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. DRADA family members contain at least one double-stranded RNA binding motifs (DSRM); vertebrate proteins contain three. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889925673  667 KNPISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGGRQFPAVIAKAKKDGKREAADVALRTLISE 737
Cdd:cd19902      1 KNPVSALMEYAQSRGVTAEIEVLSQSGPPHNPRFKAAVFVGGRRFPSVEASSKKDAKQEAADLALRALIAE 71

Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA- editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889925673     1 MAELQGRVLDLFAAQATRPRRTTEVAGNLGITKKEASTALYALQRQGAVERVQQSPPTWRL 61
Cdd:smart00550    4 QDSLEEKILEFLENSGDETSTALQLAKNLGLPKKEVNRVLYSLEKKGKVCKQGGTPPLWKL 64

Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA- editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1889925673   211 IANHLGLaSRKQVNPTLYAMQKRGLLVKVSETPPRW 246
Cdd:smart00550   28 LAKNLGL-PKKEVNRVLYSLEKKGKVCKQGGTPPLW 62

Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate adenosine to form inosine. In long double-stranded RNA, this process is non-specific; it occurs site-specifically in RNA transcripts. The former is important in defence against viruses, whereas the latter may affect splicing or untranslated regions. They are primarily nuclear proteins, but a longer isoform of ADAR1 is found predominantly in the cytoplasm. ADARs are derived from the Tad1-like tRNA deaminases that are present across eukaryotes. These in turn belong to the nucleotide/nucleic acid deaminase superfamily and are characterized by a distinct insert between the two conserved cysteines that are involved in binding zinc.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889925673  810 SIGTGNRCITGEHLSLEGQTVNDSHAEIIARRGLLrylyqqllTY-YD--------DPENSIFQECDEDSKqhFKLKPDV 880
Cdd:pfam02137    1 ALGTGTKCIGGSKLSPSGRVLNDSHAEVIARRSLL--------RYlYSqlllalsgNPSKSIFEPNPDSGK--LRLKPGI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889925673  881 TFHLYISTAPCGDGALFSLHDTEQvseveeplemsDNIQHTPIFSDPGKqglLRTKMEQGEGTIPIDPDTPiQTWDGVLR 960
Cdd:pfam02137   71 SFHLYISQTPCGDARIFSPLELEP-----------ESSPAHPVRRFRGQ---LRLKVETGAKTIPVESSED-QTWDGVKP 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889925673  961 GERLRTMSCSDKIARWNVVGLQGALLSHFLEPVYLSSVTLGM-MYIHGHLTRAVCCRWARgdveIQSLLPPNYKLNHPQV 1039
Cdd:pfam02137  136 GRRTLSMSCSDKLARWNVLGVQGALLSHFIEPIYLSSITVGGsLYDTEHLERAIYQRLDG----VLDSLPPPYRVNKPLI 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889925673 1040 GRVmtfsppretektkplsinwclgqdiaevidstkgkcverygchpVSKVSKSSLYVLFRTLCSKMNRDDLLTAKTYHQ 1119
Cdd:pfam02137  212 GQV--------------------------------------------ASRLCKAALFSRFLKLLSELSREDLLAPLTYHE 247

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1889925673 1120 AKLMAKEFQKAKAALFEVCEKNGYGKWMQKP 1150
Cdd:pfam02137  248 AKAAAKDYQEAKQQLKSLLRQQGLGSWIRKP 278

Double-stranded RNA binding motif;

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889925673   669 PISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGGRQFPAVIAKAKKDGKREAADVALRTL 734
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSL 66

dsRNA-specific ribonuclease [Transcription];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889925673  640 QGGDAATTPVERQAAPVLNNETFAALNKNPISALMEYAQSRHvKASI--EVIAETGPPHNPRFTMAAVVGGRQFPAVIAK 717
Cdd:COG0571    130 GGLEAARKFVLRLFEPRLEEIAPGGAGKDYKTALQEWLQARG-LPLPeyEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGR 208

                           90
                   ....*....|....*..
gi 1889925673  718 AKKDGKREAADVALRTL 734
Cdd:COG0571    209 SKKEAEQAAAKAALEKL 225

Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known as Zab.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889925673     1 MAELQGRVLDLFAAQATRPRRTTEVAGNLGITKKEASTALYALQRQGAVERVQQSPPTWRL 61
Cdd:smart00550    4 QDSLEEKILEFLENSGDETSTALQLAKNLGLPKKEVNRVLYSLEKKGKVCKQGGTPPLWKL 64

Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known as Zab.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889925673   398 SLEDRLLAALSRADSP-INSNDLAKMVGFrTKKEINPTLFAMQRKGLVKKVNDVPPLWQVVEAA 460
Cdd:smart00550    6 SLEEKILEFLENSGDEtSTALQLAKNLGL-PKKEVNRVLYSLEKKGKVCKQGGTPPLWKLTDKA 68

Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA- editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889925673  398 SLEDRLLAALSRADSPINSNDLAKMVGFRT-KKEINPTLFAMQRKGLVKKVNDVPPLWQVVEA 459
Cdd:pfam02295    4 ECAEKILELLENLGEGKAATAIALERGLSTpKREINRVLYDLERKGDVYREDGTPPRWFLTCA 66

Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA- editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1889925673  195 IISFLVQFQEPKDPTEIANHLGLAS-RKQVNPTLYAMQKRGLLVKVSETPPRWGLVP 250
Cdd:pfam02295    9 ILELLENLGEGKAATAIALERGLSTpKREINRVLYDLERKGDVYREDGTPPRWFLTC 65

seadornavirus double-stranded RNA-binding protein; This protein family occurs in the seadornavirus virus group, with an N-terminal domain for binding double-stranded RNA, is designated VP12 in Banna virus, VP8 in Kadipiro virus, and VP11 in Liao ning virus.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889925673  668 NPISALMEYAQSRHVKA-SIEVIAETGPPHNPRFTMAAVVGGRQFPAvIAKAKKDGKREAADVALRTLISEGHLQLP 743
Cdd:TIGR04238    1 NVVGMLQELAVKRGLELpVYEKVGKEGPDHAPTFTIKLTANDIEVIE-AASSKKQAEKLAAATIYEDMKENGLLEVH 76

Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate adenosine to form inosine. In long double-stranded RNA, this process is non-specific; it occurs site-specifically in RNA transcripts. The former is important in defence against viruses, whereas the latter may affect splicing or untranslated regions. They are primarily nuclear proteins, but a longer isoform of ADAR1 is found predominantly in the cytoplasm. ADARs are derived from the Tad1-like tRNA deaminases that are present across eukaryotes. These in turn belong to the nucleotide/nucleic acid deaminase superfamily and are characterized by a distinct insert between the two conserved cysteines that are involved in binding zinc.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889925673  810 SIGTGNRCITGEHLSLEGQTVNDSHAEIIARRGLLrylyqqllTY-YD--------DPENSIFQECDEDSKqhFKLKPDV 880
Cdd:pfam02137    1 ALGTGTKCIGGSKLSPSGRVLNDSHAEVIARRSLL--------RYlYSqlllalsgNPSKSIFEPNPDSGK--LRLKPGI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889925673  881 TFHLYISTAPCGDGALFSLHDTEQvseveeplemsDNIQHTPIFSDPGKqglLRTKMEQGEGTIPIDPDTPiQTWDGVLR 960
Cdd:pfam02137   71 SFHLYISQTPCGDARIFSPLELEP-----------ESSPAHPVRRFRGQ---LRLKVETGAKTIPVESSED-QTWDGVKP 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889925673  961 GERLRTMSCSDKIARWNVVGLQGALLSHFLEPVYLSSVTLGM-MYIHGHLTRAVCCRWARgdveIQSLLPPNYKLNHPQV 1039
Cdd:pfam02137  136 GRRTLSMSCSDKLARWNVLGVQGALLSHFIEPIYLSSITVGGsLYDTEHLERAIYQRLDG----VLDSLPPPYRVNKPLI 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889925673 1040 GRVmtfsppretektkplsinwclgqdiaevidstkgkcverygchpVSKVSKSSLYVLFRTLCSKMNRDDLLTAKTYHQ 1119
Cdd:pfam02137  212 GQV--------------------------------------------ASRLCKAALFSRFLKLLSELSREDLLAPLTYHE 247

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1889925673 1120 AKLMAKEFQKAKAALFEVCEKNGYGKWMQKP 1150
Cdd:pfam02137  248 AKAAAKDYQEAKQQLKSLLRQQGLGSWIRKP 278

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

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889925673  667 KNPISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGGRQFPAVIAKAKKDGKREAADVALRTLISE 737
Cdd:cd19915      1 TNPVSGLLEYARSKGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHNKKQGKQEAADAALRVLIGE 71

first double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA); 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 first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889925673  667 KNPISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGGRQFPAVIAKAKKDGKREAADVALRTLISE 737
Cdd:cd19913      1 KNPVSGLMEYAQFLGQTCEFLLLEQSGPSHDPRFKFQAVIDGRRFPPAEASSKKVAKKDAAAIALKILLRE 71

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        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889925673  667 KNPISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGGRQFPAVIAKAKKDGKREAADVALRTLISE 737
Cdd:cd19914      1 KNPISVLMEHSQKSGNMCEFQLLSQEGPPHDPKFTYCVKVGEQTFPSVVANSKKVAKQMAAEEAVKELMGE 71

double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) and similar proteins; ADAD1 (also known as testis nuclear RNA-binding protein (TENR)) is phylogenetically related to a family of adenosine deaminases involved in RNA editing. It 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. ADAD1 contains a double-stranded RNA binding motif (DSRM) and a C-terminal adenosine-deaminase (editase) domain. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889925673  667 KNPISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGGRQFPAVIAKAKKDGKREAADVALRTLI 735
Cdd:cd19905      1 KNPVSALHEYAQMTRLKLSFKETVTTGNVAGPYFAFCAVVDGIEYPTGVGKTKKEAKANAAKIALDELL 69

dsRNA-specific ribonuclease [Transcription];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889925673  640 QGGDAATTPVERQAAPVLNNETFAALNKNPISALMEYAQSRHvKASI--EVIAETGPPHNPRFTMAAVVGGRQFPAVIAK 717
Cdd:COG0571    130 GGLEAARKFVLRLFEPRLEEIAPGGAGKDYKTALQEWLQARG-LPLPeyEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGR 208

                           90
                   ....*....|....*..
gi 1889925673  718 AKKDGKREAADVALRTL 734
Cdd:COG0571    209 SKKEAEQAAAKAALEKL 225

double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known as Bax antagonist selected in saccharomyces 1 (BASS1), negative regulatory element-binding protein (NRE-binding protein), or protein DBP-5, or SON3) is an RNA-binding protein which acts as an mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. It specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Members of this group contain a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889925673  666 NKNPISALMEYAQSRHVKA-SIEVIAETGPPHNPRFTMAAVVGGRQF-PAVIAKAKKDGKREAADVALRTL 734
Cdd:cd19870      1 GKHPVSALMELCNKRKWGPpEFRLVEESGPPHRKHFLFKVVVNGVEYqPSVASGNKKDAKAQAATVALQAL 71

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        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889925673  667 KNPISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGGrqfpaVIAKA----KKDGKREAADVALRTLIS 736
Cdd:cd19862      1 KTPISVLQELCAKRGITPKYELISSEGAVHEPTFTFRVTVGD-----ITATGsgtsKKKAKHAAAENALEQLKG 69

Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known as Zab.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1889925673   527 LAKRENQKTTSLDLAKALGFqTKKDINPTLYALQNKGFVAKINDCPPCWTI 577
Cdd:smart00550   15 LENSGDETSTALQLAKNLGL-PKKEVNRVLYSLEKKGKVCKQGGTPPLWKL 64

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 1889925673  671 SALMEYAQsrhvKASIEV----IAETGPPHNPRFTMAAVVGGRQFPAVIAKAKKDGKREAADVALRTL 734
Cdd:cd19878      3 NLLQEYAQ----KKKIPLpkyeSAKSGPSHQPTFVSTVIVLGVRFSSEGAKNKKQAEQSAAKVALKEL 66

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        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889925673  667 KNPISALMEYAQSRHVKasieVIAETGPPHNPRFTMAAVVGGRQFPAvIAKAKKDGKREAADVALRTL 734
Cdd:cd19865      1 KNALMQLNELRPGLQYK----LTSQTGPVHAPVFTMSVEVNGQTFEG-TGRSKKKAKLEAAEKALRSF 63

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 1889925673  668 NPISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGGRQFPAVIAKAKKDGKREAADVALRTL 734
Cdd:cd20314      2 NYVSLLNEYCQKERLTVKYEEEKRSGPTHKPRFFCKYIIDGKEYPEGEGKSKKEAKQAAARLAYEEL 68

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889925673  667 KNPISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGgrQFPAV-IAKAKKDGKREAADVALRTL 734
Cdd:cd19883      1 KSEISQVFEIALKRNMPVNFEVTKETGPPHMKSFVTKVSVG--EFAGEgEGKSKKISKKNAAIAVLEEL 67

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889925673  669 PISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGgrQFPAV-IAKAKKDGKREAADVALRTL 734
Cdd:cd19859      1 EISLVHEIALKRNLTVNFEVLRESGPPHMKNFITRCTVG--SFVTEgEGNSKKVSKKRAAEKMLEEL 65

third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins; Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889925673  667 KNPISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGgrQFPAV-IAKAKKDGKREAADVALRTL 734
Cdd:cd19884      1 KSEISLVFEIALKRNMPVSFEVIKESGPPHMKSFVTRVTVG--EFTAEgEGNSKKLSKKRAATSVLQEL 67

Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA- editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1889925673   22 TTEVAGNLGIT--KKEASTALYALQRQGAVERVQQSPPTWRLLP 63
Cdd:pfam02295   22 ATAIALERGLStpKREINRVLYDLERKGDVYREDGTPPRWFLTC 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        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889925673  668 NPISALMEYAQSRHVKASIEVIAETGPPHNPRFTMAAVVGGRQFPAVIAKAKKDGKREAADVALRTLI 735
Cdd:cd19904      2 NYISLLNQYAQKKRLTVNYEQCASTGVPGPPRFSCKCKIGQKEYGIGTGSTKQEAKQAAAKEAYEQLL 69

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889925673  669 PISALMeyaQSRHVKASIE--VIAETGPPHNPRFTMAAVVGGRQFPAViAKAKKDGKREAADVALRTLI 735
Cdd:cd19895      5 PKNALM---QLNEIKPGLQykLLSQTGPVHAPVFVMSVEVNGQVFEGS-GPTKKKAKLHAAEKALRSFV 69

first double-stranded RNA binding motif of RNA-editing deaminase 2 (RED2) and similar proteins; RED2 (also known as 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 contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the first DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure. RED2 lacks editing activity for currently known substrate RNAs, and may have an inactive editase domain.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1889925673  688 VIAETGPPHNPRFTMAAVVGGRQFPAViAKAKKDGKREAADVALRTLI 735
Cdd:cd19896     23 MVSQTGPVHAPVFAVAVEVNGLTFEGT-GPTKKKAKMRAAEMALKSFV 69

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        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889925673  667 KNPISALMEYAQSrhvkASIEVIAETGPPHNPRFTMAAVVGGRQFPAViAKAKKDGKREAADVALRTL 734
Cdd:cd19898      3 KNPVMILNELRPG----LKYEFVSESGESHAKNFVMSVTVDGQTFEGS-GRNKKLAKARAAQAALAKL 65