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Conserved domains on  [gi|1958752887|ref|XP_038959138|]
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double-stranded RNA-specific adenosine deaminase isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
754-1137 1.51e-178

tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);


:

Pssm-ID: 214718  Cd Length: 374  Bit Score: 527.72  E-value: 1.51e-178
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   754 TFHDQIAMLSHRCFNALTNSFQPSLLGRKILAAIIMKRDPEDMGVVVSLGTGNRCVKGDSLSLKGETVNDCHAEIISRRG 833
Cdd:smart00552    1 DTGDEISQLVLEKFGSLPKIGKPGLREWTILAGVVMTNGMDNEKQVVSLGTGTKCISGEKLSPNGLVLNDCHAEILARRG 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   834 FIRFLYSELMKYNHhTAKNSIFELARGGEKLQIKKTVSFHLYISTAPCGDGALFDKSCSDRAvestESRHYPVFENPKQG 913
Cdd:smart00552   81 FLRFLYSELQLFNS-SSEDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKN----DDSKHPVRKNIKRS 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   914 KLRTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFLQPVYLKSVTLG-YLFSQGHLT 992
Cdd:smart00552  156 KLRTKIEIGEGTVPVRSSDIVQTWDGIGDGERLLSMSCSDKIARWNVLGVQGALLSHFIEPIYLSSIVLGkSLYSAEHLE 235

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   993 RAICCRVTRDgnafeDGLRYPFIVNHPKVGRVSVYDSKRQSGKTKETSVNWCLADGYdLEILDGTRGTVDGPGKELSRVS 1072
Cdd:smart00552  236 RALYGRLDPL-----DGLPTPFRVNRPLISLVSVADFQRQTAKSPNFSVNWSQGDES-LEILNGLTGKTQKSLGSPSRLC 309

                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958752887  1073 KKNIFLQFKKLCSFRARRDLLQLSYGEAKKAARDYDLAKNYFKKSLRDMGYGNWISKPQEEKNFY 1137
Cdd:smart00552  310 KKALFRLFQKLCSKLKRDDLLHISYAEAKEAASEYQEAKQLLFEALNKAGLGSWIKKPPEQDQFK 374
DSRM_DRADA_rpt3 cd19915
third double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 640-710 8.86e-44

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.


:

Pssm-ID: 380744  Cd Length: 71  Bit Score: 152.79  E-value: 8.86e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  640 TNPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVLIGE 710
Cdd:cd19915      1 TNPVSGLLEYARSKGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHNKKQGKQEAADAALRVLIGE 71
DSRM_DRADA_rpt1 cd19913
first double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 421-491 1.04e-41

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.


:

Pssm-ID: 380742  Cd Length: 71  Bit Score: 146.94  E-value: 1.04e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  421 KNPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILLRE 491
Cdd:cd19913      1 KNPVSGLMEYAQFLGQTCEFLLLEQSGPSHDPRFKFQAVIDGRRFPPAEASSKKVAKKDAAAIALKILLRE 71
DSRM_SF super family cl00054
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 532-602 1.78e-38

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.


The actual alignment was detected with superfamily member cd19914:

Pssm-ID: 444671  Cd Length: 71  Bit Score: 137.67  E-value: 1.78e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  532 KSPVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALQEE 602
Cdd:cd19914      1 KNPISVLMEHSQKSGNMCEFQLLSQEGPPHDPKFTYCVKVGEQTFPSVVANSKKVAKQMAAEEAVKELMGE 71
z-alpha pfam02295
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 145-211 3.87e-29

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.


:

Pssm-ID: 280459  Cd Length: 67  Bit Score: 110.67  E-value: 3.87e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  145 ISQNPEQKVLNRLEELGEGKATTAYALARELRTPKKDINRILYSLERKGKLHRGVGKPPLWSLVPLS 211
Cdd:pfam02295    1 DAQECAEKILELLENLGEGKAATAIALERGLSTPKREINRVLYDLERKGDVYREDGTPPRWFLTCAK 67
z-alpha super family cl02659
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 253-317 6.39e-23

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.


The actual alignment was detected with superfamily member pfam02295:

Pssm-ID: 295419  Cd Length: 67  Bit Score: 92.95  E-value: 6.39e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  253 DMAEIKEKICDYLFNVS-KSSALNLAKNIGLAK-ARDVNAVLIDLERQGDVYREGATPPIWYLTDKK 317
Cdd:pfam02295    1 DAQECAEKILELLENLGeGKAATAIALERGLSTpKREINRVLYDLERKGDVYREDGTPPRWFLTCAK 67
 
Name Accession Description Interval E-value
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
754-1137 1.51e-178

tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);


Pssm-ID: 214718  Cd Length: 374  Bit Score: 527.72  E-value: 1.51e-178
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   754 TFHDQIAMLSHRCFNALTNSFQPSLLGRKILAAIIMKRDPEDMGVVVSLGTGNRCVKGDSLSLKGETVNDCHAEIISRRG 833
Cdd:smart00552    1 DTGDEISQLVLEKFGSLPKIGKPGLREWTILAGVVMTNGMDNEKQVVSLGTGTKCISGEKLSPNGLVLNDCHAEILARRG 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   834 FIRFLYSELMKYNHhTAKNSIFELARGGEKLQIKKTVSFHLYISTAPCGDGALFDKSCSDRAvestESRHYPVFENPKQG 913
Cdd:smart00552   81 FLRFLYSELQLFNS-SSEDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKN----DDSKHPVRKNIKRS 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   914 KLRTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFLQPVYLKSVTLG-YLFSQGHLT 992
Cdd:smart00552  156 KLRTKIEIGEGTVPVRSSDIVQTWDGIGDGERLLSMSCSDKIARWNVLGVQGALLSHFIEPIYLSSIVLGkSLYSAEHLE 235

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   993 RAICCRVTRDgnafeDGLRYPFIVNHPKVGRVSVYDSKRQSGKTKETSVNWCLADGYdLEILDGTRGTVDGPGKELSRVS 1072
Cdd:smart00552  236 RALYGRLDPL-----DGLPTPFRVNRPLISLVSVADFQRQTAKSPNFSVNWSQGDES-LEILNGLTGKTQKSLGSPSRLC 309

                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958752887  1073 KKNIFLQFKKLCSFRARRDLLQLSYGEAKKAARDYDLAKNYFKKSLRDMGYGNWISKPQEEKNFY 1137
Cdd:smart00552  310 KKALFRLFQKLCSKLKRDDLLHISYAEAKEAASEYQEAKQLLFEALNKAGLGSWIKKPPEQDQFK 374
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
 801-1130 9.22e-119

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.


Pssm-ID: 460458  Cd Length: 278  Bit Score: 367.66  E-value: 9.22e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  801 SLGTGNRCVKGDSLSLKGETVNDCHAEIISRRGFIRFLYSELMKYNHHTAKNSIFELARGGEKLQIKKTVSFHLYISTAP 880
Cdd:pfam02137    1 ALGTGTKCIGGSKLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNPSKSIFEPNPDSGKLRLKPGISFHLYISQTP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  881 CGDGALFDKSCSdravESTESRHYPVFENPkqGKLRTKVENGEGTIPVESSDIvPTWDGIRLGERLRTMSCSDKILRWNV 960
Cdd:pfam02137   81 CGDARIFSPLEL----EPESSPAHPVRRFR--GQLRLKVETGAKTIPVESSED-QTWDGVKPGRRTLSMSCSDKLARWNV 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  961 LGLQGALLTHFLQPVYLKSVTL-GYLFSQGHLTRAICCRVTRdgnaFEDGLRYPFIVNHPKVGRVSvydskrqsgktket 1039
Cdd:pfam02137  154 LGVQGALLSHFIEPIYLSSITVgGSLYDTEHLERAIYQRLDG----VLDSLPPPYRVNKPLIGQVA-------------- 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887 1040 svnwcladgydleildgtrgtvdgpgkelSRVSKKNIFLQFKKLCSFRARRDLLQ-LSYGEAKKAARDYDLAKNYFKKSL 1118
Cdd:pfam02137  216 -----------------------------SRLCKAALFSRFLKLLSELSREDLLApLTYHEAKAAAKDYQEAKQQLKSLL 266

                          330
                   ....*....|..
gi 1958752887 1119 RDMGYGNWISKP 1130
Cdd:pfam02137  267 RQQGLGSWIRKP 278
DSRM_DRADA_rpt3 cd19915
third double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 640-710 8.86e-44

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.


Pssm-ID: 380744  Cd Length: 71  Bit Score: 152.79  E-value: 8.86e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  640 TNPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVLIGE 710
Cdd:cd19915      1 TNPVSGLLEYARSKGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHNKKQGKQEAADAALRVLIGE 71
DSRM_DRADA_rpt1 cd19913
first double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 421-491 1.04e-41

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.


Pssm-ID: 380742  Cd Length: 71  Bit Score: 146.94  E-value: 1.04e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  421 KNPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILLRE 491
Cdd:cd19913      1 KNPVSGLMEYAQFLGQTCEFLLLEQSGPSHDPRFKFQAVIDGRRFPPAEASSKKVAKKDAAAIALKILLRE 71
DSRM_DRADA_rpt2 cd19914
second double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 532-602 1.78e-38

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.


Pssm-ID: 380743  Cd Length: 71  Bit Score: 137.67  E-value: 1.78e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  532 KSPVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALQEE 602
Cdd:cd19914      1 KNPISVLMEHSQKSGNMCEFQLLSQEGPPHDPKFTYCVKVGEQTFPSVVANSKKVAKQMAAEEAVKELMGE 71
z-alpha pfam02295
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 145-211 3.87e-29

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.


Pssm-ID: 280459  Cd Length: 67  Bit Score: 110.67  E-value: 3.87e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  145 ISQNPEQKVLNRLEELGEGKATTAYALARELRTPKKDINRILYSLERKGKLHRGVGKPPLWSLVPLS 211
Cdd:pfam02295    1 DAQECAEKILELLENLGEGKAATAIALERGLSTPKREINRVLYDLERKGDVYREDGTPPRWFLTCAK 67
z-alpha pfam02295
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 253-317 6.39e-23

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.


Pssm-ID: 280459  Cd Length: 67  Bit Score: 92.95  E-value: 6.39e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  253 DMAEIKEKICDYLFNVS-KSSALNLAKNIGLAK-ARDVNAVLIDLERQGDVYREGATPPIWYLTDKK 317
Cdd:pfam02295    1 DAQECAEKILELLENLGeGKAATAIALERGLSTpKREINRVLYDLERKGDVYREDGTPPRWFLTCAK 67
Zalpha smart00550
Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known ...
 251-317 1.99e-21

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


Pssm-ID: 128823  Cd Length: 68  Bit Score: 88.93  E-value: 1.99e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887   251 LLDMAEIKEKICDYLFNVS--KSSALNLAKNIGLAKaRDVNAVLIDLERQGDVYREGATPPIWYLTDKK 317
Cdd:smart00550    1 SLTQDSLEEKILEFLENSGdeTSTALQLAKNLGLPK-KEVNRVLYSLEKKGKVCKQGGTPPLWKLTDKA 68
DSRM smart00358
Double-stranded RNA binding motif;
423-488 5.41e-20

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 84.62  E-value: 5.41e-20
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887   423 PVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSL 66
DSRM smart00358
Double-stranded RNA binding motif;
534-600 1.01e-18

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 81.16  E-value: 1.01e-18
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887   534 PVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALQ 600
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSLK 67
Zalpha smart00550
Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known ...
 144-207 3.04e-18

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


Pssm-ID: 128823  Cd Length: 68  Bit Score: 79.69  E-value: 3.04e-18
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958752887   144 SISQNP-EQKVLNRLEELGEGkATTAYALARELRTPKKDINRILYSLERKGKLHRGVGKPPLWSL 207
Cdd:smart00550    1 SLTQDSlEEKILEFLENSGDE-TSTALQLAKNLGLPKKEVNRVLYSLEKKGKVCKQGGTPPLWKL 64
PHA03103 PHA03103
double-strand RNA-binding protein; Provisional
 253-489 1.28e-16

double-strand RNA-binding protein; Provisional


Pssm-ID: 222987 [Multi-domain]  Cd Length: 183  Bit Score: 79.03  E-value: 1.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  253 DMAEIKEKICDYLFNVSKS---SALNLAKNIGLAKaRDVNAVLIDLERQGDVYREGATPPIWYLTdkkrerlqmkrsths 329
Cdd:PHA03103     7 DEVDIYELVKKEVKNLGLGegiTAIEISRKLNIEK-SEVNKQLYKLQREGMVYMSDSNPPKWFKT--------------- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  330 gpaatpaavseaTQStsfptchppqsggsssmatskrvENGQEPVTKYESRHearpgpvrlrphayHNGPSRAGPTLPrc 409
Cdd:PHA03103    71 ------------TEA-----------------------DNDDNDDVSREKSM--------------REDNKSFSDTIP-- 99

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  410 spYKKLTECQLKNPVSGLLEYAQFTSQTCDFNlIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILL 489
Cdd:PHA03103   100 --YKKIISWKDKNPCTVINEYCQITSRDWSIN-ITSSGPSHSPTFTASVIISGIKFKPAIGSTKKEAKNNAAKLAMDKIL 176
DSRM smart00358
Double-stranded RNA binding motif;
642-707 2.47e-15

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 71.53  E-value: 2.47e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887   642 PVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 423-488 2.74e-14

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.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 68.41  E-value: 2.74e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  423 PVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 642-707 1.15e-10

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.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 58.40  E-value: 1.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  642 PVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 534-599 2.82e-10

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.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 57.24  E-value: 2.82e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  534 PVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKAL 599
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
421-488 2.46e-09

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 58.96  E-value: 2.46e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  421 KNPVSGLLEYAQFTSQTC-DFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:COG0571    157 KDYKTALQEWLQARGLPLpEYEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGRSKKEAEQAAAKAALEKL 225
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
531-602 7.99e-08

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 54.33  E-value: 7.99e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958752887  531 GKSPVTTLLECMHKLGNSC-EFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALQEE 602
Cdd:COG0571    156 GKDYKTALQEWLQARGLPLpEYEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGRSKKEAEQAAAKAALEKLGKK 228
RNaseIII TIGR02191
ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. ...
 633-704 1.15e-07

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]


Pssm-ID: 274024 [Multi-domain]  Cd Length: 220  Bit Score: 53.75  E-value: 1.15e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958752887  633 ELVRYLNTNPVGGLLEYARSHGFAA-EFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAAL 704
Cdd:TIGR02191  145 IIKEETLKDYKTALQEWAQARGKPLpEYRLIKEEGPDHDKEFTVEVSVNGEPYGEGKGKSKKEAEQNAAKAAL 217
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
646-707 6.60e-07

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 51.64  E-value: 6.60e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958752887  646 LLEYARSHGFAA-EFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:COG0571    163 LQEWLQARGLPLpEYEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGRSKKEAEQAAAKAALEKL 225
RNaseIII TIGR02191
ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. ...
 550-599 1.09e-06

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]


Pssm-ID: 274024 [Multi-domain]  Cd Length: 220  Bit Score: 50.67  E-value: 1.09e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958752887  550 EFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKAL 599
Cdd:TIGR02191  171 EYRLIKEEGPDHDKEFTVEVSVNGEPYGEGKGKSKKEAEQNAAKAALEKL 220
PHA02701 PHA02701
ORF020 dsRNA-binding PKR inhibitor; Provisional
 422-489 2.57e-05

ORF020 dsRNA-binding PKR inhibitor; Provisional


Pssm-ID: 177482 [Multi-domain]  Cd Length: 183  Bit Score: 46.09  E-value: 2.57e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  422 NPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILL 489
Cdd:PHA02701   109 NPVSAVNEFCMRTHRPLEFCETRSGGHDHCPLFTCTIVVSGKVVATASGCSKKLARHAACADALTILI 176
 
Name Accession Description Interval E-value
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
754-1137 1.51e-178

tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);


Pssm-ID: 214718  Cd Length: 374  Bit Score: 527.72  E-value: 1.51e-178
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   754 TFHDQIAMLSHRCFNALTNSFQPSLLGRKILAAIIMKRDPEDMGVVVSLGTGNRCVKGDSLSLKGETVNDCHAEIISRRG 833
Cdd:smart00552    1 DTGDEISQLVLEKFGSLPKIGKPGLREWTILAGVVMTNGMDNEKQVVSLGTGTKCISGEKLSPNGLVLNDCHAEILARRG 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   834 FIRFLYSELMKYNHhTAKNSIFELARGGEKLQIKKTVSFHLYISTAPCGDGALFDKSCSDRAvestESRHYPVFENPKQG 913
Cdd:smart00552   81 FLRFLYSELQLFNS-SSEDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKN----DDSKHPVRKNIKRS 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   914 KLRTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFLQPVYLKSVTLG-YLFSQGHLT 992
Cdd:smart00552  156 KLRTKIEIGEGTVPVRSSDIVQTWDGIGDGERLLSMSCSDKIARWNVLGVQGALLSHFIEPIYLSSIVLGkSLYSAEHLE 235

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887   993 RAICCRVTRDgnafeDGLRYPFIVNHPKVGRVSVYDSKRQSGKTKETSVNWCLADGYdLEILDGTRGTVDGPGKELSRVS 1072
Cdd:smart00552  236 RALYGRLDPL-----DGLPTPFRVNRPLISLVSVADFQRQTAKSPNFSVNWSQGDES-LEILNGLTGKTQKSLGSPSRLC 309

                           330       340       350       360       370       380
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958752887  1073 KKNIFLQFKKLCSFRARRDLLQLSYGEAKKAARDYDLAKNYFKKSLRDMGYGNWISKPQEEKNFY 1137
Cdd:smart00552  310 KKALFRLFQKLCSKLKRDDLLHISYAEAKEAASEYQEAKQLLFEALNKAGLGSWIKKPPEQDQFK 374
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
 801-1130 9.22e-119

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.


Pssm-ID: 460458  Cd Length: 278  Bit Score: 367.66  E-value: 9.22e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  801 SLGTGNRCVKGDSLSLKGETVNDCHAEIISRRGFIRFLYSELMKYNHHTAKNSIFELARGGEKLQIKKTVSFHLYISTAP 880
Cdd:pfam02137    1 ALGTGTKCIGGSKLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNPSKSIFEPNPDSGKLRLKPGISFHLYISQTP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  881 CGDGALFDKSCSdravESTESRHYPVFENPkqGKLRTKVENGEGTIPVESSDIvPTWDGIRLGERLRTMSCSDKILRWNV 960
Cdd:pfam02137   81 CGDARIFSPLEL----EPESSPAHPVRRFR--GQLRLKVETGAKTIPVESSED-QTWDGVKPGRRTLSMSCSDKLARWNV 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  961 LGLQGALLTHFLQPVYLKSVTL-GYLFSQGHLTRAICCRVTRdgnaFEDGLRYPFIVNHPKVGRVSvydskrqsgktket 1039
Cdd:pfam02137  154 LGVQGALLSHFIEPIYLSSITVgGSLYDTEHLERAIYQRLDG----VLDSLPPPYRVNKPLIGQVA-------------- 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887 1040 svnwcladgydleildgtrgtvdgpgkelSRVSKKNIFLQFKKLCSFRARRDLLQ-LSYGEAKKAARDYDLAKNYFKKSL 1118
Cdd:pfam02137  216 -----------------------------SRLCKAALFSRFLKLLSELSREDLLApLTYHEAKAAAKDYQEAKQQLKSLL 266

                          330
                   ....*....|..
gi 1958752887 1119 RDMGYGNWISKP 1130
Cdd:pfam02137  267 RQQGLGSWIRKP 278
DSRM_DRADA_rpt3 cd19915
third double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 640-710 8.86e-44

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.


Pssm-ID: 380744  Cd Length: 71  Bit Score: 152.79  E-value: 8.86e-44
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  640 TNPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVLIGE 710
Cdd:cd19915      1 TNPVSGLLEYARSKGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHNKKQGKQEAADAALRVLIGE 71
DSRM_DRADA_rpt1 cd19913
first double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 421-491 1.04e-41

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.


Pssm-ID: 380742  Cd Length: 71  Bit Score: 146.94  E-value: 1.04e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  421 KNPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILLRE 491
Cdd:cd19913      1 KNPVSGLMEYAQFLGQTCEFLLLEQSGPSHDPRFKFQAVIDGRRFPPAEASSKKVAKKDAAAIALKILLRE 71
DSRM_DRADA_rpt2 cd19914
second double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 532-602 1.78e-38

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.


Pssm-ID: 380743  Cd Length: 71  Bit Score: 137.67  E-value: 1.78e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  532 KSPVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALQEE 602
Cdd:cd19914      1 KNPISVLMEHSQKSGNMCEFQLLSQEGPPHDPKFTYCVKVGEQTFPSVVANSKKVAKQMAAEEAVKELMGE 71
DSRM_DRADA cd19902
double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) ...
 640-710 1.83e-33

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.


Pssm-ID: 380731  Cd Length: 71  Bit Score: 123.17  E-value: 1.83e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  640 TNPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVLIGE 710
Cdd:cd19902      1 KNPVSALMEYAQSRGVTAEIEVLSQSGPPHNPRFKAAVFVGGRRFPSVEASSKKDAKQEAADLALRALIAE 71
DSRM_DRADA cd19902
double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) ...
 421-491 5.48e-30

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.


Pssm-ID: 380731  Cd Length: 71  Bit Score: 113.54  E-value: 5.48e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  421 KNPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILLRE 491
Cdd:cd19902      1 KNPVSALMEYAQSRGVTAEIEVLSQSGPPHNPRFKAAVFVGGRRFPSVEASSKKDAKQEAADLALRALIAE 71
z-alpha pfam02295
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 145-211 3.87e-29

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.


Pssm-ID: 280459  Cd Length: 67  Bit Score: 110.67  E-value: 3.87e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  145 ISQNPEQKVLNRLEELGEGKATTAYALARELRTPKKDINRILYSLERKGKLHRGVGKPPLWSLVPLS 211
Cdd:pfam02295    1 DAQECAEKILELLENLGEGKAATAIALERGLSTPKREINRVLYDLERKGDVYREDGTPPRWFLTCAK 67
DSRM_DRADA cd19902
double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) ...
 532-602 1.32e-28

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.


Pssm-ID: 380731  Cd Length: 71  Bit Score: 109.30  E-value: 1.32e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  532 KSPVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALQEE 602
Cdd:cd19902      1 KNPVSALMEYAQSRGVTAEIEVLSQSGPPHNPRFKAAVFVGGRRFPSVEASSKKDAKQEAADLALRALIAE 71
z-alpha pfam02295
Adenosine deaminase z-alpha domain; This family consists of the N-terminus and thus the ...
 253-317 6.39e-23

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.


Pssm-ID: 280459  Cd Length: 67  Bit Score: 92.95  E-value: 6.39e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  253 DMAEIKEKICDYLFNVS-KSSALNLAKNIGLAK-ARDVNAVLIDLERQGDVYREGATPPIWYLTDKK 317
Cdd:pfam02295    1 DAQECAEKILELLENLGeGKAATAIALERGLSTpKREINRVLYDLERKGDVYREDGTPPRWFLTCAK 67
DSRM_DRADA_rpt1 cd19913
first double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 641-710 5.57e-22

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.


Pssm-ID: 380742  Cd Length: 71  Bit Score: 90.70  E-value: 5.57e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  641 NPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVLIGE 710
Cdd:cd19913      2 NPVSGLMEYAQFLGQTCEFLLLEQSGPSHDPRFKFQAVIDGRRFPPAEASSKKVAKKDAAAIALKILLRE 71
Zalpha smart00550
Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known ...
 251-317 1.99e-21

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


Pssm-ID: 128823  Cd Length: 68  Bit Score: 88.93  E-value: 1.99e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887   251 LLDMAEIKEKICDYLFNVS--KSSALNLAKNIGLAKaRDVNAVLIDLERQGDVYREGATPPIWYLTDKK 317
Cdd:smart00550    1 SLTQDSLEEKILEFLENSGdeTSTALQLAKNLGLPK-KEVNRVLYSLEKKGKVCKQGGTPPLWKLTDKA 68
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 641-707 2.39e-21

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.


Pssm-ID: 380704  Cd Length: 67  Bit Score: 88.48  E-value: 2.39e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  641 NPVGGLLEYARSHGFAAEFKlIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:cd19875      2 NPVSALNEYCQKRGLSLEFV-DVSVGPDHCPGFTASATIDGIVFASATGTSKKEAKRAAAKLALKKL 67
DSRM_DRADA_rpt2 cd19914
second double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 641-710 4.37e-21

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.


Pssm-ID: 380743  Cd Length: 71  Bit Score: 87.98  E-value: 4.37e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  641 NPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVLIGE 710
Cdd:cd19914      2 NPISVLMEHSQKSGNMCEFQLLSQEGPPHDPKFTYCVKVGEQTFPSVVANSKKVAKQMAAEEAVKELMGE 71
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 421-488 8.23e-21

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.


Pssm-ID: 380704  Cd Length: 67  Bit Score: 86.94  E-value: 8.23e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  421 KNPVSGLLEYAQFTSQTCDFNlIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:cd19875      1 KNPVSALNEYCQKRGLSLEFV-DVSVGPDHCPGFTASATIDGIVFASATGTSKKEAKRAAAKLALKKL 67
DSRM_DRADA_rpt2 cd19914
second double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 421-491 9.17e-21

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.


Pssm-ID: 380743  Cd Length: 71  Bit Score: 87.21  E-value: 9.17e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  421 KNPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILLRE 491
Cdd:cd19914      1 KNPISVLMEHSQKSGNMCEFQLLSQEGPPHDPKFTYCVKVGEQTFPSVVANSKKVAKQMAAEEAVKELMGE 71
DSRM smart00358
Double-stranded RNA binding motif;
423-488 5.41e-20

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 84.62  E-value: 5.41e-20
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887   423 PVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSL 66
DSRM smart00358
Double-stranded RNA binding motif;
534-600 1.01e-18

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 81.16  E-value: 1.01e-18
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887   534 PVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALQ 600
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSLK 67
DSRM_DRADA_rpt3 cd19915
third double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 421-491 1.95e-18

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.


Pssm-ID: 380744  Cd Length: 71  Bit Score: 80.37  E-value: 1.95e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  421 KNPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILLRE 491
Cdd:cd19915      1 TNPVSGLLEYARSKGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHNKKQGKQEAADAALRVLIGE 71
Zalpha smart00550
Z-DNA-binding domain in adenosine deaminases; Helix-turn-helix-containing domain. Also known ...
 144-207 3.04e-18

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


Pssm-ID: 128823  Cd Length: 68  Bit Score: 79.69  E-value: 3.04e-18
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958752887   144 SISQNP-EQKVLNRLEELGEGkATTAYALARELRTPKKDINRILYSLERKGKLHRGVGKPPLWSL 207
Cdd:smart00550    1 SLTQDSlEEKILEFLENSGDE-TSTALQLAKNLGLPKKEVNRVLYSLEKKGKVCKQGGTPPLWKL 64
DSRM_DRADA_rpt1 cd19913
first double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 532-602 4.21e-18

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.


Pssm-ID: 380742  Cd Length: 71  Bit Score: 79.53  E-value: 4.21e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  532 KSPVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALQEE 602
Cdd:cd19913      1 KNPVSGLMEYAQFLGQTCEFLLLEQSGPSHDPRFKFQAVIDGRRFPPAEASSKKVAKKDAAAIALKILLRE 71
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
 422-488 5.51e-17

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.


Pssm-ID: 380732  Cd Length: 68  Bit Score: 76.27  E-value: 5.51e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  422 NPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:cd19903      2 NYMGKLNEYCQKQKVVLDYVEVPTSGPSHDPRFTFQVVIDGKEYPEGEGKSKKEAKQAAAKLALEIL 68
PHA03103 PHA03103
double-strand RNA-binding protein; Provisional
 253-489 1.28e-16

double-strand RNA-binding protein; Provisional


Pssm-ID: 222987 [Multi-domain]  Cd Length: 183  Bit Score: 79.03  E-value: 1.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  253 DMAEIKEKICDYLFNVSKS---SALNLAKNIGLAKaRDVNAVLIDLERQGDVYREGATPPIWYLTdkkrerlqmkrsths 329
Cdd:PHA03103     7 DEVDIYELVKKEVKNLGLGegiTAIEISRKLNIEK-SEVNKQLYKLQREGMVYMSDSNPPKWFKT--------------- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  330 gpaatpaavseaTQStsfptchppqsggsssmatskrvENGQEPVTKYESRHearpgpvrlrphayHNGPSRAGPTLPrc 409
Cdd:PHA03103    71 ------------TEA-----------------------DNDDNDDVSREKSM--------------REDNKSFSDTIP-- 99

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  410 spYKKLTECQLKNPVSGLLEYAQFTSQTCDFNlIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILL 489
Cdd:PHA03103   100 --YKKIISWKDKNPCTVINEYCQITSRDWSIN-ITSSGPSHSPTFTASVIISGIKFKPAIGSTKKEAKNNAAKLAMDKIL 176
DSRM smart00358
Double-stranded RNA binding motif;
642-707 2.47e-15

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 71.53  E-value: 2.47e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887   642 PVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 423-488 2.74e-14

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.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 68.41  E-value: 2.74e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  423 PVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
 640-707 3.00e-14

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.


Pssm-ID: 380732  Cd Length: 68  Bit Score: 68.57  E-value: 3.00e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  640 TNPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:cd19903      1 GNYMGKLNEYCQKQKVVLDYVEVPTSGPSHDPRFTFQVVIDGKEYPEGEGKSKKEAKQAAAKLALEIL 68
DSRM_ADAD1 cd19905
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) ...
 421-489 3.16e-14

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.


Pssm-ID: 380734  Cd Length: 69  Bit Score: 68.45  E-value: 3.16e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  421 KNPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILL 489
Cdd:cd19905      1 KNPVSALHEYAQMTRLKLSFKETVTTGNVAGPYFAFCAVVDGIEYPTGVGKTKKEAKANAAKIALDELL 69
DSRM_PRKRA-like_rpt1 cd19862
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
 532-601 3.66e-11

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.


Pssm-ID: 380691 [Multi-domain]  Cd Length: 70  Bit Score: 59.97  E-value: 3.66e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  532 KSPVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAAEEAMKALQE 601
Cdd:cd19862      1 KTPISVLQELCAKRGITPKYELISSEGAVHEPTFTFRVTVGDITATG-SGTSKKKAKHAAAENALEQLKG 69
DSRM_PRKRA-like_rpt1 cd19862
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
 641-709 4.95e-11

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.


Pssm-ID: 380691 [Multi-domain]  Cd Length: 70  Bit Score: 59.58  E-value: 4.95e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958752887  641 NPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGrwfpAVC---AHSKKQGKQDAADAALRVLIG 709
Cdd:cd19862      2 TPISVLQELCAKRGITPKYELISSEGAVHEPTFTFRVTVGD----ITAtgsGTSKKKAKHAAAENALEQLKG 69
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
 531-599 6.86e-11

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.


Pssm-ID: 380699  Cd Length: 75  Bit Score: 59.22  E-value: 6.86e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  531 GKSPVTTLLE-CMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTF-PSVSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19870      1 GKHPVSALMElCNKRKWGPPEFRLVEESGPPHRKHFLFKVVVNGVEYqPSVASGNKKDAKAQAATVALQAL 71
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 642-707 1.15e-10

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.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 58.40  E-value: 1.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  642 PVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
 421-488 1.82e-10

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.


Pssm-ID: 380682 [Multi-domain]  Cd Length: 69  Bit Score: 57.89  E-value: 1.82e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  421 KNPVSGLLEYAQ-FTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:cd10845      1 KDYKTALQEYLQkRGLPLPEYELVEEEGPDHNKTFTVEVKVNGKVIGEGTGRSKKEAEQAAAKAALEKL 69
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
 640-707 1.83e-10

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.


Pssm-ID: 380682 [Multi-domain]  Cd Length: 69  Bit Score: 57.89  E-value: 1.83e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  640 TNPVGGLLEYARSHGFAA-EFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:cd10845      1 KDYKTALQEYLQKRGLPLpEYELVEEEGPDHNKTFTVEVKVNGKVIGEGTGRSKKEAEQAAAKAALEKL 69
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 534-599 2.82e-10

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.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 57.24  E-value: 2.82e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  534 PVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKAL 599
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 532-599 3.00e-10

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.


Pssm-ID: 380704  Cd Length: 67  Bit Score: 57.28  E-value: 3.00e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  532 KSPVTTLLE-CMhKLGNSCEFRLLSkEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19875      1 KNPVSALNEyCQ-KRGLSLEFVDVS-VGPDHCPGFTASATIDGIVFASATGTSKKEAKRAAAKLALKKL 67
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 422-488 8.85e-10

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.


Pssm-ID: 380746  Cd Length: 68  Bit Score: 55.86  E-value: 8.85e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  422 NPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:cd20314      2 NYVSLLNEYCQKERLTVKYEEEKRSGPTHKPRFFCKYIIDGKEYPEGEGKSKKEAKQAAARLAYEEL 68
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
 421-481 1.14e-09

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.


Pssm-ID: 380699  Cd Length: 75  Bit Score: 55.75  E-value: 1.14e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958752887  421 KNPVSGLLEY-AQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEA-GSKKVAKQDAA 481
Cdd:cd19870      2 KHPVSALMELcNKRKWGPPEFRLVEESGPPHRKHFLFKVVVNGVEYQPSVAsGNKKDAKAQAA 64
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
421-488 2.46e-09

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 58.96  E-value: 2.46e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  421 KNPVSGLLEYAQFTSQTC-DFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:COG0571    157 KDYKTALQEWLQARGLPLpEYEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGRSKKEAEQAAAKAALEKL 225
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
 540-599 2.48e-09

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.


Pssm-ID: 380732  Cd Length: 68  Bit Score: 54.70  E-value: 2.48e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  540 ECMHKLGNSC-------EFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19903      2 NYMGKLNEYCqkqkvvlDYVEVPTSGPSHDPRFTFQVVIDGKEYPEGEGKSKKEAKQAAAKLALEIL 68
DSRM_STRBP_RED-like_rpt1 cd19865
first double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This ...
 532-599 4.61e-09

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.


Pssm-ID: 380694  Cd Length: 63  Bit Score: 53.50  E-value: 4.61e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  532 KSPVTTLLECMHKLgnscEFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19865      1 KNALMQLNELRPGL----QYKLTSQTGPVHAPVFTMSVEVNGQTFEG-TGRSKKKAKLEAAEKALRSF 63
DSRM_DGCR8_rpt1 cd19867
first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
 421-489 9.07e-09

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


Pssm-ID: 380696  Cd Length: 74  Bit Score: 53.10  E-value: 9.07e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958752887  421 KNPVSGLLEYAQFTSQT---CDFNLIEQSGpshEPrFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILL 489
Cdd:cd19867      6 KSPVCILHEYCQRVLKVqpeYNFTETENAA---TP-FSAEVFINGVEYGSGEASSKKLAKQKAARATLEILI 73
DSRM_STRBP_RED-like_rpt1 cd19865
first double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This ...
 421-486 2.82e-08

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.


Pssm-ID: 380694  Cd Length: 63  Bit Score: 51.19  E-value: 2.82e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  421 KNPVSGLLEyaqfTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFpPAEAGSKKVAKQDAAVKAMA 486
Cdd:cd19865      1 KNALMQLNE----LRPGLQYKLTSQTGPVHAPVFTMSVEVNGQTF-EGTGRSKKKAKLEAAEKALR 61
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
 532-599 3.86e-08

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.


Pssm-ID: 380682 [Multi-domain]  Cd Length: 69  Bit Score: 51.34  E-value: 3.86e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  532 KSPVTTLLECMHKLGNSC-EFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd10845      1 KDYKTALQEYLQKRGLPLpEYELVEEEGPDHNKTFTVEVKVNGKVIGEGTGRSKKEAEQAAAKAALEKL 69
DSRM_TARBP2_rpt1 cd19890
first double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar ...
 531-601 4.03e-08

first double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar proteins; TARBP2 (also known as 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. TARBP2 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.


Pssm-ID: 380719  Cd Length: 72  Bit Score: 51.29  E-value: 4.03e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  531 GKSPVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGaQTFPSVSAPSKKVAKQMAAEEAMKALQE 601
Cdd:cd19890      2 GKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVG-DISCTGQGPSKKAAKHKAAEVALKLLKG 71
DSRM_PRKRA-like_rpt1 cd19862
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
 421-490 4.26e-08

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.


Pssm-ID: 380691 [Multi-domain]  Cd Length: 70  Bit Score: 51.11  E-value: 4.26e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  421 KNPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREfPPAEAGSKKVAKQDAAVKAMAILLR 490
Cdd:cd19862      1 KTPISVLQELCAKRGITPKYELISSEGAVHEPTFTFRVTVGDIT-ATGSGTSKKKAKHAAAENALEQLKG 69
DSRM_STRBP_RED-like_rpt1 cd19865
first double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This ...
 658-705 4.97e-08

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.


Pssm-ID: 380694  Cd Length: 63  Bit Score: 50.81  E-value: 4.97e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958752887  658 EFKLIDQSGPPHEPKFVYQAKVGGRWFPAVcAHSKKQGKQDAADAALR 705
Cdd:cd19865     15 QYKLTSQTGPVHAPVFTMSVEVNGQTFEGT-GRSKKKAKLEAAEKALR 61
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
531-602 7.99e-08

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 54.33  E-value: 7.99e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958752887  531 GKSPVTTLLECMHKLGNSC-EFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALQEE 602
Cdd:COG0571    156 GKDYKTALQEWLQARGLPLpEYEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGRSKKEAEQAAAKAALEKLGKK 228
RNaseIII TIGR02191
ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. ...
 633-704 1.15e-07

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]


Pssm-ID: 274024 [Multi-domain]  Cd Length: 220  Bit Score: 53.75  E-value: 1.15e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958752887  633 ELVRYLNTNPVGGLLEYARSHGFAA-EFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAAL 704
Cdd:TIGR02191  145 IIKEETLKDYKTALQEWAQARGKPLpEYRLIKEEGPDHDKEFTVEVSVNGEPYGEGKGKSKKEAEQNAAKAAL 217
DSRM_RED2_rpt1 cd19896
first double-stranded RNA binding motif of RNA-editing deaminase 2 (RED2) and similar proteins; ...
 533-599 2.13e-07

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.


Pssm-ID: 380725  Cd Length: 74  Bit Score: 49.32  E-value: 2.13e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  533 SPVTTLLEcMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19896      4 TPKNALVQ-LNELKPGLQYRMVSQTGPVHAPVFAVAVEVNGLTFEG-TGPTKKKAKMRAAEMALKSF 68
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 541-596 2.21e-07

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.


Pssm-ID: 380679 [Multi-domain]  Cd Length: 57  Bit Score: 48.82  E-value: 2.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  541 CMHKLGNSCEFRLlSKEGPAHDPKFQYCVAVGAQTFpSVSAPSKKVAKQMAAEEAM 596
Cdd:cd00048      4 CQKNKWPPPEYET-VEEGGPHNPRFTCTVTVNGQTF-EGEGKSKKEAKQAAAEKAL 57
DSRM_EIF2AK2_rpt2 cd19904
second double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
 422-489 2.61e-07

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.


Pssm-ID: 380733  Cd Length: 69  Bit Score: 49.05  E-value: 2.61e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  422 NPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILL 489
Cdd:cd19904      2 NYISLLNQYAQKKRLTVNYEQCASTGVPGPPRFSCKCKIGQKEYGIGTGSTKQEAKQAAAKEAYEQLL 69
DSRM_PRKRA_rpt1 cd19889
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
 531-600 3.27e-07

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


Pssm-ID: 380718 [Multi-domain]  Cd Length: 71  Bit Score: 48.76  E-value: 3.27e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  531 GKSPVTTLLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAAEEAMKALQ 600
Cdd:cd19889      1 GKTPIQLLHEYGTKTGNIPVYELEKSEGQAHLPSFTFRVTVGDITCTG-EGTSKKLAKHRAAEAALNILK 69
DSRM_ADAD1 cd19905
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) ...
 640-708 3.73e-07

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.


Pssm-ID: 380734  Cd Length: 69  Bit Score: 48.42  E-value: 3.73e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  640 TNPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVLI 708
Cdd:cd19905      1 KNPVSALHEYAQMTRLKLSFKETVTTGNVAGPYFAFCAVVDGIEYPTGVGKTKKEAKANAAKIALDELL 69
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 443-485 5.30e-07

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.


Pssm-ID: 380679 [Multi-domain]  Cd Length: 57  Bit Score: 47.66  E-value: 5.30e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958752887  443 IEQSGPSHEPRFKFQVVINGREFpPAEAGSKKVAKQDAAVKAM 485
Cdd:cd00048     16 TVEEGGPHNPRFTCTVTVNGQTF-EGEGKSKKEAKQAAAEKAL 57
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
646-707 6.60e-07

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 51.64  E-value: 6.60e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958752887  646 LLEYARSHGFAA-EFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:COG0571    163 LQEWLQARGLPLpEYEVVEEEGPDHAKTFTVEVLVGGKVLGEGTGRSKKEAEQAAAKAALEKL 225
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
 641-707 9.49e-07

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.


Pssm-ID: 380699  Cd Length: 75  Bit Score: 47.28  E-value: 9.49e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  641 NPVGGLLEY-ARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGG-RWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:cd19870      3 HPVSALMELcNKRKWGPPEFRLVEESGPPHRKHFLFKVVVNGvEYQPSVASGNKKDAKAQAATVALQAL 71
RNaseIII TIGR02191
ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. ...
 550-599 1.09e-06

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]


Pssm-ID: 274024 [Multi-domain]  Cd Length: 220  Bit Score: 50.67  E-value: 1.09e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958752887  550 EFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKAL 599
Cdd:TIGR02191  171 EYRLIKEEGPDHDKEFTVEVSVNGEPYGEGKGKSKKEAEQNAAKAALEKL 220
DSRM_AtDRB-like cd19878
double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins ...
 646-707 3.01e-06

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.


Pssm-ID: 380707 [Multi-domain]  Cd Length: 67  Bit Score: 45.97  E-value: 3.01e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958752887  646 LLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:cd19878      5 LQEYAQKKKIPLPKYESAKSGPSHQPTFVSTVIVLGVRFSSEGAKNKKQAEQSAAKVALKEL 66
DSRM_RED1_rpt1 cd19895
first double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins; ...
 534-599 3.14e-06

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.


Pssm-ID: 380724  Cd Length: 72  Bit Score: 45.84  E-value: 3.14e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  534 PVTTLLEcMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19895      5 PKNALMQ-LNEIKPGLQYKLLSQTGPVHAPVFVMSVEVNGQVFEG-SGPTKKKAKLHAAEKALRSF 68
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 648-704 3.88e-06

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.


Pssm-ID: 380679 [Multi-domain]  Cd Length: 57  Bit Score: 44.97  E-value: 3.88e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  648 EYARSHGF-AAEFKLIdQSGPPHEPKFVYQAKVGGRWFPAVcAHSKKQGKQDAADAAL 704
Cdd:cd00048      2 ELCQKNKWpPPEYETV-EEGGPHNPRFTCTVTVNGQTFEGE-GKSKKEAKQAAAEKAL 57
DSRM_AtDRB-like_rpt1 cd19907
first double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding ...
 427-488 3.93e-06

first 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). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380736 [Multi-domain]  Cd Length: 69  Bit Score: 45.54  E-value: 3.93e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  427 LLEYAQftsQTCdFNL----IEQSGPSHEPRFKFQVVINGREF-PPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:cd19907      6 LQEYAQ---KSC-LNLpvyaCIREGPDHAPRFRATVTFNGVIFeSPPGFPTLKAAEHSAAEVALNSL 68
DSRM_STRBP-like_rpt1 cd19894
first double-stranded RNA binding motif of STRBP, ILF3 and similar proteins; This family ...
 542-599 5.96e-06

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


Pssm-ID: 380723  Cd Length: 63  Bit Score: 44.68  E-value: 5.96e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  542 MHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19894      7 LNQLRPGLQYKLASQTGPVHAPQFTMSVEVDGVTYEA-SGPSKKTAKLHVAVKVLQAM 63
PHA02701 PHA02701
ORF020 dsRNA-binding PKR inhibitor; Provisional
 422-489 2.57e-05

ORF020 dsRNA-binding PKR inhibitor; Provisional


Pssm-ID: 177482 [Multi-domain]  Cd Length: 183  Bit Score: 46.09  E-value: 2.57e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  422 NPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKAMAILL 489
Cdd:PHA02701   109 NPVSAVNEFCMRTHRPLEFCETRSGGHDHCPLFTCTIVVSGKVVATASGCSKKLARHAACADALTILI 176
DSRM_AtDRB-like cd19878
double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins ...
 427-481 2.58e-05

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.


Pssm-ID: 380707 [Multi-domain]  Cd Length: 67  Bit Score: 43.27  E-value: 2.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958752887  427 LLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAA 481
Cdd:cd19878      5 LQEYAQKKKIPLPKYESAKSGPSHQPTFVSTVIVLGVRFSSEGAKNKKQAEQSAA 59
DSRM_STAU_rpt3 cd19859
third double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
 642-707 2.93e-05

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.


Pssm-ID: 380688  Cd Length: 65  Bit Score: 42.77  E-value: 2.93e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752887  642 PVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGrwFPAV-CAHSKKQGKQDAADAALRVL 707
Cdd:cd19859      1 EISLVHEIALKRNLTVNFEVLRESGPPHMKNFITRCTVGS--FVTEgEGNSKKVSKKRAAEKMLEEL 65
DSRM_STRBP-like_rpt1 cd19894
first double-stranded RNA binding motif of STRBP, ILF3 and similar proteins; This family ...
 440-488 3.22e-05

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


Pssm-ID: 380723  Cd Length: 63  Bit Score: 42.76  E-value: 3.22e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958752887  440 FNLIEQSGPSHEPRFKFQVVINGREFpPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:cd19894     16 YKLASQTGPVHAPQFTMSVEVDGVTY-EASGPSKKTAKLHVAVKVLQAM 63
DSRM_AtDRB-like cd19878
double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins ...
 554-600 3.71e-05

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.


Pssm-ID: 380707 [Multi-domain]  Cd Length: 67  Bit Score: 42.89  E-value: 3.71e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958752887  554 LSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALQ 600
Cdd:cd19878     21 SAKSGPSHQPTFVSTVIVLGVRFSSEGAKNKKQAEQSAAKVALKELG 67
DSRM_STRBP_RED-like_rpt2 cd19866
second double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This ...
 532-599 4.21e-05

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.


Pssm-ID: 380695  Cd Length: 63  Bit Score: 42.54  E-value: 4.21e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  532 KSPVTTLLEcmhkLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19866      1 KNPVMLLNE----LRPGLKYKCLSESGESHAKSFVMSVTVDGQTFEG-TGRSKKLAKAAAAQAALAKL 63
DSRM_STRBP_rpt1 cd19909
first double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) ...
 550-599 5.02e-05

first double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) and similar proteins; 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. STRBP contains an N-terminal DZF domain and 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.


Pssm-ID: 380738  Cd Length: 84  Bit Score: 43.10  E-value: 5.02e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958752887  550 EFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19909     20 QYKLLSQSGPVHAPVFTMSVDVDGTTYEA-SGPSKKTAKLHVAVKVLQAM 68
DSRM_STRBP_RED-like_rpt2 cd19866
second double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This ...
 421-488 5.39e-05

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.


Pssm-ID: 380695  Cd Length: 63  Bit Score: 42.15  E-value: 5.39e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  421 KNPVSGLLEyaqfTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAeAGSKKVAKQDAAVKAMAIL 488
Cdd:cd19866      1 KNPVMLLNE----LRPGLKYKCLSESGESHAKSFVMSVTVDGQTFEGT-GRSKKLAKAAAAQAALAKL 63
DSRM_RED1_rpt2 cd19898
second double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar ...
 530-599 1.32e-04

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.


Pssm-ID: 380727  Cd Length: 70  Bit Score: 41.33  E-value: 1.32e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  530 SGKSPVTTLLEcmhkLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19898      1 SGKNPVMILNE----LRPGLKYEFVSESGESHAKNFVMSVTVDGQTFEG-SGRNKKLAKARAAQAALAKL 65
DSRM_PRKRA_rpt1 cd19889
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
 421-488 1.35e-04

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


Pssm-ID: 380718 [Multi-domain]  Cd Length: 71  Bit Score: 41.44  E-value: 1.35e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  421 KNPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVInGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:cd19889      2 KTPIQLLHEYGTKTGNIPVYELEKSEGQAHLPSFTFRVTV-GDITCTGEGTSKKLAKHRAAEAALNIL 68
DSRM_RED1_rpt1 cd19895
first double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins; ...
 658-708 1.72e-04

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.


Pssm-ID: 380724  Cd Length: 72  Bit Score: 41.22  E-value: 1.72e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  658 EFKLIDQSGPPHEPKFVYQAKVGGRWFPAvCAHSKKQGKQDAADAALRVLI 708
Cdd:cd19895     20 QYKLLSQTGPVHAPVFVMSVEVNGQVFEG-SGPTKKKAKLHAAEKALRSFV 69
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 640-707 1.86e-04

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.


Pssm-ID: 380746  Cd Length: 68  Bit Score: 40.84  E-value: 1.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  640 TNPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVL 707
Cdd:cd20314      1 GNYVSLLNEYCQKERLTVKYEEEKRSGPTHKPRFFCKYIIDGKEYPEGEGKSKKEAKQAAARLAYEEL 68
DSRM_ILF3_rpt1 cd19910
first double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and ...
 542-601 2.82e-04

first double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and similar proteins; 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. ILF3 contains an N-terminal DZF domain and 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.


Pssm-ID: 380739  Cd Length: 73  Bit Score: 40.51  E-value: 2.82e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752887  542 MHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAaeeAMKALQE 601
Cdd:cd19910     12 LNQLKPGLQYKLISQTGPVHAPVFTMSVEVDGKTFEA-SGPSKKTAKLHV---AVKVLQD 67
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 556-599 3.14e-04

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.


Pssm-ID: 380746  Cd Length: 68  Bit Score: 40.07  E-value: 3.14e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958752887  556 KEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd20314     25 RSGPTHKPRFFCKYIIDGKEYPEGEGKSKKEAKQAAARLAYEEL 68
DSRM_TARBP2_rpt1 cd19890
first double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar ...
 421-488 3.67e-04

first double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar proteins; TARBP2 (also known as 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. TARBP2 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.


Pssm-ID: 380719  Cd Length: 72  Bit Score: 40.12  E-value: 3.67e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  421 KNPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVInGREFPPAEAGSKKVAKQDAAVKAMAIL 488
Cdd:cd19890      3 KTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTV-GDISCTGQGPSKKAAKHKAAEVALKLL 69
DSRM_STAU_rpt3 cd19859
third double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
 423-483 4.00e-04

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.


Pssm-ID: 380688  Cd Length: 65  Bit Score: 39.69  E-value: 4.00e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  423 PVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVInGREFPPAEAGSKKVAKQDAAVK 483
Cdd:cd19859      1 EISLVHEIALKRNLTVNFEVLRESGPPHMKNFITRCTV-GSFVTEGEGNSKKVSKKRAAEK 60
DSRM_AtDRB-like_rpt1 cd19907
first double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding ...
 556-599 4.41e-04

first 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). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380736 [Multi-domain]  Cd Length: 69  Bit Score: 39.77  E-value: 4.41e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958752887  556 KEGPAHDPKFQYCVAVGAQTFPSVSA-PSKKVAKQMAAEEAMKAL 599
Cdd:cd19907     24 REGPDHAPRFRATVTFNGVIFESPPGfPTLKAAEHSAAEVALNSL 68
DSRM_STRBP_rpt1 cd19909
first double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) ...
 422-485 4.50e-04

first double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) and similar proteins; 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. STRBP contains an N-terminal DZF domain and 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.


Pssm-ID: 380738  Cd Length: 84  Bit Score: 40.40  E-value: 4.50e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958752887  422 NPVSGLLEYAQFtSQTCDFNLIEQSGPSHEPRFKFQVVINGREFpPAEAGSKKVAKQDAAVKAM 485
Cdd:cd19909      4 QPMNALMRLNQI-RPGLQYKLLSQSGPVHAPVFTMSVDVDGTTY-EASGPSKKTAKLHVAVKVL 65
DSRM_DGCR8_rpt1 cd19867
first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
 639-708 4.60e-04

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


Pssm-ID: 380696  Cd Length: 74  Bit Score: 40.01  E-value: 4.60e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  639 NTNPVGGLLEYARsHGFAA----EFKLIDQSGPPhepkfvYQAKV--GGRWFPAVCAHSKKQGKQDAADAALRVLI 708
Cdd:cd19867      5 GKSPVCILHEYCQ-RVLKVqpeyNFTETENAATP------FSAEVfiNGVEYGSGEASSKKLAKQKAARATLEILI 73
DSRM_ILF3_rpt1 cd19910
first double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and ...
 440-485 4.97e-04

first double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and similar proteins; 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. ILF3 contains an N-terminal DZF domain and 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.


Pssm-ID: 380739  Cd Length: 73  Bit Score: 39.74  E-value: 4.97e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958752887  440 FNLIEQSGPSHEPRFKFQVVINGREFpPAEAGSKKVAKQDAAVKAM 485
Cdd:cd19910     21 YKLISQTGPVHAPVFTMSVEVDGKTF-EASGPSKKTAKLHVAVKVL 65
DSRM_AtDRB-like_rpt1 cd19907
first double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding ...
 646-707 5.12e-04

first 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). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380736 [Multi-domain]  Cd Length: 69  Bit Score: 39.38  E-value: 5.12e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958752887  646 LLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHS-KKQGKQDAADAALRVL 707
Cdd:cd19907      6 LQEYAQKSCLNLPVYACIREGPDHAPRFRATVTFNGVIFESPPGFPtLKAAEHSAAEVALNSL 68
DSRM_STAU_rpt1 cd19857
first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
 422-484 9.12e-04

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.


Pssm-ID: 380686  Cd Length: 64  Bit Score: 38.79  E-value: 9.12e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958752887  422 NPVSGLLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKA 484
Cdd:cd19857      1 TPMCLLNELARFNKIRPQYTLVDEEGPAHKKTFTVKLTLGDEEEYEASGSSIKKAQHAAAEKA 63
DSRM_DGCR8_rpt1 cd19867
first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
 530-599 9.61e-04

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


Pssm-ID: 380696  Cd Length: 74  Bit Score: 38.85  E-value: 9.61e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752887  530 SGKSPVTTLLE-CMHKLGNSCEFRLLSKEGPAhDPkFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19867      4 DGKSPVCILHEyCQRVLKVQPEYNFTETENAA-TP-FSAEVFINGVEYGSGEASSKKLAKQKAARATLEIL 72
DSRM_ILF3_rpt2 cd19912
second double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and ...
 421-489 9.88e-04

second double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and similar proteins; 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. ILF3 contains 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.


Pssm-ID: 380741  Cd Length: 72  Bit Score: 38.86  E-value: 9.88e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  421 KNPVSGLLEyaqfTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAeAGSKKVAKQDAAVKAMAILL 489
Cdd:cd19912      7 KNPVMELNE----KRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGA-GSNKKVAKAYAALAALEKLF 70
DSRM_STRBP_rpt2 cd19911
second double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) ...
 532-599 1.26e-03

second double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) and similar proteins; 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. STRBP contains 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.


Pssm-ID: 380740  Cd Length: 64  Bit Score: 38.19  E-value: 1.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  532 KSPVTTLLECMHKLgnscEFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19911      1 KNPVMELNEKRRGL----KYELISETGGSHDKRFVMEVEVDGQKFRG-AGPNKKVAKASAALAALEKL 63
DSRM_STRBP_rpt2 cd19911
second double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) ...
 421-489 1.92e-03

second double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) and similar proteins; 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. STRBP contains 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.


Pssm-ID: 380740  Cd Length: 64  Bit Score: 37.81  E-value: 1.92e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  421 KNPVSGLLEyaqfTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAeAGSKKVAKQDAAVKAMAILL 489
Cdd:cd19911      1 KNPVMELNE----KRRGLKYELISETGGSHDKRFVMEVEVDGQKFRGA-GPNKKVAKASAALAALEKLF 64
DSRM_EIF2AK2_rpt2 cd19904
second double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
 640-708 2.29e-03

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.


Pssm-ID: 380733  Cd Length: 69  Bit Score: 37.88  E-value: 2.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  640 TNPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQDAADAALRVLI 708
Cdd:cd19904      1 VNYISLLNQYAQKKRLTVNYEQCASTGVPGPPRFSCKCKIGQKEYGIGTGSTKQEAKQAAAKEAYEQLL 69
DSRM_PRKRA_rpt2 cd19891
second double-stranded RNA binding motif of protein activator of the interferon-induced ...
 641-704 2.44e-03

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.


Pssm-ID: 380720  Cd Length: 67  Bit Score: 37.61  E-value: 2.44e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958752887  641 NPVGGLLEYARSHGFA-AEFKLIDQSGPPHEPKFVYQAKVgGRWFPAVCAHSKKQGKQDAADAAL 704
Cdd:cd19891      1 NPIGSLQELAVQKGWRlPEYTLAQESGPPHKREFTITCRV-ETFVETGTGTSKKVAKRNAAEKLL 64
DSRM_PRKRA_rpt1 cd19889
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
 642-710 2.64e-03

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


Pssm-ID: 380718 [Multi-domain]  Cd Length: 71  Bit Score: 37.58  E-value: 2.64e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958752887  642 PVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVGgrwfPAVCA---HSKKQGKQDAADAALRVLIGE 710
Cdd:cd19889      4 PIQLLHEYGTKTGNIPVYELEKSEGQAHLPSFTFRVTVG----DITCTgegTSKKLAKHRAAEAALNILKGN 71
DSRM_DCL_plant cd19869
double-stranded RNA binding motif of plant Dicer-like proteins; The family includes plant ...
 658-707 2.87e-03

double-stranded RNA binding motif of plant Dicer-like proteins; The family includes plant Dicer-like (DCL) proteins and other ribonuclease (RNase) III-like (RTL) proteins. DCLs are endoribonucleases involved in RNA-mediated post-transcriptional gene silencing (PTGS). They function in the microRNA (miRNA) biogenesis pathway by cleaving primary miRNAs (pri-miRNAs) and precursor miRNAs (pre-miRNAs). Family members 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.


Pssm-ID: 380698  Cd Length: 70  Bit Score: 37.35  E-value: 2.87e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  658 EFKLIDQSGPPHEPKFVYQAKVG--GRWFPAVCA----HSKKQGKQDAADAALRVL 707
Cdd:cd19869     13 VYRCVEEEGPAHAKRFTYMVRVKipERGWTIECEgepmRSKKRAKDSAALLLLEYL 68
DSRM_DCL_plant cd19869
double-stranded RNA binding motif of plant Dicer-like proteins; The family includes plant ...
 439-488 3.01e-03

double-stranded RNA binding motif of plant Dicer-like proteins; The family includes plant Dicer-like (DCL) proteins and other ribonuclease (RNase) III-like (RTL) proteins. DCLs are endoribonucleases involved in RNA-mediated post-transcriptional gene silencing (PTGS). They function in the microRNA (miRNA) biogenesis pathway by cleaving primary miRNAs (pri-miRNAs) and precursor miRNAs (pre-miRNAs). Family members 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.


Pssm-ID: 380698  Cd Length: 70  Bit Score: 37.35  E-value: 3.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752887  439 DFNLIEQSGPSHEPRFKFQVVINGREFP-PAEA-----GSKKVAKQDAAVKAMAIL 488
Cdd:cd19869     13 VYRCVEEEGPAHAKRFTYMVRVKIPERGwTIECegepmRSKKRAKDSAALLLLEYL 68
DSRM_AtDRB-like_rpt2 cd19908
second double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding ...
 427-484 3.98e-03

second 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). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380737 [Multi-domain]  Cd Length: 69  Bit Score: 37.07  E-value: 3.98e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752887  427 LLEYAQFTSQTCDFNLIEQSGPSHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAVKA 484
Cdd:cd19908      7 LQEYAQKAGLPLPLYTTVRSGPGHVPTFTCTVEIAGITFTGEAAKTKKQAEKSAARTA 64
DSRM_RED1_rpt1 cd19895
first double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins; ...
 440-485 4.35e-03

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.


Pssm-ID: 380724  Cd Length: 72  Bit Score: 36.98  E-value: 4.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958752887  440 FNLIEQSGPSHEPRFKFQVVINGREFpPAEAGSKKVAKQDAAVKAM 485
Cdd:cd19895     21 YKLLSQTGPVHAPVFVMSVEVNGQVF-EGSGPTKKKAKLHAAEKAL 65
DSRM_AtDRB-like_rpt2 cd19908
second double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding ...
 538-600 4.57e-03

second 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). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380737 [Multi-domain]  Cd Length: 69  Bit Score: 36.69  E-value: 4.57e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958752887  538 LLECMHKLGNSCEFRLLSKEGPAHDPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALQ 600
Cdd:cd19908      7 LQEYAQKAGLPLPLYTTVRSGPGHVPTFTCTVEIAGITFTGEAAKTKKQAEKSAARTAWSSIK 69
DSRM_STAU_rpt1 cd19857
first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
 641-704 7.06e-03

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.


Pssm-ID: 380686  Cd Length: 64  Bit Score: 36.09  E-value: 7.06e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958752887  641 NPVGGLLEYARSHGFAAEFKLIDQSGPPHEPKFVYQAKVG-GRWFPAVcAHSKKQGKQDAADAAL 704
Cdd:cd19857      1 TPMCLLNELARFNKIRPQYTLVDEEGPAHKKTFTVKLTLGdEEEYEAS-GSSIKKAQHAAAEKAL 64
DSRM_ILF3_rpt2 cd19912
second double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and ...
 531-599 7.63e-03

second double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and similar proteins; 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. ILF3 contains 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.


Pssm-ID: 380741  Cd Length: 72  Bit Score: 36.55  E-value: 7.63e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752887  531 GKSPVTTLLECMHKLgnscEFRLLSKEGPAHDPKFQYCVAVGAQTFPSvSAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19912      6 GKNPVMELNEKRRGL----KYELISETGGSHDKRFVMEVEVDGQKFQG-AGSNKKVAKAYAALAALEKL 69
DSRM_STAU_rpt4 cd19860
fourth double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
 550-599 8.65e-03

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


Pssm-ID: 380689  Cd Length: 68  Bit Score: 36.16  E-value: 8.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958752887  550 EFRLLSKEGPAHDPKFQYCVAVGAQTFPSVsAPSKKVAKQMAAEEAMKAL 599
Cdd:cd19860     19 VYSLVAERGTPRRREFVMQVTVGDKTATGT-GPNKKLAKRNAAEAMLELL 67
seadorna_dsRNA TIGR04238
seadornavirus double-stranded RNA-binding protein; This protein family occurs in the ...
 641-700 9.28e-03

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.


Pssm-ID: 275074 [Multi-domain]  Cd Length: 201  Bit Score: 38.77  E-value: 9.28e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958752887  641 NPVGGLLEYARSHGFAAE-FKLIDQSGPPHEPKFVYQAKVGGrwFPAVC-AHSKKQGKQDAA 700
Cdd:TIGR04238    1 NVVGMLQELAVKRGLELPvYEKVGKEGPDHAPTFTIKLTAND--IEVIEaASSKKQAEKLAA 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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