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Conserved domains on  [gi|170172601|ref|NP_001116221|]
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microprocessor complex subunit DGCR8 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DSRM_DGCR8_rpt1 cd19867
first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
 514-587 4.10e-38

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: 136.31  E-value: 4.10e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170172601 514 INPNGKSEVCILHEYMQRVLKVRPVYNFFECENPSEPFGASVIIDGVTYGTGTASSKKLAKNKAARATLEILIP 587
Cdd:cd19867    1 INPDGKSPVCILHEYCQRVLKVQPEYNFTETENAATPFSAEVFINGVEYGSGEASSKKLAKQKAARATLEILIP 74
DSRM_DGCR8_rpt2 cd19868
second double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
 627-695 9.39e-36

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


:

Pssm-ID: 380697  Cd Length: 69  Bit Score: 129.32  E-value: 9.39e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170172601 627 LSPYQILHECLKRNHGMGDTSIKFEVIPGKNQKSEYVMTCGKHTVRGWCKNKRVGKQLASQKILQMLHP 695
Cdd:cd19868    1 PSPYQILQECLKRNHGMGDTELKFEVINDKHQKHEYTMTVGKHTVTVICKNKKEGKQLAAQAILKKLHP 69
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 293-323 2.94e-06

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


:

Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 44.13  E-value: 2.94e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 170172601   293 PLPDGWIMTFHNSGIPVYLHRETRVVTWSRP 323
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
 
Name Accession Description Interval E-value
DSRM_DGCR8_rpt1 cd19867
first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
 514-587 4.10e-38

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: 136.31  E-value: 4.10e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170172601 514 INPNGKSEVCILHEYMQRVLKVRPVYNFFECENPSEPFGASVIIDGVTYGTGTASSKKLAKNKAARATLEILIP 587
Cdd:cd19867    1 INPDGKSPVCILHEYCQRVLKVQPEYNFTETENAATPFSAEVFINGVEYGSGEASSKKLAKQKAARATLEILIP 74
DSRM_DGCR8_rpt2 cd19868
second double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
 627-695 9.39e-36

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


Pssm-ID: 380697  Cd Length: 69  Bit Score: 129.32  E-value: 9.39e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170172601 627 LSPYQILHECLKRNHGMGDTSIKFEVIPGKNQKSEYVMTCGKHTVRGWCKNKRVGKQLASQKILQMLHP 695
Cdd:cd19868    1 PSPYQILQECLKRNHGMGDTELKFEVINDKHQKHEYTMTVGKHTVTVICKNKKEGKQLAAQAILKKLHP 69
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 522-585 2.42e-14

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 68.03  E-value: 2.42e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170172601  522 VCILHEYMQRvLKVRPVYNFFECENPSEP--FGASVIIDGVTYGTGTASSKKLAKNKAARATLEIL 585
Cdd:pfam00035   2 KSLLQEYAQK-NGKPPPYEYVSEEGPPHSpkFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM smart00358
Double-stranded RNA binding motif;
522-585 4.83e-12

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 61.51  E-value: 4.83e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170172601   522 VCILHEYMQRvLKVRPVYNFFECENPSEP--FGASVIIDGVTYGTGTASSKKLAKNKAARATLEIL 585
Cdd:smart00358   2 KSLLQELAQK-RKLPPEYELVKEEGPDHAprFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 629-693 1.23e-07

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: 49.15  E-value: 1.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170172601  629 PYQILHECLKRNHGMGDTSIKFEVIPGKNQKseYVMTC---GKHTVRGWCKNKRVGKQLASQKILQML 693
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPK--FTVTVkvdGKLYGSGTGSSKKEAEQLAAEKALEKL 66
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
505-585 1.20e-06

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 50.10  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172601 505 DAPTKKEFVINPngKSEvciLHEYMQRVLKVRPVYNFFECENPS-EP-FGASVIIDGVTYGTGTASSKKLAKNKAARATL 582
Cdd:COG0571  148 EEIAPGGAGKDY--KTA---LQEWLQARGLPLPEYEVVEEEGPDhAKtFTVEVLVGGKVLGEGTGRSKKEAEQAAAKAAL 222


                 ...
gi 170172601 583 EIL 585
Cdd:COG0571  223 EKL 225
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 293-323 2.94e-06

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 44.13  E-value: 2.94e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 170172601   293 PLPDGWIMTFHNSGIPVYLHRETRVVTWSRP 323
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
PHA03103 PHA03103
double-strand RNA-binding protein; Provisional
 507-586 4.03e-05

double-strand RNA-binding protein; Provisional


Pssm-ID: 222987 [Multi-domain]  Cd Length: 183  Bit Score: 45.14  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172601 507 PTKKefVINPNGKSEVCILHEYMQrvLKVRPVY-NFFECENPSEP-FGASVIIDGVTYGTGTASSKKLAKNKAARATLEI 584
Cdd:PHA03103  99 PYKK--IISWKDKNPCTVINEYCQ--ITSRDWSiNITSSGPSHSPtFTASVIISGIKFKPAIGSTKKEAKNNAAKLAMDK 174


                 ..
gi 170172601 585 LI 586
Cdd:PHA03103 175 IL 176
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 294-323 4.21e-05

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 40.95  E-value: 4.21e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 170172601  294 LPDGWIMTFHNSGIPVYLHRETRVVTWSRP 323
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 295-323 1.34e-03

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 36.74  E-value: 1.34e-03
                         10        20
                 ....*....|....*....|....*....
gi 170172601 295 PDGWIMTFHNSGIPVYLHRETRVVTWSRP 323
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
 
Name Accession Description Interval E-value
DSRM_DGCR8_rpt1 cd19867
first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
 514-587 4.10e-38

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: 136.31  E-value: 4.10e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170172601 514 INPNGKSEVCILHEYMQRVLKVRPVYNFFECENPSEPFGASVIIDGVTYGTGTASSKKLAKNKAARATLEILIP 587
Cdd:cd19867    1 INPDGKSPVCILHEYCQRVLKVQPEYNFTETENAATPFSAEVFINGVEYGSGEASSKKLAKQKAARATLEILIP 74
DSRM_DGCR8_rpt2 cd19868
second double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
 627-695 9.39e-36

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


Pssm-ID: 380697  Cd Length: 69  Bit Score: 129.32  E-value: 9.39e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170172601 627 LSPYQILHECLKRNHGMGDTSIKFEVIPGKNQKSEYVMTCGKHTVRGWCKNKRVGKQLASQKILQMLHP 695
Cdd:cd19868    1 PSPYQILQECLKRNHGMGDTELKFEVINDKHQKHEYTMTVGKHTVTVICKNKKEGKQLAAQAILKKLHP 69
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 522-585 2.42e-14

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 68.03  E-value: 2.42e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170172601  522 VCILHEYMQRvLKVRPVYNFFECENPSEP--FGASVIIDGVTYGTGTASSKKLAKNKAARATLEIL 585
Cdd:pfam00035   2 KSLLQEYAQK-NGKPPPYEYVSEEGPPHSpkFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM smart00358
Double-stranded RNA binding motif;
522-585 4.83e-12

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 61.51  E-value: 4.83e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170172601   522 VCILHEYMQRvLKVRPVYNFFECENPSEP--FGASVIIDGVTYGTGTASSKKLAKNKAARATLEIL 585
Cdd:smart00358   2 KSLLQELAQK-RKLPPEYELVKEEGPDHAprFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSL 66
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 519-585 5.26e-12

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: 61.51  E-value: 5.26e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170172601 519 KSEVCILHEYMQRvLKVRPVYNFFECENPSEP-FGASVIIDGVTYGTGTASSKKLAKNKAARATLEIL 585
Cdd:cd19875    1 KNPVSALNEYCQK-RGLSLEFVDVSVGPDHCPgFTASATIDGIVFASATGTSKKEAKRAAAKLALKKL 67
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 526-582 7.07e-11

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: 58.07  E-value: 7.07e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 170172601 526 HEYMQRVLKVRPVYNFFECENPSEP-FGASVIIDGVTYgTGTASSKKLAKNKAARATL 582
Cdd:cd00048    1 NELCQKNKWPPPEYETVEEGGPHNPrFTCTVTVNGQTF-EGEGKSKKEAKQAAAEKAL 57
DSRM_PRKRA-like_rpt1 cd19862
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
 519-585 1.28e-08

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


Pssm-ID: 380691 [Multi-domain]  Cd Length: 70  Bit Score: 52.26  E-value: 1.28e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170172601 519 KSEVCILHEYMQRvLKVRPVYNFFECENPS-EP-FGASVIIDGVTyGTGTASSKKLAKNKAARATLEIL 585
Cdd:cd19862    1 KTPISVLQELCAK-RGITPKYELISSEGAVhEPtFTFRVTVGDIT-ATGSGTSKKKAKHAAAENALEQL 67
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 629-693 1.23e-07

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: 49.15  E-value: 1.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170172601  629 PYQILHECLKRNHGMGDTSIKFEVIPGKNQKseYVMTC---GKHTVRGWCKNKRVGKQLASQKILQML 693
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPK--FTVTVkvdGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
 524-585 6.83e-07

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: 47.10  E-value: 6.83e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170172601 524 ILHEYMQRVLKVRPVYNFFECENPS-EP-FGASVIIDGVTYGTGTASSKKLAKNKAARATLEIL 585
Cdd:cd10845    6 ALQEYLQKRGLPLPEYELVEEEGPDhNKtFTVEVKVNGKVIGEGTGRSKKEAEQAAAKAALEKL 69
DSRM_ADAD2 cd19906
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 2 (ADAD2) ...
 518-585 7.29e-07

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: 47.15  E-value: 7.29e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170172601 518 GKSEVCILHEYMQRvLKVRPVYNFFECENPSEPFGASVII------DGVTYGTGTASSKKLAKNKAARATLEIL 585
Cdd:cd19906    2 PKTPLSLLHEYAAK-LSLEVEFRETQEEGPVGPFTVSARLrsrvqrTGVVCGAGTARAKKDAKQVAAAAALEKL 74
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
505-585 1.20e-06

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 50.10  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172601 505 DAPTKKEFVINPngKSEvciLHEYMQRVLKVRPVYNFFECENPS-EP-FGASVIIDGVTYGTGTASSKKLAKNKAARATL 582
Cdd:COG0571  148 EEIAPGGAGKDY--KTA---LQEWLQARGLPLPEYEVVEEEGPDhAKtFTVEVLVGGKVLGEGTGRSKKEAEQAAAKAAL 222


                 ...
gi 170172601 583 EIL 585
Cdd:COG0571  223 EKL 225
DSRM_ADAD1 cd19905
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) ...
 514-586 1.27e-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: 46.49  E-value: 1.27e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170172601 514 INPngkseVCILHEYMQRVlkvRPVYNFFECEN----PSEPFGASVIIDGVTYGTGTASSKKLAKNKAARATLEILI 586
Cdd:cd19905    1 KNP-----VSALHEYAQMT---RLKLSFKETVTtgnvAGPYFAFCAVVDGIEYPTGVGKTKKEAKANAAKIALDELL 69
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 522-585 2.15e-06

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: 45.85  E-value: 2.15e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170172601 522 VCILHEYMQrvlKVRPVYNFFECENPSEP----FGASVIIDGVTYGTGTASSKKLAKNKAARATLEIL 585
Cdd:cd20314    4 VSLLNEYCQ---KERLTVKYEEEKRSGPThkprFFCKYIIDGKEYPEGEGKSKKEAKQAAARLAYEEL 68
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 293-323 2.94e-06

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 44.13  E-value: 2.94e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 170172601   293 PLPDGWIMTFHNSGIPVYLHRETRVVTWSRP 323
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
 525-585 4.82e-06

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: 44.69  E-value: 4.82e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170172601 525 LHEYMQrvlKVRPVYNFFECENPSEP----FGASVIIDGVTYGTGTASSKKLAKNKAARATLEIL 585
Cdd:cd19903    7 LNEYCQ---KQKVVLDYVEVPTSGPShdprFTFQVVIDGKEYPEGEGKSKKEAKQAAAKLALEIL 68
DSRM_PRKRA_rpt1 cd19889
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
 518-585 2.62e-05

first double-stranded RNA binding motif of protein activator of the interferon-induced protein kinase (PRKRA) and similar proteins; PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. PRKRA contains three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380718 [Multi-domain]  Cd Length: 71  Bit Score: 42.98  E-value: 2.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170172601 518 GKSEVCILHEYMQRVlKVRPVYNFFECE----NPSepFGASVIIDGVTYgTGTASSKKLAKNKAARATLEIL 585
Cdd:cd19889    1 GKTPIQLLHEYGTKT-GNIPVYELEKSEgqahLPS--FTFRVTVGDITC-TGEGTSKKLAKHRAAEAALNIL 68
PHA03103 PHA03103
double-strand RNA-binding protein; Provisional
 507-586 4.03e-05

double-strand RNA-binding protein; Provisional


Pssm-ID: 222987 [Multi-domain]  Cd Length: 183  Bit Score: 45.14  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172601 507 PTKKefVINPNGKSEVCILHEYMQrvLKVRPVY-NFFECENPSEP-FGASVIIDGVTYGTGTASSKKLAKNKAARATLEI 584
Cdd:PHA03103  99 PYKK--IISWKDKNPCTVINEYCQ--ITSRDWSiNITSSGPSHSPtFTASVIISGIKFKPAIGSTKKEAKNNAAKLAMDK 174


                 ..
gi 170172601 585 LI 586
Cdd:PHA03103 175 IL 176
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 294-323 4.21e-05

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 40.95  E-value: 4.21e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 170172601  294 LPDGWIMTFHNSGIPVYLHRETRVVTWSRP 323
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
DSRM_TARBP2_rpt1 cd19890
first double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar ...
 518-585 1.96e-04

first double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar proteins; TARBP2 (also known as TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)), participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. TARBP2 contains three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380719  Cd Length: 72  Bit Score: 40.50  E-value: 1.96e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170172601 518 GKSEVCILHEYMQRVLKVrPVYNFFECE----NPSEPFGASViidGVTYGTGTASSKKLAKNKAARATLEIL 585
Cdd:cd19890    2 GKTPISLLQEYGTRIGKT-PVYDLLKAEgqahQPNFTFRVTV---GDISCTGQGPSKKAAKHKAAEVALKLL 69
DSRM_DHX9_rpt1 cd19854
first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; ...
 534-590 2.83e-04

first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; DHX9 (EC 3.6.4.13; also known as ATP-dependent RNA helicase A, DExH-box helicase 9 (DDX9), Leukophysin (LKP), nuclear DNA helicase II (NDH II), NDH2, or RNA helicase A) is a multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation, and RNA-mediated gene silencing. It contains two double-stranded RNA binding motifs (DSRMs) at the N-terminal region. This model corresponds to the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380683  Cd Length: 69  Bit Score: 39.95  E-value: 2.83e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 170172601 534 KVRPVYNFFECENP-SEPFGASVIIDGVTY-GTGTASSKKLAKNKAARatleilipDFV 590
Cdd:cd19854   14 KLTPEYDIKEAGNKhRQRFKCEVRVEGFDYvGTGNATNKKDAQTNAAR--------DFL 64
DSRM_DRADA cd19902
double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) ...
 519-586 3.03e-04

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: 39.58  E-value: 3.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172601 519 KSEVCILHEYMQrVLKVRPVYNFFECENPS-EP-FGASVIIDGVTYGTGTASSKKLAKNKAARATLEILI 586
Cdd:cd19902    1 KNPVSALMEYAQ-SRGVTAEIEVLSQSGPPhNPrFKAAVFVGGRRFPSVEASSKKDAKQEAADLALRALI 69
DSRM_RNT1p-like cd19876
double-stranded RNA binding motif of Saccharomyces cerevisiae ribonuclease 3 (RNT1p) and ...
 533-583 4.97e-04

double-stranded RNA binding motif of Saccharomyces cerevisiae ribonuclease 3 (RNT1p) and similar proteins; RNT1p (EC 3.1.26.3; also known as ribonuclease III (RNase III)) is a dsRNA-specific nuclease that cleaves eukaryotic pre-ribosomal RNA at the U3 snoRNP-dependent A0 site in the 5'-external transcribed spacer (ETS) and in the 3'-ETS. RNT1p contains 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: 380705  Cd Length: 69  Bit Score: 39.24  E-value: 4.97e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 170172601 533 LKVRPVYNFFECENPSEP-FGASVIIDGVTYGTGTASSKKLAKNKAARATLE 583
Cdd:cd19876   15 ASLKPEYVVVKKEGGNDPnYTVACRINGEVLGTGVGRSIKKAGQRAAMSALS 66
DSRM_RED1_rpt2 cd19898
second double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar ...
 518-582 5.56e-04

second double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins; RED1 (EC 3.5.4.37; also known as double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. It contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the second DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380727  Cd Length: 70  Bit Score: 39.02  E-value: 5.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170172601 518 GKSEVCILHEymqrvlkVRP--VYNFFE--CENPSEPFGASVIIDGVTYgTGTASSKKLAKNKAARATL 582
Cdd:cd19898    2 GKNPVMILNE-------LRPglKYEFVSesGESHAKNFVMSVTVDGQTF-EGSGRNKKLAKARAAQAAL 62
DSRM_STRBP_RED-like_rpt2 cd19866
second double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This ...
 551-585 6.39e-04

second double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3), as well as two RNA-editing deaminases, RED1 and RED2. STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. RED1 (EC 3.5.4.37; also called double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. RED2 (also called double-stranded RNA-specific editase B2, RNA-dependent adenosine deaminase 3, RNA-editing enzyme 2, dsRNA adenosine deaminase B2, ADAR3, or ADARB2) prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. It is capable of binding to dsRNA but also to ssRNA. RED2 lacks editing activity for currently known substrate RNAs. Members of this group contain two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380695  Cd Length: 63  Bit Score: 38.69  E-value: 6.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 170172601 551 FGASVIIDGVTYgTGTASSKKLAKNKAARATLEIL 585
Cdd:cd19866   30 FVMSVTVDGQTF-EGTGRSKKLAKAAAAQAALAKL 63
DSRM_DRADA_rpt1 cd19913
first double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
 519-586 8.97e-04

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: 38.31  E-value: 8.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170172601 519 KSEVCILHEYMQrvlkvrpvYNFFECE-------NPS-EP-FGASVIIDGVTYGTGTASSKKLAKNKAARATLEILI 586
Cdd:cd19913    1 KNPVSGLMEYAQ--------FLGQTCEfllleqsGPShDPrFKFQAVIDGRRFPPAEASSKKVAKKDAAAIALKILL 69
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 295-323 1.34e-03

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 36.74  E-value: 1.34e-03
                         10        20
                 ....*....|....*....|....*....
gi 170172601 295 PDGWIMTFHNSGIPVYLHRETRVVTWSRP 323
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
 518-585 1.93e-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: 37.65  E-value: 1.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170172601 518 GKSEVCILHEYMQRVLKVRPVynfFECENPSEP-----FGASVIIDGVTYGTGTASS-KKLAKNKAARATLEIL 585
Cdd:cd19870    1 GKHPVSALMELCNKRKWGPPE---FRLVEESGPphrkhFLFKVVVNGVEYQPSVASGnKKDAKAQAATVALQAL 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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