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Conserved domains on  [gi|254675158|ref|NP_083704|]
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adenosine deaminase domain-containing protein 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
 239-554 1.67e-77

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: 245.94  E-value: 1.67e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  239 ALGTGSSSCAG-WLEFSGRRLHDCHGLVIARRALLRFFFRQLLLVTQGGPkgqERSVLTPQPGPGPpFALKPGVFLHLYV 317
Cdd:pfam02137   1 ALGTGTKCIGGsKLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNP---SKSIFEPNPDSGK-LRLKPGISFHLYI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  318 SNTPKGAAHdIYLPLASE-DSVLHSPAF------RLQAHVCGQLKPVSYVAPALRDT-----HVGCLSASDKLARWAILG 385
Cdd:pfam02137  77 SQTPCGDAR-IFSPLELEpESSPAHPVRrfrgqlRLKVETGAKTIPVESSEDQTWDGvkpgrRTLSMSCSDKLARWNVLG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  386 LGGGLLAHFLPPLYATSLVLADPCHDPSTLNRVIHSrpRLDSVLGScLPCPYVRTTLHLFAGplvapsdpgpstchslsl 465
Cdd:pfam02137 156 VQGALLSHFIEPIYLSSITVGGSLYDTEHLERAIYQ--RLDGVLDS-LPPPYRVNKPLIGQV------------------ 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  466 nwslgdpdievvdvatgrvktdssvgpPSRLCKAAFLSAFRQVARALEKPQLLSLQTYEAAK--AVPYREARQQLSLLLD 543
Cdd:pfam02137 215 ---------------------------ASRLCKAALFSRFLKLLSELSREDLLAPLTYHEAKaaAKDYQEAKQQLKSLLR 267

                         330
                  ....*....|.
gi 254675158  544 QQGLGAWPSKP 554
Cdd:pfam02137 268 QQGLGSWIRKP 278
DSRM_SF super family cl00054
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 90-157 1.38e-12

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 cd19906:

Pssm-ID: 444671  Cd Length: 74  Bit Score: 62.94  E-value: 1.38e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675158  90 PPAQAVALLTQCMANLGVSLTFLEDQTAGPGSSFSVCADL------DGLVCPAGTGSSKLEAKQQAALSALQYI 157
Cdd:cd19906    1 PPKTPLSLLHEYAAKLSLEVEFRETQEEGPVGPFTVSARLrsrvqrTGVVCGAGTARAKKDAKQVAAAAALEKL 74
 
Name Accession Description Interval E-value
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
 239-554 1.67e-77

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: 245.94  E-value: 1.67e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  239 ALGTGSSSCAG-WLEFSGRRLHDCHGLVIARRALLRFFFRQLLLVTQGGPkgqERSVLTPQPGPGPpFALKPGVFLHLYV 317
Cdd:pfam02137   1 ALGTGTKCIGGsKLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNP---SKSIFEPNPDSGK-LRLKPGISFHLYI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  318 SNTPKGAAHdIYLPLASE-DSVLHSPAF------RLQAHVCGQLKPVSYVAPALRDT-----HVGCLSASDKLARWAILG 385
Cdd:pfam02137  77 SQTPCGDAR-IFSPLELEpESSPAHPVRrfrgqlRLKVETGAKTIPVESSEDQTWDGvkpgrRTLSMSCSDKLARWNVLG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  386 LGGGLLAHFLPPLYATSLVLADPCHDPSTLNRVIHSrpRLDSVLGScLPCPYVRTTLHLFAGplvapsdpgpstchslsl 465
Cdd:pfam02137 156 VQGALLSHFIEPIYLSSITVGGSLYDTEHLERAIYQ--RLDGVLDS-LPPPYRVNKPLIGQV------------------ 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  466 nwslgdpdievvdvatgrvktdssvgpPSRLCKAAFLSAFRQVARALEKPQLLSLQTYEAAK--AVPYREARQQLSLLLD 543
Cdd:pfam02137 215 ---------------------------ASRLCKAALFSRFLKLLSELSREDLLAPLTYHEAKaaAKDYQEAKQQLKSLLR 267

                         330
                  ....*....|.
gi 254675158  544 QQGLGAWPSKP 554
Cdd:pfam02137 268 QQGLGSWIRKP 278
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
199-554 2.14e-46

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


Pssm-ID: 214718  Cd Length: 374  Bit Score: 166.78  E-value: 2.14e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158   199 DRLLSESSPYQACKGTVAAVILEREVQGSIghsketyELVALGTG----SSSCagwLEFSGRRLHDCHGLVIARRALLRF 274
Cdd:smart00552  15 GSLPKIGKPGLREWTILAGVVMTNGMDNEK-------QVVSLGTGtkciSGEK---LSPNGLVLNDCHAEILARRGFLRF 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158   275 FFRQLLLVTQGgpkgQERSVLTPQPGpGPPFALKPGVFLHLYVSNTPKGAAHdIYLPLASEDSVLhSPAFRLQAHVCGQL 354
Cdd:smart00552  85 LYSELQLFNSS----SEDSIFEKNKE-GGKYKLKSNVLFHLYISTLPCGDAS-IFSPLEPLKNDD-SKHPVRKNIKRSKL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158   355 kpvSYVAPALRDTHVGCL-------------------SASDKLARWAILGLGGGLLAHFLPPLYATSLVLADPCHDPSTL 415
Cdd:smart00552 158 ---RTKIEIGEGTVPVRSsdivqtwdgigdgerllsmSCSDKIARWNVLGVQGALLSHFIEPIYLSSIVLGKSLYSAEHL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158   416 NRVIHSR-PRLDSvlgscLPCPYVRTTLHLFAGPLVAP-SDPGPSTChsLSLNWSLGDPDIEVVDVATGrvKTDSSVGPP 493
Cdd:smart00552 235 ERALYGRlDPLDG-----LPTPFRVNRPLISLVSVADFqRQTAKSPN--FSVNWSQGDESLEILNGLTG--KTQKSLGSP 305

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675158   494 SRLCKAAFLSAFRQVARALEKPQLLSLqTYEAAK--AVPYREARQQLSLLLDQQGLGAWPSKP 554
Cdd:smart00552 306 SRLCKKALFRLFQKLCSKLKRDDLLHI-SYAEAKeaASEYQEAKQLLFEALNKAGLGSWIKKP 367
DSRM_ADAD2 cd19906
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 2 (ADAD2) ...
 90-157 1.38e-12

double-stranded RNA binding motif of adenosine deaminase domain-containing protein 2 (ADAD2) and similar proteins; ADAD2 (also known as testis nuclear RNA-binding protein-like (TENRL)) is phylogenetically related to a family of adenosine deaminases involved in RNA editing. It is a double-stranded RNA binding protein with unclear biological function. ADAD2 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: 380735  Cd Length: 74  Bit Score: 62.94  E-value: 1.38e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675158  90 PPAQAVALLTQCMANLGVSLTFLEDQTAGPGSSFSVCADL------DGLVCPAGTGSSKLEAKQQAALSALQYI 157
Cdd:cd19906    1 PPKTPLSLLHEYAAKLSLEVEFRETQEEGPVGPFTVSARLrsrvqrTGVVCGAGTARAKKDAKQVAAAAALEKL 74
DSRM smart00358
Double-stranded RNA binding motif;
94-158 7.01e-07

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 46.49  E-value: 7.01e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675158    94 AVALLTQCMANLGVSLTFLEDQTAGPGSS--FSVCADLDGLVCPAGTGSSKLEAKQQAALSALQYIQ 158
Cdd:smart00358   1 PKSLLQELAQKRKLPPEYELVKEEGPDHAprFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSLK 67
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 94-157 1.18e-06

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: 46.07  E-value: 1.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675158   94 AVALLTQCMANLGVSLTFLEDQTAGPGSS--FSVCADLDGLVCPAGTGSSKLEAKQQAALSALQYI 157
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSpkFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
123-160 8.98e-03

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 38.16  E-value: 8.98e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 254675158 123 FSVCADLDGLVCPAGTGSSKLEAKQQAALSALQYIQKQ 160
Cdd:COG0571  191 FTVEVLVGGKVLGEGTGRSKKEAEQAAAKAALEKLGKK 228
 
Name Accession Description Interval E-value
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
 239-554 1.67e-77

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: 245.94  E-value: 1.67e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  239 ALGTGSSSCAG-WLEFSGRRLHDCHGLVIARRALLRFFFRQLLLVTQGGPkgqERSVLTPQPGPGPpFALKPGVFLHLYV 317
Cdd:pfam02137   1 ALGTGTKCIGGsKLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNP---SKSIFEPNPDSGK-LRLKPGISFHLYI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  318 SNTPKGAAHdIYLPLASE-DSVLHSPAF------RLQAHVCGQLKPVSYVAPALRDT-----HVGCLSASDKLARWAILG 385
Cdd:pfam02137  77 SQTPCGDAR-IFSPLELEpESSPAHPVRrfrgqlRLKVETGAKTIPVESSEDQTWDGvkpgrRTLSMSCSDKLARWNVLG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  386 LGGGLLAHFLPPLYATSLVLADPCHDPSTLNRVIHSrpRLDSVLGScLPCPYVRTTLHLFAGplvapsdpgpstchslsl 465
Cdd:pfam02137 156 VQGALLSHFIEPIYLSSITVGGSLYDTEHLERAIYQ--RLDGVLDS-LPPPYRVNKPLIGQV------------------ 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158  466 nwslgdpdievvdvatgrvktdssvgpPSRLCKAAFLSAFRQVARALEKPQLLSLQTYEAAK--AVPYREARQQLSLLLD 543
Cdd:pfam02137 215 ---------------------------ASRLCKAALFSRFLKLLSELSREDLLAPLTYHEAKaaAKDYQEAKQQLKSLLR 267

                         330
                  ....*....|.
gi 254675158  544 QQGLGAWPSKP 554
Cdd:pfam02137 268 QQGLGSWIRKP 278
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
199-554 2.14e-46

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


Pssm-ID: 214718  Cd Length: 374  Bit Score: 166.78  E-value: 2.14e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158   199 DRLLSESSPYQACKGTVAAVILEREVQGSIghsketyELVALGTG----SSSCagwLEFSGRRLHDCHGLVIARRALLRF 274
Cdd:smart00552  15 GSLPKIGKPGLREWTILAGVVMTNGMDNEK-------QVVSLGTGtkciSGEK---LSPNGLVLNDCHAEILARRGFLRF 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158   275 FFRQLLLVTQGgpkgQERSVLTPQPGpGPPFALKPGVFLHLYVSNTPKGAAHdIYLPLASEDSVLhSPAFRLQAHVCGQL 354
Cdd:smart00552  85 LYSELQLFNSS----SEDSIFEKNKE-GGKYKLKSNVLFHLYISTLPCGDAS-IFSPLEPLKNDD-SKHPVRKNIKRSKL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158   355 kpvSYVAPALRDTHVGCL-------------------SASDKLARWAILGLGGGLLAHFLPPLYATSLVLADPCHDPSTL 415
Cdd:smart00552 158 ---RTKIEIGEGTVPVRSsdivqtwdgigdgerllsmSCSDKIARWNVLGVQGALLSHFIEPIYLSSIVLGKSLYSAEHL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675158   416 NRVIHSR-PRLDSvlgscLPCPYVRTTLHLFAGPLVAP-SDPGPSTChsLSLNWSLGDPDIEVVDVATGrvKTDSSVGPP 493
Cdd:smart00552 235 ERALYGRlDPLDG-----LPTPFRVNRPLISLVSVADFqRQTAKSPN--FSVNWSQGDESLEILNGLTG--KTQKSLGSP 305

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675158   494 SRLCKAAFLSAFRQVARALEKPQLLSLqTYEAAK--AVPYREARQQLSLLLDQQGLGAWPSKP 554
Cdd:smart00552 306 SRLCKKALFRLFQKLCSKLKRDDLLHI-SYAEAKeaASEYQEAKQLLFEALNKAGLGSWIKKP 367
DSRM_ADAD2 cd19906
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 2 (ADAD2) ...
 90-157 1.38e-12

double-stranded RNA binding motif of adenosine deaminase domain-containing protein 2 (ADAD2) and similar proteins; ADAD2 (also known as testis nuclear RNA-binding protein-like (TENRL)) is phylogenetically related to a family of adenosine deaminases involved in RNA editing. It is a double-stranded RNA binding protein with unclear biological function. ADAD2 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: 380735  Cd Length: 74  Bit Score: 62.94  E-value: 1.38e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675158  90 PPAQAVALLTQCMANLGVSLTFLEDQTAGPGSSFSVCADL------DGLVCPAGTGSSKLEAKQQAALSALQYI 157
Cdd:cd19906    1 PPKTPLSLLHEYAAKLSLEVEFRETQEEGPVGPFTVSARLrsrvqrTGVVCGAGTARAKKDAKQVAAAAALEKL 74
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 96-157 7.91e-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: 54.97  E-value: 7.91e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675158  96 ALLTQCMANlGVSLTFLEDQTAGPGSS-FSVCADLDGLVCPAGTGSSKLEAKQQAALSALQYI 157
Cdd:cd19875    6 ALNEYCQKR-GLSLEFVDVSVGPDHCPgFTASATIDGIVFASATGTSKKEAKRAAAKLALKKL 67
DSRM smart00358
Double-stranded RNA binding motif;
94-158 7.01e-07

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 46.49  E-value: 7.01e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675158    94 AVALLTQCMANLGVSLTFLEDQTAGPGSS--FSVCADLDGLVCPAGTGSSKLEAKQQAALSALQYIQ 158
Cdd:smart00358   1 PKSLLQELAQKRKLPPEYELVKEEGPDHAprFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSLK 67
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 94-157 1.18e-06

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: 46.07  E-value: 1.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675158   94 AVALLTQCMANLGVSLTFLEDQTAGPGSS--FSVCADLDGLVCPAGTGSSKLEAKQQAALSALQYI 157
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSpkFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM_ADAD1 cd19905
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) ...
 92-155 7.51e-06

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: 43.80  E-value: 7.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675158  92 AQAVALLTQCMANLGVSLTFLEDQTAGP--GSSFSVCADLDGLVCPAGTGSSKLEAKQQAALSALQ 155
Cdd:cd19905    1 KNPVSALHEYAQMTRLKLSFKETVTTGNvaGPYFAFCAVVDGIEYPTGVGKTKKEAKANAAKIALD 66
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 101-154 6.39e-04

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: 38.03  E-value: 6.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254675158 101 CMANLGVSLTFLEDQTAGPGS-SFSVCADLDGLVCpAGTGSSKLEAKQQAALSAL 154
Cdd:cd00048    4 CQKNKWPPPEYETVEEGGPHNpRFTCTVTVNGQTF-EGEGKSKKEAKQAAAEKAL 57
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
 95-157 9.98e-04

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: 37.75  E-value: 9.98e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675158  95 VALLTQCMANLGVSLTFLEDQTAGPGSS--FSVCADLDGLVCPAGTGSSKLEAKQQAALSALQYI 157
Cdd:cd19903    4 MGKLNEYCQKQKVVLDYVEVPTSGPSHDprFTFQVVIDGKEYPEGEGKSKKEAKQAAAKLALEIL 68
DSRM_PRKRA-like_rpt3 cd19864
third double-stranded RNA binding motif of PRKRA, TARBP2 and similar proteins; The family ...
 133-158 1.74e-03

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


Pssm-ID: 380693  Cd Length: 72  Bit Score: 37.20  E-value: 1.74e-03
                         10        20
                 ....*....|....*....|....*.
gi 254675158 133 VCPaGTGSSKLEAKQQAALSALQYIQ 158
Cdd:cd19864   45 VCH-GSGASLEEAKEEAARNALEYLK 69
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 95-157 2.29e-03

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: 36.60  E-value: 2.29e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675158  95 VALLTQCMANLGVSLTFLEDQTAGP-GSSFSVCA-DLDGLVCPAGTGSSKLEAKQQAALSALQYI 157
Cdd:cd20314    4 VSLLNEYCQKERLTVKYEEEKRSGPtHKPRFFCKyIIDGKEYPEGEGKSKKEAKQAAARLAYEEL 68
DSRM_DRADA cd19902
double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) ...
 94-155 3.46e-03

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: 36.50  E-value: 3.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675158  94 AVALLTQCMANLGVSLTF-LEDQTAGPGS-SFSVCADLDGLVCPAGTGSSKLEAKQQAALSALQ 155
Cdd:cd19902    3 PVSALMEYAQSRGVTAEIeVLSQSGPPHNpRFKAAVFVGGRRFPSVEASSKKDAKQEAADLALR 66
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
 123-157 5.71e-03

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: 35.55  E-value: 5.71e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 254675158 123 FSVCADLDGLVCPAGTGSSKLEAKQQAALSALQYI 157
Cdd:cd10845   35 FTVEVKVNGKVIGEGTGRSKKEAEQAAAKAALEKL 69
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
123-160 8.98e-03

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 38.16  E-value: 8.98e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 254675158 123 FSVCADLDGLVCPAGTGSSKLEAKQQAALSALQYIQKQ 160
Cdd:COG0571  191 FTVEVLVGGKVLGEGTGRSKKEAEQAAAKAALEKLGKK 228
 
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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