLLLRALTHASYSNEH----EHNERLEFLGDAVLELVVTEYLYKKYPDLSEGDLSRLRSALVSNETLARLAKKLGLGEFI 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 445930775   116 LLGKGEKNSLGKGRRKLSANLFESLVGAIYLDQGFEIAEKFILRHL 161
Cdd:smart00535  77 RLGRGEAISGGRDKPKILADVFEALIGAIYLDSGLEAAREFIRDLL 122

ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. This enzyme cleaves double-stranded rRNA. It is involved in processing ribosomal RNA precursors. It is found even in minimal genones such as Mycoplasma genitalium and Buchnera aphidicola, and in some cases has been shown to be an essential gene. These bacterial proteins contain a double-stranded RNA binding motif (pfam00035) and a ribonuclease III domain (pfam00636). Eukaryotic homologs tend to be much longer proteins with additional domains, localized to the nucleus, and not included in this family. [Transcription, RNA processing]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445930775   24 LSKKIGIKFSKVEYYNTAFIHSSYKNENQEILEDNERLEFLGDSVLGLVAARSLFRKYPKANEGELSRIKSRIVSTPILN 103
Cdd:TIGR02191   1 LEKRLGYKFKNPELLEQALTHRSYANEHHKDVKNNERLEFLGDAVLGLVVAEYLFKNFPDASEGELSRLRAALVSEESLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445930775  104 SISEKLELSEYLLLGKGEKNSLGKGRRKLSANLFESLVGAIYLDQGFEIAEKFILRHLSEFVENPEKEESVRDYKTQLQE 183
Cdd:TIGR02191  81 EVARELGLGDFLLLGKGEEKSGGRRRDSILADAFEALIGAIYLDSGLEAARKFILKLLIPRIDAIIKEETLKDYKTALQE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 445930775  184 YSQKHFKILPIYRTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAKELYNRI 243
Cdd:TIGR02191 161 WAQARGKPLPEYRLIKEEGPDHDKEFTVEVSVNGEPYGEGKGKSKKEAEQNAAKAALEKL 220

Ribonuclease III family;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445930775    36 EYYNTAFIHSSYKNENqeilEDNERLEFLGDSVLGLVAARSLFRKYPKANEGELSRIKSRIVSTPILNSISEKLELSEYL 115
Cdd:smart00535   1 SLLLRALTHASYSNEH----EHNERLEFLGDAVLELVVTEYLYKKYPDLSEGDLSRLRSALVSNETLARLAKKLGLGEFI 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 445930775   116 LLGKGEKNSLGKGRRKLSANLFESLVGAIYLDQGFEIAEKFILRHL 161
Cdd:smart00535  77 RLGRGEAISGGRDKPKILADVFEALIGAIYLDSGLEAAREFIRDLL 122

double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase III (EC 3.1.26.3; also known as ribonuclease 3) digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. It is involved in the processing of rRNA precursors, viral transcripts, some mRNAs, and at least 1 tRNA (metY, a minor form of tRNA-init-Met). It cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs. The cleavage can occur in assembled 30S, 50S, and even 70S subunits and is influenced by the presence of ribosomal proteins. The RNase III family also includes the mitochondrion-specific ribosomal protein mL44 subfamily, which is composed of mitochondrial 54S ribosomal protein L3 (MRPL3) and mitochondrial 39S ribosomal protein L44 (MRPL44). Members of this family contain an RNase III domain and a C-terminal double-stranded RNA binding motif (DSRM). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445930775 175 RDYKTQLQEYSQKHFKILPIYRTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAKELYNRI 243
Cdd:cd10845    1 KDYKTALQEYLQKRGLPLPEYELVEEEGPDHNKTFTVEVKVNGKVIGEGTGRSKKEAEQAAAKAALEKL 69

Double-stranded RNA binding motif;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445930775   177 YKTQLQEYSQKHfKILPIYRTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAKELYN 241
Cdd:smart00358   1 PKSLLQELAQKR-KLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALR 64

double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 amino acid domain that adopts an alpha-beta-beta-beta-alpha fold. It is not sequence specific, but highly specific for double-stranded RNAs (dsRNAs) of various origin and structure. The DSRM domains are found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila Staufen protein, E. coli RNase III, RNase H1, and dsRNA dependent adenosine deaminases. They are involved in numerous cellular mechanisms ranging from localization and transport of messenger RNAs, through maturation and degradation of RNAs, to viral response and signal transduction. Some members harbor tandem DSRMs that act in small RNA biogenesis.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 445930775 182 QEYSQKHFKILPIYRTKSESGPdHAKTFQVVVRIRDQwEASGSGVSKKSAEQNAAKELY 240
Cdd:cd00048    1 NELCQKNKWPPPEYETVEEGGP-HNPRFTCTVTVNGQ-TFEGEGKSKKEAKQAAAEKAL 57

double-stranded RNA binding motif of metazoan ribonuclease III (RNase III) and similar proteins; RNase III (EC 3.1.26.3; also known as Drosha, or ribonuclease 3) is a double-stranded RNA (dsRNA)-specific endoribonuclease that is involved in the initial step of microRNA (miRNA) biogenesis. It is a component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, RNase III cleaves the 3' and 5' strands of a stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA-ssRNA junction) to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. It is also involved in pre-rRNA processing. Metazoan RNase III is a larger protein than bacterial RNase III. It contains two RNase III domains in the C-terminal half of the protein followed by a double-stranded RNA binding motif (DSRM). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445930775 176 DYKTQLQEY-------SQKHFKIlPIYRTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAKE 238
Cdd:cd19877    2 DPKSQLQQCcltlrteGKKEPDI-PEYKVLQKSGPTNTRVYTVAVYFRGERIATGTGSSIQQAEMNAAEK 70

double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; The family includes EIF2AK2 and adenosine deaminase domain-containing proteins, ADAD1 and ADAD2. EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. ADAD1 (also called testis nuclear RNA-binding protein (TENR)) and ADAD2 (also called testis nuclear RNA-binding protein-like (TENRL)) are phylogenetically related to a family of adenosine deaminases involved in RNA editing. ADAD1 plays an essential function in spermatid morphogenesis. It may be involved in testis-specific nuclear post-transcriptional processes such as heterogeneous nuclear RNA (hnRNA) packaging, alternative splicing, or nuclear/cytoplasmic transport of mRNAs. ADAD2 is a double-stranded RNA binding protein with unclear biological function. Members of this group contains varying numbers of double-stranded RNA binding motifs (DSRMs). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445930775 175 RDYKTQLQEYSQKHFKILPIyrTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAKELYNRI 243
Cdd:cd19875    1 KNPVSALNEYCQKRGLSLEF--VDVSVGPDHCPGFTASATIDGIVFASATGTSKKEAKRAAAKLALKKL 67

first double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 445930775 190 KILPIYRTKSESGPDHAKTFQVVVRIRDQ-WEASGSGVsKKSAEQNAAKEL 239
Cdd:cd19879   17 KIQPEYKLLSEQGPAHSKVFTVQLTLGDQhWEAEGTSI-KKAQHAAAAKAL 66

second double-stranded RNA binding motif of PRKRA, TARBP2 and similar proteins; The family includes protein activator of the interferon-induced protein kinase (PRKRA) and the RISC-loading complex subunit TARBP2. PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. TARBP2 (also called TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)) participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. The family also includes Drosophila melanogaster Loquacious and similar proteins. Loquacious (Loqs) is a double-stranded RNA-binding domain (dsRBD) protein, a homolog of human TAR RNA binding protein (TRBP) that is a protein first identified as binding the HIV trans-activator RNA (TAR). Loqs interacts with Dicer1 (dmDcr1) to facilitate miRNA processing. PRKRA family proteins contain three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445930775 180 QLQEYSQKHFKILPIYRTKSESGPDHAKTFQVVVRIRDQWEaSGSGVSKKSAEQNAAKELYNRI 243
Cdd:cd19863    5 ILQELCVQRRWRLPEYEVEQESGPPHEKEFTIACRVENFSE-TGSGKSKKLAKRAAAEKMLTRL 67

second double-stranded RNA binding motif of protein activator of the interferon-induced protein kinase (PRKRA) and similar proteins; PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. PRKRA contains three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 445930775 181 LQEYSQKHFKILPIYRTKSESGPDHAKTFQVVVRIrDQWEASGSGVSKKSAEQNAAKEL 239
Cdd:cd19891    6 LQELAVQKGWRLPEYTLAQESGPPHKREFTITCRV-ETFVETGTGTSKKVAKRNAAEKL 63

first double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3), as well as two RNA-editing deaminases, RED1 and RED2. STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. RED1 (EC 3.5.4.37; also called double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. RED2 (also called double-stranded RNA-specific editase B2, RNA-dependent adenosine deaminase 3, RNA-editing enzyme 2, dsRNA adenosine deaminase B2, ADAR3, or ADARB2) prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. It is capable of binding to dsRNA, but also to ssRNA. RED2 lacks editing activity for currently known substrate RNAs. Members of this group contain two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 445930775 194 IYRTKSESGPDHAKTFQVVVRIRDQwEASGSGVSKKSAEQNAA 236
Cdd:cd19865   15 QYKLTSQTGPVHAPVFTMSVEVNGQ-TFEGTGRSKKKAKLEAA 56

first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445930775 175 RDYKTQLQEYSQKHfKILPIYRTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAK 237
Cdd:cd19903    1 GNYMGKLNEYCQKQ-KVVLDYVEVPTSGPSHDPRFTFQVVIDGKEYPEGEGKSKKEAKQAAAK 62

second double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445930775 176 DYKTQLQEYSQKHfKILPIYRTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAKELYNRI 243
Cdd:cd19904    2 NYISLLNQYAQKK-RLTVNYEQCASTGVPGPPRFSCKCKIGQKEYGIGTGSTKQEAKQAAAKEAYEQL 68

second double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) and similar proteins; DRADA (EC 3.5.4.37; also known as 136 kDa double-stranded RNA-binding protein (p136), interferon-inducible protein 4 (IFI-4), K88DSRBP, ADAR1, G1P1, or ADAR) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. Vertebrate DRADA contains three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 445930775 179 TQLQEYSQKHFKILPiYRTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAKE 238
Cdd:cd19914    5 SVLMEHSQKSGNMCE-FQLLSQEGPPHDPKFTYCVKVGEQTFPSVVANSKKVAKQMAAEE 63

double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins; DUS2L (also known as dihydrouridine synthase 2 (DUS2), up-regulated in lung cancer protein 8 (URLC8), or tRNA-dihydrouridine synthase 2-like) catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. It negatively regulates the activation of EIF2AK2/PKR. DUS2L contains an N-terminal FMN-binding domain and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445930775 178 KTQLQEYSQKHFKILPIYRTKSESGpdhAKTFQVVVRIRDQ------WEAsgsgvSKKSAEQNAA 236
Cdd:cd19871    3 KMILNEWCRKNKLPQPVYETVQRPS---DRLFQSVVTVDGKkytsslWEK-----SKKLAEQAAA 59

double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445930775 176 DYKTQLQEYSQKhfKILPI-YRTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAKELYNRI 243
Cdd:cd20314    2 NYVSLLNEYCQK--ERLTVkYEEEKRSGPTHKPRFFCKYIIDGKEYPEGEGKSKKEAKQAAARLAYEEL 68

first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; DHX9 (EC 3.6.4.13; also known as ATP-dependent RNA helicase A, DExH-box helicase 9 (DDX9), Leukophysin (LKP), nuclear DNA helicase II (NDH II), NDH2, or RNA helicase A) is a multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation, and RNA-mediated gene silencing. It contains two double-stranded RNA binding motifs (DSRMs) at the N-terminal region. This model corresponds to the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 445930775 190 KILPIYRTKsESGPDHAKTFQVVVRIRD-QWEASGSGVSKKSAEQNAAKELYNRIRK 245
Cdd:cd19854   14 KLTPEYDIK-EAGNKHRQRFKCEVRVEGfDYVGTGNATNKKDAQTNAARDFLNYLVR 69