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Conserved domains on  [gi|21245124|ref|NP_640336|]
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adenosine deaminase domain-containing protein 1 isoform 1 [Homo sapiens]

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);
204-575 3.02e-132

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


:

Pssm-ID: 214718  Cd Length: 374  Bit Score: 390.59  E-value: 3.02e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    204 IQYAKISQIVKERFNQLISNRSEYLKYSSSLAAFIIERA--GQHEVVAIGTGEYNYSQD-IKPDGRVLHDTHAVVTARRS 280
Cdd:smart00552   1 DTGDEISQLVLEKFGSLPKIGKPGLREWTILAGVVMTNGmdNEKQVVSLGTGTKCISGEkLSPNGLVLNDCHAEILARRG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    281 LLRYFYRQLLLFYSKNpammEKSIFCTEPTSNLLTLKQNINICLYMNQLPKGSAQIKSQLRLNPHSISAFEANEELCLHV 360
Cdd:smart00552  81 FLRFLYSELQLFNSSS----EDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKNDDSKHPVRKNIKRSK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    361 ----------AVEGKIYLTVYCpKDGV---NRISSMSSSDKLTRWEVLGVQGALLSHFIQPVYISSILIGDgNCSDTRGL 427
Cdd:smart00552 157 lrtkieigegTVPVRSSDIVQT-WDGIgdgERLLSMSCSDKIARWNVLGVQGALLSHFIEPIYLSSIVLGK-SLYSAEHL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    428 EIAIKQRVDDAltSKLPMFYLVNRPHISLVPSAYPLQMNLEYKFLSLNWAQGDVSLEIVDGLSGKitesspFKSGMSMAS 507
Cdd:smart00552 235 ERALYGRLDPL--DGLPTPFRVNRPLISLVSVADFQRQTAKSPNFSVNWSQGDESLEILNGLTGK------TQKSLGSPS 306

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21245124    508 RLCKAAMLSRFNLLAKEAKKELLEAGTYHAAKCMSASYQEAKCKLKSYLQQHGYGSWIVKSPCIEQFN 575
Cdd:smart00552 307 RLCKKALFRLFQKLCSKLKRDDLLHISYAEAKEAASEYQEAKQLLFEALNKAGLGSWIKKPPEQDQFK 374
DSRM_ADAD1 cd19905
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) ...
 95-163 6.53e-38

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: 133.93  E-value: 6.53e-38
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21245124  95 INPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELL 163
Cdd:cd19905   1 KNPVSALHEYAQMTRLKLSFKETVTTGNVAGPYFAFCAVVDGIEYPTGVGKTKKEAKANAAKIALDELL 69
 
Name Accession Description Interval E-value
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
204-575 3.02e-132

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


Pssm-ID: 214718  Cd Length: 374  Bit Score: 390.59  E-value: 3.02e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    204 IQYAKISQIVKERFNQLISNRSEYLKYSSSLAAFIIERA--GQHEVVAIGTGEYNYSQD-IKPDGRVLHDTHAVVTARRS 280
Cdd:smart00552   1 DTGDEISQLVLEKFGSLPKIGKPGLREWTILAGVVMTNGmdNEKQVVSLGTGTKCISGEkLSPNGLVLNDCHAEILARRG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    281 LLRYFYRQLLLFYSKNpammEKSIFCTEPTSNLLTLKQNINICLYMNQLPKGSAQIKSQLRLNPHSISAFEANEELCLHV 360
Cdd:smart00552  81 FLRFLYSELQLFNSSS----EDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKNDDSKHPVRKNIKRSK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    361 ----------AVEGKIYLTVYCpKDGV---NRISSMSSSDKLTRWEVLGVQGALLSHFIQPVYISSILIGDgNCSDTRGL 427
Cdd:smart00552 157 lrtkieigegTVPVRSSDIVQT-WDGIgdgERLLSMSCSDKIARWNVLGVQGALLSHFIEPIYLSSIVLGK-SLYSAEHL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    428 EIAIKQRVDDAltSKLPMFYLVNRPHISLVPSAYPLQMNLEYKFLSLNWAQGDVSLEIVDGLSGKitesspFKSGMSMAS 507
Cdd:smart00552 235 ERALYGRLDPL--DGLPTPFRVNRPLISLVSVADFQRQTAKSPNFSVNWSQGDESLEILNGLTGK------TQKSLGSPS 306

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21245124    508 RLCKAAMLSRFNLLAKEAKKELLEAGTYHAAKCMSASYQEAKCKLKSYLQQHGYGSWIVKSPCIEQFN 575
Cdd:smart00552 307 RLCKKALFRLFQKLCSKLKRDDLLHISYAEAKEAASEYQEAKQLLFEALNKAGLGSWIKKPPEQDQFK 374
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
 249-568 2.20e-121

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: 359.18  E-value: 2.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124   249 AIGTGEYNYSQD-IKPDGRVLHDTHAVVTARRSLLRYFYRQLLLFYSKNPammEKSIFCTEPTSNLLTLKQNINICLYMN 327
Cdd:pfam02137   1 ALGTGTKCIGGSkLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNP---SKSIFEPNPDSGKLRLKPGISFHLYIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124   328 QLPKGSAQIKSQLRLNPHSISA---FEANEELCLHVAVEGKIYLTVYCP---KDGVN---RISSMSSSDKLTRWEVLGVQ 398
Cdd:pfam02137  78 QTPCGDARIFSPLELEPESSPAhpvRRFRGQLRLKVETGAKTIPVESSEdqtWDGVKpgrRTLSMSCSDKLARWNVLGVQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124   399 GALLSHFIQPVYISSILIGdGNCSDTRGLEIAIKQRVDDALTSkLPMFYLVNRPHISLVPsayplqmnleykflslnwaq 478
Cdd:pfam02137 158 GALLSHFIEPIYLSSITVG-GSLYDTEHLERAIYQRLDGVLDS-LPPPYRVNKPLIGQVA-------------------- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124   479 gdvsleivdglsgkitesspfksgmsmaSRLCKAAMLSRFNLLAKEAKKELLEAG-TYHAAKCMSASYQEAKCKLKSYLQ 557
Cdd:pfam02137 216 ----------------------------SRLCKAALFSRFLKLLSELSREDLLAPlTYHEAKAAAKDYQEAKQQLKSLLR 267

                         330
                  ....*....|.
gi 21245124   558 QHGYGSWIVKS 568
Cdd:pfam02137 268 QQGLGSWIRKP 278
DSRM_ADAD1 cd19905
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) ...
 95-163 6.53e-38

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: 133.93  E-value: 6.53e-38
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21245124  95 INPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELL 163
Cdd:cd19905   1 KNPVSALHEYAQMTRLKLSFKETVTTGNVAGPYFAFCAVVDGIEYPTGVGKTKKEAKANAAKIALDELL 69
DSRM smart00358
Double-stranded RNA binding motif;
97-162 1.24e-15

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 71.53  E-value: 1.24e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21245124     97 PVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDEL 162
Cdd:smart00358   1 PKSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 97-162 2.44e-13

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: 64.94  E-value: 2.44e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21245124    97 PVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDEL 162
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
PHA03103 PHA03103
double-strand RNA-binding protein; Provisional
 82-163 2.71e-10

double-strand RNA-binding protein; Provisional


Pssm-ID: 222987 [Multi-domain]  Cd Length: 183  Bit Score: 59.77  E-value: 2.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124   82 IPKEFIMKYKrgEINPVSALHQFAQMQRVQLDLKETvTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDE 161
Cdd:PHA03103  98 IPYKKIISWK--DKNPCTVINEYCQITSRDWSINIT-SSGPSHSPTFTASVIISGIKFKPAIGSTKKEAKNNAAKLAMDK 174


                 ..
gi 21245124  162 LL 163
Cdd:PHA03103 175 IL 176
 
Name Accession Description Interval E-value
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
204-575 3.02e-132

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


Pssm-ID: 214718  Cd Length: 374  Bit Score: 390.59  E-value: 3.02e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    204 IQYAKISQIVKERFNQLISNRSEYLKYSSSLAAFIIERA--GQHEVVAIGTGEYNYSQD-IKPDGRVLHDTHAVVTARRS 280
Cdd:smart00552   1 DTGDEISQLVLEKFGSLPKIGKPGLREWTILAGVVMTNGmdNEKQVVSLGTGTKCISGEkLSPNGLVLNDCHAEILARRG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    281 LLRYFYRQLLLFYSKNpammEKSIFCTEPTSNLLTLKQNINICLYMNQLPKGSAQIKSQLRLNPHSISAFEANEELCLHV 360
Cdd:smart00552  81 FLRFLYSELQLFNSSS----EDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKNDDSKHPVRKNIKRSK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    361 ----------AVEGKIYLTVYCpKDGV---NRISSMSSSDKLTRWEVLGVQGALLSHFIQPVYISSILIGDgNCSDTRGL 427
Cdd:smart00552 157 lrtkieigegTVPVRSSDIVQT-WDGIgdgERLLSMSCSDKIARWNVLGVQGALLSHFIEPIYLSSIVLGK-SLYSAEHL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124    428 EIAIKQRVDDAltSKLPMFYLVNRPHISLVPSAYPLQMNLEYKFLSLNWAQGDVSLEIVDGLSGKitesspFKSGMSMAS 507
Cdd:smart00552 235 ERALYGRLDPL--DGLPTPFRVNRPLISLVSVADFQRQTAKSPNFSVNWSQGDESLEILNGLTGK------TQKSLGSPS 306

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21245124    508 RLCKAAMLSRFNLLAKEAKKELLEAGTYHAAKCMSASYQEAKCKLKSYLQQHGYGSWIVKSPCIEQFN 575
Cdd:smart00552 307 RLCKKALFRLFQKLCSKLKRDDLLHISYAEAKEAASEYQEAKQLLFEALNKAGLGSWIKKPPEQDQFK 374
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
 249-568 2.20e-121

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: 359.18  E-value: 2.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124   249 AIGTGEYNYSQD-IKPDGRVLHDTHAVVTARRSLLRYFYRQLLLFYSKNPammEKSIFCTEPTSNLLTLKQNINICLYMN 327
Cdd:pfam02137   1 ALGTGTKCIGGSkLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNP---SKSIFEPNPDSGKLRLKPGISFHLYIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124   328 QLPKGSAQIKSQLRLNPHSISA---FEANEELCLHVAVEGKIYLTVYCP---KDGVN---RISSMSSSDKLTRWEVLGVQ 398
Cdd:pfam02137  78 QTPCGDARIFSPLELEPESSPAhpvRRFRGQLRLKVETGAKTIPVESSEdqtWDGVKpgrRTLSMSCSDKLARWNVLGVQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124   399 GALLSHFIQPVYISSILIGdGNCSDTRGLEIAIKQRVDDALTSkLPMFYLVNRPHISLVPsayplqmnleykflslnwaq 478
Cdd:pfam02137 158 GALLSHFIEPIYLSSITVG-GSLYDTEHLERAIYQRLDGVLDS-LPPPYRVNKPLIGQVA-------------------- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124   479 gdvsleivdglsgkitesspfksgmsmaSRLCKAAMLSRFNLLAKEAKKELLEAG-TYHAAKCMSASYQEAKCKLKSYLQ 557
Cdd:pfam02137 216 ----------------------------SRLCKAALFSRFLKLLSELSREDLLAPlTYHEAKAAAKDYQEAKQQLKSLLR 267

                         330
                  ....*....|.
gi 21245124   558 QHGYGSWIVKS 568
Cdd:pfam02137 268 QQGLGSWIRKP 278
DSRM_ADAD1 cd19905
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) ...
 95-163 6.53e-38

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: 133.93  E-value: 6.53e-38
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21245124  95 INPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELL 163
Cdd:cd19905   1 KNPVSALHEYAQMTRLKLSFKETVTTGNVAGPYFAFCAVVDGIEYPTGVGKTKKEAKANAAKIALDELL 69
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 95-162 4.17e-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: 4.17e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21245124  95 INPVSALHQFAQMQRVQLDLKEtVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDEL 162
Cdd:cd19875   1 KNPVSALNEYCQKRGLSLEFVD-VSVGPDHCPGFTASATIDGIVFASATGTSKKEAKRAAAKLALKKL 67
DSRM smart00358
Double-stranded RNA binding motif;
97-162 1.24e-15

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 71.53  E-value: 1.24e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21245124     97 PVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDEL 162
Cdd:smart00358   1 PKSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 97-162 2.44e-13

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: 64.94  E-value: 2.44e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21245124    97 PVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDEL 162
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
 96-162 1.00e-11

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: 60.48  E-value: 1.00e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21245124  96 NPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDEL 162
Cdd:cd19903   2 NYMGKLNEYCQKQKVVLDYVEVPTSGPSHDPRFTFQVVIDGKEYPEGEGKSKKEAKQAAAKLALEIL 68
DSRM_DRADA cd19902
double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) ...
 96-164 2.11e-10

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: 56.91  E-value: 2.11e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21245124  96 NPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELLQ 164
Cdd:cd19902   2 NPVSALMEYAQSRGVTAEIEVLSQSGPPHNPRFKAAVFVGGRRFPSVEASSKKDAKQEAADLALRALIA 70
PHA03103 PHA03103
double-strand RNA-binding protein; Provisional
 82-163 2.71e-10

double-strand RNA-binding protein; Provisional


Pssm-ID: 222987 [Multi-domain]  Cd Length: 183  Bit Score: 59.77  E-value: 2.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124   82 IPKEFIMKYKrgEINPVSALHQFAQMQRVQLDLKETvTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDE 161
Cdd:PHA03103  98 IPYKKIISWK--DKNPCTVINEYCQITSRDWSINIT-SSGPSHSPTFTASVIISGIKFKPAIGSTKKEAKNNAAKLAMDK 174


                 ..
gi 21245124  162 LL 163
Cdd:PHA03103 175 IL 176
DSRM_DGCR8_rpt1 cd19867
first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
 96-163 2.47e-08

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: 51.18  E-value: 2.47e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21245124  96 NPVSALHQFAQMQ-RVQLDLKETVTTGNVMGpyfaFCAVV--DGIQYKTGLGQNKKESRSNAAKLALDELL 163
Cdd:cd19867   7 SPVCILHEYCQRVlKVQPEYNFTETENAATP----FSAEVfiNGVEYGSGEASSKKLAKQKAARATLEILI 73
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 95-162 4.74e-07

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: 47.39  E-value: 4.74e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21245124  95 INPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDEL 162
Cdd:cd20314   1 GNYVSLLNEYCQKERLTVKYEEEKRSGPTHKPRFFCKYIIDGKEYPEGEGKSKKEAKQAAARLAYEEL 68
DSRM_DRADA_rpt1 cd19913
first double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 96-164 1.17e-05

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: 43.32  E-value: 1.17e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21245124  96 NPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELLQ 164
Cdd:cd19913   2 NPVSGLMEYAQFLGQTCEFLLLEQSGPSHDPRFKFQAVIDGRRFPPAEASSKKVAKKDAAAIALKILLR 70
DSRM_RED2_rpt1 cd19896
first double-stranded RNA binding motif of RNA-editing deaminase 2 (RED2) and similar proteins; ...
 95-165 8.63e-05

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: 41.23  E-value: 8.63e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21245124  95 INPVSALHQFAQMqRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKtGLGQNKKESRSNAAKLALDELLQL 165
Cdd:cd19896   3 VTPKNALVQLNEL-KPGLQYRMVSQTGPVHAPVFAVAVEVNGLTFE-GTGPTKKKAKMRAAEMALKSFVQF 71
DSRM_AtDRB-like cd19878
double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins ...
 99-162 1.17e-04

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: 40.58  E-value: 1.17e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21245124  99 SALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDEL 162
Cdd:cd19878   3 NLLQEYAQKKKIPLPKYESAKSGPSHQPTFVSTVIVLGVRFSSEGAKNKKQAEQSAAKVALKEL 66
DSRM_STRBP_RED-like_rpt1 cd19865
first double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This ...
 96-159 1.69e-04

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: 40.02  E-value: 1.69e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21245124  96 NPVSALHQFaqmqRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKtGLGQNKKESRSNAAKLAL 159
Cdd:cd19865   2 NALMQLNEL----RPGLQYKLTSQTGPVHAPVFTMSVEVNGQTFE-GTGRSKKKAKLEAAEKAL 60
DSRM_EIF2AK2_rpt2 cd19904
second double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
 96-163 3.94e-04

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: 39.03  E-value: 3.94e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21245124  96 NPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELL 163
Cdd:cd19904   2 NYISLLNQYAQKKRLTVNYEQCASTGVPGPPRFSCKCKIGQKEYGIGTGSTKQEAKQAAAKEAYEQLL 69
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 116-159 4.65e-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: 38.42  E-value: 4.65e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 21245124 116 ETVTTGNVMGPYFAFCAVVDGIQYkTGLGQNKKESRSNAAKLAL 159
Cdd:cd00048  15 ETVEEGGPHNPRFTCTVTVNGQTF-EGEGKSKKEAKQAAAEKAL 57
DSRM_PRKRA-like_rpt1 cd19862
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
 96-165 1.27e-03

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: 37.62  E-value: 1.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21245124  96 NPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQyKTGLGQNKKESRSNAAKLALDELLQL 165
Cdd:cd19862   2 TPISVLQELCAKRGITPKYELISSEGAVHEPTFTFRVTVGDIT-ATGSGTSKKKAKHAAAENALEQLKGS 70
PHA02701 PHA02701
ORF020 dsRNA-binding PKR inhibitor; Provisional
 87-163 2.49e-03

ORF020 dsRNA-binding PKR inhibitor; Provisional


Pssm-ID: 177482 [Multi-domain]  Cd Length: 183  Bit Score: 39.16  E-value: 2.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21245124   87 IMKYKrgEINPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELL 163
Cdd:PHA02701 102 VMRLK--TLNPVSAVNEFCMRTHRPLEFCETRSGGHDHCPLFTCTIVVSGKVVATASGCSKKLARHAACADALTILI 176
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
 96-162 4.56e-03

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: 36.10  E-value: 4.56e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21245124  96 NPVSALHQFAQMQRVQLDLKETVT-TGNVMGPYFAFCAVVDGIQYKTGLGQ-NKKESRSNAAKLALDEL 162
Cdd:cd19870   3 HPVSALMELCNKRKWGPPEFRLVEeSGPPHRKHFLFKVVVNGVEYQPSVASgNKKDAKAQAATVALQAL 71
 
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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