R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB proteins that can silence the IFNbeta promoter via binding to a negative regulatory element (NRE). Beside R3H NRF also contains a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462630161 603 KRDIEQIIRNYARSESHTDLTFSRELTNDERKQIHQIAQKYGLKSKSHGVGHDRYLVVGR 662
Cdd:cd02640     1 KNDYRQIIQNYAHSDDIRDMVFSPEFSKEERALIHQIAQKYGLKSRSYGSGNDRYLVISK 60

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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462630161 449 SNPVCTLNDTAQFNRMTVEYVYER---MTGLRWKCKVILESEVIAEAVG-VKKTVKYEAAGEAVKTL 511
Cdd:cd19875     1 KNPVSALNEYCQKRGLSLEFVDVSvgpDHCPGFTASATIDGIVFASATGtSKKEAKRAAAKLALKKL 67

R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB proteins that can silence the IFNbeta promoter via binding to a negative regulatory element (NRE). Beside R3H NRF also contains a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462630161 603 KRDIEQIIRNYARSESHTDLTFSRELTNDERKQIHQIAQKYGLKSKSHGVGHDRYLVVGR 662
Cdd:cd02640     1 KNDYRQIIQNYAHSDDIRDMVFSPEFSKEERALIHQIAQKYGLKSRSYGSGNDRYLVISK 60

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462630161 604 RDIEQIIRNYARSeSHTDLTFSReLTNDERKQIHQIAQKYGLKSKSHGVGHDRYLVV 660
Cdd:pfam01424   4 EQLAEKLAEFVKD-TGKSLELPP-MSSYERRIIHELAQKYGLESESEGEEPNRRVVV 58

glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462630161  549 IKEDNIGNQLLRKMGWTGGGLG-KSGEGIREPISVKEQHKREGLG 592
Cdd:smart00443   1 ISTSNIGAKLLRKMGWKEGQGLgKNEQGIVEPISAEIKKDRKGLG 45

G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462630161 552 DNIGNQLLRKMGWTGGGLG-KSGEGIREPISVKEQHKREGLGLD 594
Cdd:pfam01585   2 SNIGFKLLQKMGWKEGQGLgKNEQGIAEPIEAKIKKDRRGLGAE 45

R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB proteins that can silence the IFNbeta promoter via binding to a negative regulatory element (NRE). Beside R3H NRF also contains a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462630161 603 KRDIEQIIRNYARSESHTDLTFSRELTNDERKQIHQIAQKYGLKSKSHGVGHDRYLVVGR 662
Cdd:cd02640     1 KNDYRQIIQNYAHSDDIRDMVFSPEFSKEERALIHQIAQKYGLKSRSYGSGNDRYLVISK 60

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462630161 603 KRDIEQIIRNYARSESHTDLTFSReLTNDERKQIHQIAQKYGLKSKSHGVGHDRYLVVGR 662
Cdd:cd02325     1 REEREEELEAFAKDAAGKSLELPP-MNSYERKLIHDLAEYYGLKSESEGEGPNRRVVITK 59

R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may function as ATP-dependent DNA or RNA helicases. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2462630161 615 RSESHTDLTFSRELTNDERKQIHQIAQKYGLKSKSHGVGHDRYLVV 660
Cdd:cd06007    12 RASDNEEYEFPSSLTNHERAVIHRLCRKLGLKSKSKGKGSNRRLSV 57

Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General function prediction only];

                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462630161 632 ERKQIHQIAQKY-GLKSKSHGVGHDRYLVVGRKR 664
Cdd:COG1847   110 ERRIIHDALADDpGVETESEGEEPYRRVVISPKR 143

R3H domain found in proteins homologous to Bacillus subtilus Jag, which is associated with SpoIIIJ. SpoIIIJ is necessary for the third stage of sporulation. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462630161 596 ERVNKIAKRDIEQIIRnyarseSHTDLTFsRELTNDERKQIHQIAQKY-GLKSKSHGVGHDRYLVVGRK 663
Cdd:cd02644     6 ETLIRLAERAAEKVRR------TGKPVKL-EPMNAYERRIIHDALANDeDVETESEGEGPYRRVVISPK 67

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 2462630161 449 SNPVCTLNDTAQFNRMTVEYVYER---MTGLRWKCKVILESEVIAEAVG-VKKTVKYEAAGEAVKTL 511
Cdd:cd19875     1 KNPVSALNEYCQKRGLSLEFVDVSvgpDHCPGFTASATIDGIVFASATGtSKKEAKRAAAKLALKKL 67

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 2462630161 348 DAIGILNNSASFNKMSIEYkyEMMPN-----RTWRCRVFLQDHCLAEGYG-TKKTSKHAAADEALKIL 409
Cdd:cd19875     2 NPVSALNEYCQKRGLSLEF--VDVSVgpdhcPGFTASATIDGIVFASATGtSKKEAKRAAAKLALKKL 67

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
                  ....*....|....*....|....*....|....*
gi 2462630161 373 NRTWRCRVFLQDHcLAEGYG-TKKTSKHAAADEAL 406
Cdd:cd00048    24 NPRFTCTVTVNGQ-TFEGEGkSKKEAKQAAAEKAL 57