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Conserved domains on  [gi|1331881609|gb|PNJ29746|]
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ADAD2 isoform 6, partial [Pongo abelii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DSRM_ADAD2 cd19906
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 2 (ADAD2) ...
 36-103 3.00e-26

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: 97.61  E-value: 3.00e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331881609  36 PASQAVSLLTEYAASLGIFLLFREDQPPGPCFPFSVSAEL------DGVVCPAGTANSKTEAKQQAALSALCYI 103
Cdd:cd19906     1 PPKTPLSLLHEYAAKLSLEVEFRETQEEGPVGPFTVSARLrsrvqrTGVVCGAGTARAKKDAKQVAAAAALEKL 74
A_deamin super family cl02661
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
 169-265 1.85e-23

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.


The actual alignment was detected with superfamily member pfam02137:

Pssm-ID: 470647  Cd Length: 278  Bit Score: 96.09  E-value: 1.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331881609 169 ALGTGSSCCAG-WLEFSGQQLHDCHGLVIARRALLRFLFRQLLLATQGGPkgkEQSVLAPQPGPGpPFTLKPRVFLHLYI 247
Cdd:pfam02137   1 ALGTGTKCIGGsKLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNP---SKSIFEPNPDSG-KLRLKPGISFHLYI 76

                          90
                  ....*....|....*...
gi 1331881609 248 SNTPKGAARdIYLPPTSE 265
Cdd:pfam02137  77 SQTPCGDAR-IFSPLELE 93
 
Name Accession Description Interval E-value
DSRM_ADAD2 cd19906
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 2 (ADAD2) ...
 36-103 3.00e-26

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: 97.61  E-value: 3.00e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331881609  36 PASQAVSLLTEYAASLGIFLLFREDQPPGPCFPFSVSAEL------DGVVCPAGTANSKTEAKQQAALSALCYI 103
Cdd:cd19906     1 PPKTPLSLLHEYAAKLSLEVEFRETQEEGPVGPFTVSARLrsrvqrTGVVCGAGTARAKKDAKQVAAAAALEKL 74
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
 169-265 1.85e-23

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: 96.09  E-value: 1.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331881609 169 ALGTGSSCCAG-WLEFSGQQLHDCHGLVIARRALLRFLFRQLLLATQGGPkgkEQSVLAPQPGPGpPFTLKPRVFLHLYI 247
Cdd:pfam02137   1 ALGTGTKCIGGsKLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNP---SKSIFEPNPDSG-KLRLKPGISFHLYI 76

                          90
                  ....*....|....*...
gi 1331881609 248 SNTPKGAARdIYLPPTSE 265
Cdd:pfam02137  77 SQTPCGDAR-IFSPLELE 93
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
121-258 2.92e-11

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


Pssm-ID: 214718  Cd Length: 374  Bit Score: 62.78  E-value: 2.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331881609  121 AALVSAGFDLLLDERSPYWACKGTVAGFILEREIPGArghvkeiYKLVALGTGSSCCAG-WLEFSGQQLHDCHGLVIARR 199
Cdd:smart00552   7 SQLVLEKFGSLPKIGKPGLREWTILAGVVMTNGMDNE-------KQVVSLGTGTKCISGeKLSPNGLVLNDCHAEILARR 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331881609  200 ALLRF-LFRQLLLATQggpkgKEQSVLAPQPGpGPPFTLKPRVFLHLYISNTPKGAARDI 258
Cdd:smart00552  80 GFLRFlYSELQLFNSS-----SEDSIFEKNKE-GGKYKLKSNVLFHLYISTLPCGDASIF 133
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 40-103 7.24e-09

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: 51.08  E-value: 7.24e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331881609  40 AVSLLTEYAASLGIFLLFREDQPPGP--CFPFSVSAELDGVVCPAGTANSKTEAKQQAALSALCYI 103
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEYVSEEGPphSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM smart00358
Double-stranded RNA binding motif;
40-100 1.17e-05

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 42.25  E-value: 1.17e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331881609   40 AVSLLTEYAASLGI---FLLFREDQPP-GPCFpfSVSAELDGVVCPAGTANSKTEAKQQAALSAL 100
Cdd:smart00358   1 PKSLLQELAQKRKLppeYELVKEEGPDhAPRF--TVTVKVGGKRTGEGEGSSKKEAKQRAAEAAL 63
 
Name Accession Description Interval E-value
DSRM_ADAD2 cd19906
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 2 (ADAD2) ...
 36-103 3.00e-26

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: 97.61  E-value: 3.00e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331881609  36 PASQAVSLLTEYAASLGIFLLFREDQPPGPCFPFSVSAEL------DGVVCPAGTANSKTEAKQQAALSALCYI 103
Cdd:cd19906     1 PPKTPLSLLHEYAAKLSLEVEFRETQEEGPVGPFTVSARLrsrvqrTGVVCGAGTARAKKDAKQVAAAAALEKL 74
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
 169-265 1.85e-23

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: 96.09  E-value: 1.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331881609 169 ALGTGSSCCAG-WLEFSGQQLHDCHGLVIARRALLRFLFRQLLLATQGGPkgkEQSVLAPQPGPGpPFTLKPRVFLHLYI 247
Cdd:pfam02137   1 ALGTGTKCIGGsKLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNP---SKSIFEPNPDSG-KLRLKPGISFHLYI 76

                          90
                  ....*....|....*...
gi 1331881609 248 SNTPKGAARdIYLPPTSE 265
Cdd:pfam02137  77 SQTPCGDAR-IFSPLELE 93
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 38-103 4.39e-19

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: 78.85  E-value: 4.39e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331881609  38 SQAVSLLTEYAASLGIFLLFREDQP-PGPCFPFSVSAELDGVVCPAGTANSKTEAKQQAALSALCYI 103
Cdd:cd19875     1 KNPVSALNEYCQKRGLSLEFVDVSVgPDHCPGFTASATIDGIVFASATGTSKKEAKRAAAKLALKKL 67
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
121-258 2.92e-11

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


Pssm-ID: 214718  Cd Length: 374  Bit Score: 62.78  E-value: 2.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331881609  121 AALVSAGFDLLLDERSPYWACKGTVAGFILEREIPGArghvkeiYKLVALGTGSSCCAG-WLEFSGQQLHDCHGLVIARR 199
Cdd:smart00552   7 SQLVLEKFGSLPKIGKPGLREWTILAGVVMTNGMDNE-------KQVVSLGTGTKCISGeKLSPNGLVLNDCHAEILARR 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331881609  200 ALLRF-LFRQLLLATQggpkgKEQSVLAPQPGpGPPFTLKPRVFLHLYISNTPKGAARDI 258
Cdd:smart00552  80 GFLRFlYSELQLFNSS-----SEDSIFEKNKE-GGKYKLKSNVLFHLYISTLPCGDASIF 133
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 40-103 7.24e-09

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: 51.08  E-value: 7.24e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331881609  40 AVSLLTEYAASLGIFLLFREDQPPGP--CFPFSVSAELDGVVCPAGTANSKTEAKQQAALSALCYI 103
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEYVSEEGPphSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM_ADAD1 cd19905
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) ...
 39-100 6.10e-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: 43.03  E-value: 6.10e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331881609  39 QAVSLLTEYAASLGIFLLFRED--QPPGPCFPFSVSAELDGVVCPAGTANSKTEAKQQAALSAL 100
Cdd:cd19905     2 NPVSALHEYAQMTRLKLSFKETvtTGNVAGPYFAFCAVVDGIEYPTGVGKTKKEAKANAAKIAL 65
DSRM smart00358
Double-stranded RNA binding motif;
40-100 1.17e-05

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 42.25  E-value: 1.17e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331881609   40 AVSLLTEYAASLGI---FLLFREDQPP-GPCFpfSVSAELDGVVCPAGTANSKTEAKQQAALSAL 100
Cdd:smart00358   1 PKSLLQELAQKRKLppeYELVKEEGPDhAPRF--TVTVKVGGKRTGEGEGSSKKEAKQRAAEAAL 63
DSRM_PRKRA-like_rpt1 cd19862
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
 41-100 3.33e-05

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: 41.09  E-value: 3.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331881609  41 VSLLTEYAASLGIF----LLFREDQPPGPCFPFSVSAelDGVVCpAGTANSKTEAKQQAALSAL 100
Cdd:cd19862     4 ISVLQELCAKRGITpkyeLISSEGAVHEPTFTFRVTV--GDITA-TGSGTSKKKAKHAAAENAL 64
DSRM_DGCR8_rpt1 cd19867
first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
 68-100 1.01e-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: 39.62  E-value: 1.01e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1331881609  68 PFSVSAELDGVVCPAGTANSKTEAKQQAALSAL 100
Cdd:cd19867    37 PFSAEVFINGVEYGSGEASSKKLAKQKAARATL 69
DSRM_DRADA_rpt3 cd19915
third double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 40-100 3.61e-04

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: 38.00  E-value: 3.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331881609  40 AVSLLTEYAASLGIFLLFREDQPPGPCF--PFSVSAELDGVVCPAGTANSKTEAKQQAALSAL 100
Cdd:cd19915     3 PVSGLLEYARSKGFAAEFKLVDQSGPPHepKFVYQAKVGGRWFPAVCAHNKKQGKQEAADAAL 65
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 69-100 9.68e-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: 36.49  E-value: 9.68e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1331881609  69 FSVSAELDGVVCpAGTANSKTEAKQQAALSAL 100
Cdd:cd00048    27 FTCTVTVNGQTF-EGEGKSKKEAKQAAAEKAL 57
DSRM_DRADA cd19902
double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) ...
 40-100 1.22e-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: 1.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331881609  40 AVSLLTEYAASLGIFLLFREDQPPGPcfP----FSVSAELDGVVCPAGTANSKTEAKQQAALSAL 100
Cdd:cd19902     3 PVSALMEYAQSRGVTAEIEVLSQSGP--PhnprFKAAVFVGGRRFPSVEASSKKDAKQEAADLAL 65
DSRM_DRADA_rpt1 cd19913
first double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 41-100 1.83e-03

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: 36.00  E-value: 1.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331881609  41 VSLLTEYAASLGI---FLLFREDQPP-GPCFPFSVSaeLDGVVCPAGTANSKTEAKQQAALSAL 100
Cdd:cd19913     4 VSGLMEYAQFLGQtceFLLLEQSGPShDPRFKFQAV--IDGRRFPPAEASSKKVAKKDAAAIAL 65
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 41-100 2.77e-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: 35.45  E-value: 2.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331881609  41 VSLLTEYAASLGIFLLFREDQPPGPCFP--FSVSAELDGVVCPAGTANSKTEAKQQAALSAL 100
Cdd:cd20314     4 VSLLNEYCQKERLTVKYEEEKRSGPTHKprFFCKYIIDGKEYPEGEGKSKKEAKQAAARLAY 65
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
 41-100 4.01e-03

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: 35.06  E-value: 4.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331881609  41 VSLLTEYAASLGIFLLFREDQPPGPcfP----FSVSAELDGVVCPAGTANSKTEAKQQAALSAL 100
Cdd:cd19903     4 MGKLNEYCQKQKVVLDYVEVPTSGP--ShdprFTFQVVIDGKEYPEGEGKSKKEAKQAAAKLAL 65
DSRM_PRKRA-like_rpt3 cd19864
third double-stranded RNA binding motif of PRKRA, TARBP2 and similar proteins; The family ...
 78-104 5.11e-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: 34.89  E-value: 5.11e-03
                          10        20
                  ....*....|....*....|....*..
gi 1331881609  78 VVCPaGTANSKTEAKQQAALSALCYIR 104
Cdd:cd19864    44 TVCH-GSGASLEEAKEEAARNALEYLK 69
 
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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