dsRNA-specific ribonuclease [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377725371   9 LKRDFDITFKDVDLLDAAFTHASYVNEtperKKKLKYYERIEFLGDAVMQLCVSEYIYEHYPEMPEGKMSRLRAAMVRAD 88
Cdd:COG0571     7 LEERLGYRFKDPELLEQALTHRSYANE----HGGLENNERLEFLGDAVLGLVVAEYLYRRFPDAPEGELSKLRAALVSEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377725371  89 SFSKFAIECHFNEYIRLGKGEEKGNARQRPSLLCDIFESFIGALYLDQGKDEVVRFISKVIFPKLE-LGWFDHMMDNKTE 167
Cdd:COG0571    83 TLAEIARELGLGDYLRLGKGEEKSGGRRRPSILADAFEALIGAIYLDGGLEAARKFVLRLFEPRLEeIAPGGAGKDYKTA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1377725371 168 LQEVLQQNGECKIKYNEVNVTGPDNERVYTMNVVVNNEVMGEGTGRTKKAAEQMAAYQALKKLRK 232
Cdd:COG0571   163 LQEWLQARGLPLPEYEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGRSKKEAEQAAAKAALEKLGK 227

dsRNA-specific ribonuclease [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377725371   9 LKRDFDITFKDVDLLDAAFTHASYVNEtperKKKLKYYERIEFLGDAVMQLCVSEYIYEHYPEMPEGKMSRLRAAMVRAD 88
Cdd:COG0571     7 LEERLGYRFKDPELLEQALTHRSYANE----HGGLENNERLEFLGDAVLGLVVAEYLYRRFPDAPEGELSKLRAALVSEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377725371  89 SFSKFAIECHFNEYIRLGKGEEKGNARQRPSLLCDIFESFIGALYLDQGKDEVVRFISKVIFPKLE-LGWFDHMMDNKTE 167
Cdd:COG0571    83 TLAEIARELGLGDYLRLGKGEEKSGGRRRPSILADAFEALIGAIYLDGGLEAARKFVLRLFEPRLEeIAPGGAGKDYKTA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1377725371 168 LQEVLQQNGECKIKYNEVNVTGPDNERVYTMNVVVNNEVMGEGTGRTKKAAEQMAAYQALKKLRK 232
Cdd:COG0571   163 LQEWLQARGLPLPEYEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGRSKKEAEQAAAKAALEKLGK 227

RIBOc. Ribonuclease III C terminal domain. This group consists of eukaryotic, bacterial and archeal ribonuclease III (RNAse III) proteins. RNAse III is a double stranded RNA-specific endonuclease. Prokaryotic RNAse III is important in post-transcriptional control of mRNA stability and translational efficiency. It is involved in the processing of ribosomal RNA precursors. Prokaryotic RNAse III also plays a role in the maturation of tRNA precursors and in the processing of phage and plasmid transcripts. Eukaryotic RNase III's participate (through direct cleavage) in rRNA processing, in processing of small nucleolar RNAs (snoRNAs) and snRNA's (components of the spliceosome). In eukaryotes RNase III or RNaseIII like enzymes such as Dicer are involved in RNAi (RNA interference) and miRNA (micro-RNA) gene silencing.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377725371  21 DLLDAAFTHASYVNEtperkKKLKYYERIEFLGDAVMQLCVSEYIYEHYPEMPEGKMSRLRAAMVRADSFSKFAIECHFN 100
Cdd:cd00593     1 SLLLEALTHPSYANE-----HGRFNNERLEFLGDAVLELVVTEYLFKKFPDLSEGDLTRLRSALVSNETLARLARELGLG 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1377725371 101 EYIRLGKGEEKGNARQRPSLLCDIFESFIGALYLDQGKDEVVRFISKVIFPKLE 154
Cdd:cd00593    76 KYLRLGKGEEKSGGRLRPKILADVFEALIGAIYLDGGFEAARKFLLRLLGPLIE 129

Ribonuclease-III-like; Members of this family are involved in rDNA transcription and rRNA processing. They probably also cleave a stem-loop structure at the 3' end of U2 snRNA to ensure formation of the correct U2 3' end; they are involved in polyadenylation-independent transcription termination. Some members may be mitochondrial ribosomal protein subunit L15, others may be 60S ribosomal protein L3.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377725371  21 DLLDAAFTHASYVNEtperkkKLKYYERIEFLGDAVMQLCVSEYIYEHyPEMPEGKMSRLRAAMVRADSFSKFAIECHFN 100
Cdd:pfam14622   2 ELLLQALTHKSYANG------RKPYNERLEFLGDAVLELSVSEYLFKK-PDLDEGGLTKLRASIVSEESLAEIAREIGLG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1377725371 101 EYIRLGKGEEKGNARQRPSLLCDIFESFIGALYLDQGKDEVVRFISKVIFPKL 153
Cdd:pfam14622  75 KYLRLGKGEEETGGSGRESILADALEALIGAIYLDGGFEVAKEFILKKILPDL 127

dsRNA-specific ribonuclease [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377725371   9 LKRDFDITFKDVDLLDAAFTHASYVNEtperKKKLKYYERIEFLGDAVMQLCVSEYIYEHYPEMPEGKMSRLRAAMVRAD 88
Cdd:COG0571     7 LEERLGYRFKDPELLEQALTHRSYANE----HGGLENNERLEFLGDAVLGLVVAEYLYRRFPDAPEGELSKLRAALVSEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377725371  89 SFSKFAIECHFNEYIRLGKGEEKGNARQRPSLLCDIFESFIGALYLDQGKDEVVRFISKVIFPKLE-LGWFDHMMDNKTE 167
Cdd:COG0571    83 TLAEIARELGLGDYLRLGKGEEKSGGRRRPSILADAFEALIGAIYLDGGLEAARKFVLRLFEPRLEeIAPGGAGKDYKTA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1377725371 168 LQEVLQQNGECKIKYNEVNVTGPDNERVYTMNVVVNNEVMGEGTGRTKKAAEQMAAYQALKKLRK 232
Cdd:COG0571   163 LQEWLQARGLPLPEYEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGRSKKEAEQAAAKAALEKLGK 227

RIBOc. Ribonuclease III C terminal domain. This group consists of eukaryotic, bacterial and archeal ribonuclease III (RNAse III) proteins. RNAse III is a double stranded RNA-specific endonuclease. Prokaryotic RNAse III is important in post-transcriptional control of mRNA stability and translational efficiency. It is involved in the processing of ribosomal RNA precursors. Prokaryotic RNAse III also plays a role in the maturation of tRNA precursors and in the processing of phage and plasmid transcripts. Eukaryotic RNase III's participate (through direct cleavage) in rRNA processing, in processing of small nucleolar RNAs (snoRNAs) and snRNA's (components of the spliceosome). In eukaryotes RNase III or RNaseIII like enzymes such as Dicer are involved in RNAi (RNA interference) and miRNA (micro-RNA) gene silencing.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377725371  21 DLLDAAFTHASYVNEtperkKKLKYYERIEFLGDAVMQLCVSEYIYEHYPEMPEGKMSRLRAAMVRADSFSKFAIECHFN 100
Cdd:cd00593     1 SLLLEALTHPSYANE-----HGRFNNERLEFLGDAVLELVVTEYLFKKFPDLSEGDLTRLRSALVSNETLARLARELGLG 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1377725371 101 EYIRLGKGEEKGNARQRPSLLCDIFESFIGALYLDQGKDEVVRFISKVIFPKLE 154
Cdd:cd00593    76 KYLRLGKGEEKSGGRLRPKILADVFEALIGAIYLDGGFEAARKFLLRLLGPLIE 129

Ribonuclease-III-like; Members of this family are involved in rDNA transcription and rRNA processing. They probably also cleave a stem-loop structure at the 3' end of U2 snRNA to ensure formation of the correct U2 3' end; they are involved in polyadenylation-independent transcription termination. Some members may be mitochondrial ribosomal protein subunit L15, others may be 60S ribosomal protein L3.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377725371  21 DLLDAAFTHASYVNEtperkkKLKYYERIEFLGDAVMQLCVSEYIYEHyPEMPEGKMSRLRAAMVRADSFSKFAIECHFN 100
Cdd:pfam14622   2 ELLLQALTHKSYANG------RKPYNERLEFLGDAVLELSVSEYLFKK-PDLDEGGLTKLRASIVSEESLAEIAREIGLG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1377725371 101 EYIRLGKGEEKGNARQRPSLLCDIFESFIGALYLDQGKDEVVRFISKVIFPKL 153
Cdd:pfam14622  75 KYLRLGKGEEETGGSGRESILADALEALIGAIYLDGGFEVAKEFILKKILPDL 127

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 1377725371 162 MDNKTELQEVLQQNGECKIKYNEVNVTGPDNERVYTMNVVVNNEVMGEGTGRTKKAAEQMAAYQALKKL 230
Cdd:cd10845     1 KDYKTALQEYLQKRGLPLPEYELVEEEGPDHNKTFTVEVKVNGKVIGEGTGRSKKEAEQAAAKAALEKL 69

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1377725371 165 KTELQEVLQQNGEcKIKYNEVNVTGPDNERVYTMNVVVNNEVMGEGTGRTKKAAEQMAAYQALKKL 230
Cdd:pfam00035   2 KSLLQEYAQKNGK-PPPYEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66

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 1377725371 167 ELQEVLQQNGEcKIKYNEVnVTGPDNERVYTMNVVVNNEVMGEGTGRTKKAAEQMAAYQALKKL 230
Cdd:cd19875     6 ALNEYCQKRGL-SLEFVDV-SVGPDHCPGFTASATIDGIVFASATGTSKKEAKRAAAKLALKKL 67

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 1377725371 163 DNKTELQEV---LQQNGECKI---KYNEVNVTGPDNERVYTMNVVVNNEVMGEGTGRTKKAAEQMAAYQALKKL 230
Cdd:cd19877     2 DPKSQLQQCcltLRTEGKKEPdipEYKVLQKSGPTNTRVYTVAVYFRGERIATGTGSSIQQAEMNAAEKALEKL 75

first double-stranded RNA binding motif of protein activator of the interferon-induced protein kinase (PRKRA) and similar proteins; This 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. This 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 first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1377725371 168 LQEVLQQNGeCKIKYNEVNVTGPDNERVYTMNVVVNnEVMGEGTGRTKKAAEQMAAYQALKKL 230
Cdd:cd19862     7 LQELCAKRG-ITPKYELISSEGAVHEPTFTFRVTVG-DITATGSGTSKKKAKHAAAENALEQL 67

second 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 second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1377725371 180 IKYNEVNVTGPDNERVYTMNVVVNNEVMgEGTGRTKKAAEQMAAYQALKKL 230
Cdd:cd19866    14 LKYKCLSESGESHAKSFVMSVTVDGQTF-EGTGRSKKLAKAAAAQAALAKL 63

second 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 second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1377725371 162 MDN-KTELQEVLQQNG-ECKIKYNEVnvtGPDNERVYT--MNVVV---NNEVMGEGTGRTKKAAEQMAAYQALKKL 230
Cdd:cd19855     1 LDNaKSRLNEFLQKNKiPAEYKYTSV---GPDHNRSFIaeLSIFVkqlGKTIYARETGSNKKLASQSCALSLVRQL 73

second double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins; RED1 (EC 3.5.4.37; also known as 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. It contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the second DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1377725371 180 IKYNEVNVTGPDNERVYTMNVVVNNEVMgEGTGRTKKAAEQMAAYQALKKL 230
Cdd:cd19898    16 LKYEFVSESGESHAKNFVMSVTVDGQTF-EGSGRNKKLAKARAAQAALAKL 65

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
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1377725371 174 QNGECKIKYNEVNVTGPDNERVYTMNVVVNNEVMGEGTGRTKKAAEQMAAYQALKKL 230
Cdd:cd19904    12 QKKRLTVNYEQCASTGVPGPPRFSCKCKIGQKEYGIGTGSTKQEAKQAAAKEAYEQL 68

double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRBs)and similar proteins; This family includes a group of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRB1-5). They bind double-stranded RNA (dsRNA) and may be involved in RNA-mediated silencing. Members of this family 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 1377725371 165 KTELQEVLQQNGECKIKYnEVNVTGPDNERVYTMNVVVNNEVMgEGTG-RTKKAAEQMAAYQALKKL 230
Cdd:cd19878     2 KNLLQEYAQKKKIPLPKY-ESAKSGPSHQPTFVSTVIVLGVRF-SSEGaKNKKQAEQSAAKVALKEL 66

first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins; Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. 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 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain 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
                  ....*....|....*....|....*....|....*....|....*....
gi 1377725371 179 KIKYNEVNVTGPDNERVYTMNVVVNNEVMGEGTGRTKKAAEQMAAYQAL 227
Cdd:cd19857    16 RPQYTLVDEEGPAHKKTFTVKLTLGDEEEYEASGSSIKKAQHAAAEKAL 64

second double-stranded RNA binding motif of STRBP, ILF3 and similar proteins; This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3). 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. Members of this STRBP/ILF3 group contain an N-terminal DZF domain and two 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 1377725371 180 IKYNEVNVTGPDNERVYTMNVVVNNEVMgEGTGRTKKAAEQMAAYQALKKL 230
Cdd:cd19897    14 LKYELISETGGSHDKRFVMEVEVDGQKF-QGAGSNKKVAKANAALAALEKL 63

second double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and similar proteins; DGCR8 is a component of the microprocessor complex that acts as an RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Within the microprocessor complex, DGCR8 functions as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11bp away from the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. DGCR8 contains two 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 1377725371 168 LQEVLQQN---GECKIKYNEVNVTgpDNERVYTMNVVvNNEVmgEGTGRTKKAAEQMAAYQALKKL 230
Cdd:cd19868     7 LQECLKRNhgmGDTELKFEVINDK--HQKHEYTMTVG-KHTV--TVICKNKKEGKQLAAQAILKKL 67