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Conserved domains on  [gi|1126170404|ref|XP_019617195|]
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PREDICTED: protein SON-like [Branchiostoma belcheri]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
676-750 1.08e-46

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: 160.14  E-value: 1.08e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126170404 676 GKHPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYQPTIASPNKKHAKAQAATVALQAMGLIP 750
Cdd:cd19870     1 GKHPVSALMELCNKRKWGPPEFRLVEESGPPHRKHFLFKVVVNGVEYQPSVASGNKKDAKAQAATVALQALGLVP 75
G-patch pfam01585
G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in ...
608-649 9.05e-14

G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines.


:

Pssm-ID: 396249 [Multi-domain]  Cd Length: 45  Bit Score: 65.99  E-value: 9.05e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1126170404 608 QGGMGMQLMKKMGWKPGEGLGKGQTGVLEPLTLDVKTDRRGL 649
Cdd:pfam01585   1 TSNIGFKLLQKMGWKEGQGLGKNEQGIAEPIEAKIKKDRRGL 42
RSRP super family cl26279
Arginine/Serine-Rich protein 1; RSRP1 is an eukaryotic protein family. Its function is unknown.
229-428 2.21e-07

Arginine/Serine-Rich protein 1; RSRP1 is an eukaryotic protein family. Its function is unknown.


The actual alignment was detected with superfamily member pfam17069:

Pssm-ID: 293674 [Multi-domain]  Cd Length: 299  Bit Score: 53.24  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 229 GECRSRSLSKDRLKSQEHRSGSGKHSRSRSKSHDRHHKHRHRSSSRERHRHKGSSRHRSRSRHRSRSRQGSRHRSRSRHR 308
Cdd:pfam17069  26 SSSRLSSRSRSRSSSRSSRSHSRSSSRFSSRSRSRPRRSRSRSRSRRRHQRKYRRYSRSYSRSRSRSRRRRYYRRSRYRY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 309 SGSHDRYRHRSRSHEKHRHRSRS------GERYPNRAKERH------HRSRSPNHSRSRTP--TERIDKAKLLEIAKANA 374
Cdd:pfam17069 106 SRRYYRSPSRSRSRSRSRSRGRSyyaiwrGSRYYGFGRTVYpersprWRSRSRTRSRSRTPfrLSEKERMELLEIAKANA 185
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1126170404 375 INQFRAGMIPAHLPIPSMTPEEELAKKSGGKTVEELTKFCKFLSEKEKAGDEDE 428
Cdd:pfam17069 186 AKALGTQNLDLPASLREMEQAKERSRGGVSSSGDKEERVRVDLSEQKTADDEAE 239
 
Name Accession Description Interval E-value
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
676-750 1.08e-46

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: 160.14  E-value: 1.08e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126170404 676 GKHPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYQPTIASPNKKHAKAQAATVALQAMGLIP 750
Cdd:cd19870     1 GKHPVSALMELCNKRKWGPPEFRLVEESGPPHRKHFLFKVVVNGVEYQPSVASGNKKDAKAQAATVALQALGLVP 75
DSRM smart00358
Double-stranded RNA binding motif;
679-747 7.47e-17

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 75.38  E-value: 7.47e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126170404  679 PVSALMEICNKRKWmPPEFVLVHDSGPDHKKNFLFKVRINsEEYQPTIASPNKKHAKAQAATVALQAMG 747
Cdd:smart00358   1 PKSLLQELAQKRKL-PPEYELVKEEGPDHAPRFTVTVKVG-GKRTGEGEGSSKKEAKQRAAEAALRSLK 67
G-patch pfam01585
G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in ...
608-649 9.05e-14

G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines.


Pssm-ID: 396249 [Multi-domain]  Cd Length: 45  Bit Score: 65.99  E-value: 9.05e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1126170404 608 QGGMGMQLMKKMGWKPGEGLGKGQTGVLEPLTLDVKTDRRGL 649
Cdd:pfam01585   1 TSNIGFKLLQKMGWKEGQGLGKNEQGIAEPIEAKIKKDRRGL 42
DND1_DSRM pfam14709
double strand RNA binding domain from DEAD END PROTEIN 1; A C-terminal domain in human dead ...
679-747 4.69e-12

double strand RNA binding domain from DEAD END PROTEIN 1; A C-terminal domain in human dead end protein 1 (DND1_HUMAN) homologous to double strand RNA binding domains (PF00035, PF00333)


Pssm-ID: 405408  Cd Length: 80  Bit Score: 61.97  E-value: 4.69e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126170404 679 PVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEE---------YQPTIASPNKKHAKAQAATVALQAMG 747
Cdd:pfam14709   3 AVSHLEELCQKNKWGSPVYELHSTAGPDGKQLFTYKVVIPGIEtpfpgviwiFMPGKLCSTKEEAKEAAAEQVLEALG 80
G_patch smart00443
glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in ...
606-649 9.28e-12

glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins.


Pssm-ID: 197727 [Multi-domain]  Cd Length: 47  Bit Score: 60.25  E-value: 9.28e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1126170404  606 PVQGGMGMQLMKKMGWKPGEGLGKGQTGVLEPLTLDVKTDRRGL 649
Cdd:smart00443   1 ISTSNIGAKLLRKMGWKEGQGLGKNEQGIVEPISAEIKKDRKGL 44
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
668-747 1.40e-08

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 55.88  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 668 DTTGKDLSGKHPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYqpTIAS-PNKKHAKAQAATVALQAM 746
Cdd:COG0571   148 EEIAPGGAGKDYKTALQEWLQARGLPLPEYEVVEEEGPDHAKTFTVEVLVGGKVL--GEGTgRSKKEAEQAAAKAALEKL 225

                  .
gi 1126170404 747 G 747
Cdd:COG0571   226 G 226
RSRP pfam17069
Arginine/Serine-Rich protein 1; RSRP1 is an eukaryotic protein family. Its function is unknown.
229-428 2.21e-07

Arginine/Serine-Rich protein 1; RSRP1 is an eukaryotic protein family. Its function is unknown.


Pssm-ID: 293674 [Multi-domain]  Cd Length: 299  Bit Score: 53.24  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 229 GECRSRSLSKDRLKSQEHRSGSGKHSRSRSKSHDRHHKHRHRSSSRERHRHKGSSRHRSRSRHRSRSRQGSRHRSRSRHR 308
Cdd:pfam17069  26 SSSRLSSRSRSRSSSRSSRSHSRSSSRFSSRSRSRPRRSRSRSRSRRRHQRKYRRYSRSYSRSRSRSRRRRYYRRSRYRY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 309 SGSHDRYRHRSRSHEKHRHRSRS------GERYPNRAKERH------HRSRSPNHSRSRTP--TERIDKAKLLEIAKANA 374
Cdd:pfam17069 106 SRRYYRSPSRSRSRSRSRSRGRSyyaiwrGSRYYGFGRTVYpersprWRSRSRTRSRSRTPfrLSEKERMELLEIAKANA 185
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1126170404 375 INQFRAGMIPAHLPIPSMTPEEELAKKSGGKTVEELTKFCKFLSEKEKAGDEDE 428
Cdd:pfam17069 186 AKALGTQNLDLPASLREMEQAKERSRGGVSSSGDKEERVRVDLSEQKTADDEAE 239
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
238-398 3.75e-03

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 40.65  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 238 KDRLKSQEhRSGSGKHSRSRSKshdrhhkhrhrsssrERHRHKGSSRHRS------RSRHRSRSRQGSRHRSRSRHRSGS 311
Cdd:TIGR01642   1 RDEEPDRE-REKSRGRDRDRSS---------------ERPRRRSRDRSRFrdrhrrSRERSYREDSRPRDRRRYDSRSPR 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 312 HDRYRHRSRSHEKHRHRSRSGERypNRAKERHHRSRSPNHSRSRTPTERI--DKAKL-LEIAKANAINQFRAGMIPAHLP 388
Cdd:TIGR01642  65 SLRYSSVRRSRDRPRRRSRSVRS--IEQHRRRLRDRSPSNQWRKDDKKRSlwDIKPPgYELVTADQAKASQVFSVPGTAP 142
                         170
                  ....*....|
gi 1126170404 389 IPSMTPEEEL 398
Cdd:TIGR01642 143 RPAMTDPEKL 152
 
Name Accession Description Interval E-value
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
676-750 1.08e-46

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: 160.14  E-value: 1.08e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126170404 676 GKHPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYQPTIASPNKKHAKAQAATVALQAMGLIP 750
Cdd:cd19870     1 GKHPVSALMELCNKRKWGPPEFRLVEESGPPHRKHFLFKVVVNGVEYQPSVASGNKKDAKAQAATVALQALGLVP 75
DSRM smart00358
Double-stranded RNA binding motif;
679-747 7.47e-17

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 75.38  E-value: 7.47e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126170404  679 PVSALMEICNKRKWmPPEFVLVHDSGPDHKKNFLFKVRINsEEYQPTIASPNKKHAKAQAATVALQAMG 747
Cdd:smart00358   1 PKSLLQELAQKRKL-PPEYELVKEEGPDHAPRFTVTVKVG-GKRTGEGEGSSKKEAKQRAAEAALRSLK 67
G-patch pfam01585
G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in ...
608-649 9.05e-14

G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines.


Pssm-ID: 396249 [Multi-domain]  Cd Length: 45  Bit Score: 65.99  E-value: 9.05e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1126170404 608 QGGMGMQLMKKMGWKPGEGLGKGQTGVLEPLTLDVKTDRRGL 649
Cdd:pfam01585   1 TSNIGFKLLQKMGWKEGQGLGKNEQGIAEPIEAKIKKDRRGL 42
DND1_DSRM pfam14709
double strand RNA binding domain from DEAD END PROTEIN 1; A C-terminal domain in human dead ...
679-747 4.69e-12

double strand RNA binding domain from DEAD END PROTEIN 1; A C-terminal domain in human dead end protein 1 (DND1_HUMAN) homologous to double strand RNA binding domains (PF00035, PF00333)


Pssm-ID: 405408  Cd Length: 80  Bit Score: 61.97  E-value: 4.69e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126170404 679 PVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEE---------YQPTIASPNKKHAKAQAATVALQAMG 747
Cdd:pfam14709   3 AVSHLEELCQKNKWGSPVYELHSTAGPDGKQLFTYKVVIPGIEtpfpgviwiFMPGKLCSTKEEAKEAAAEQVLEALG 80
G_patch smart00443
glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in ...
606-649 9.28e-12

glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins.


Pssm-ID: 197727 [Multi-domain]  Cd Length: 47  Bit Score: 60.25  E-value: 9.28e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1126170404  606 PVQGGMGMQLMKKMGWKPGEGLGKGQTGVLEPLTLDVKTDRRGL 649
Cdd:smart00443   1 ISTSNIGAKLLRKMGWKEGQGLGKNEQGIVEPISAEIKKDRKGL 44
DSRM_DCL_plant cd19869
double-stranded RNA binding motif of plant Dicer-like proteins; The family includes plant ...
685-744 9.91e-12

double-stranded RNA binding motif of plant Dicer-like proteins; The family includes plant Dicer-like (DCL) proteins and other ribonuclease (RNase) III-like (RTL) proteins. DCLs are endoribonucleases involved in RNA-mediated post-transcriptional gene silencing (PTGS). They function in the microRNA (miRNA) biogenesis pathway by cleaving primary miRNAs (pri-miRNAs) and precursor miRNAs (pre-miRNAs). Family members contain a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380698  Cd Length: 70  Bit Score: 60.84  E-value: 9.91e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126170404 685 EICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYQPTI-----ASPNKKHAKAQAATVALQ 744
Cdd:cd19869     2 EICLKRRWPMPVYRCVEEEGPAHAKRFTYMVRVKIPERGWTIecegePMRSKKRAKDSAALLLLE 66
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
677-744 1.55e-11

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: 60.36  E-value: 1.55e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126170404 677 KHPVSALMEICNKRKwMPPEFVLVhDSGPDHKKNFLFKVRINSEEYQPTIASpNKKHAKAQAATVALQ 744
Cdd:cd19875     1 KNPVSALNEYCQKRG-LSLEFVDV-SVGPDHCPGFTASATIDGIVFASATGT-SKKEAKRAAAKLALK 65
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
677-746 1.09e-10

double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase III (EC 3.1.26.3; also known as ribonuclease 3) digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. It is involved in the processing of rRNA precursors, viral transcripts, some mRNAs, and at least 1 tRNA (metY, a minor form of tRNA-init-Met). It cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs. The cleavage can occur in assembled 30S, 50S, and even 70S subunits and is influenced by the presence of ribosomal proteins. The RNase III family also includes the mitochondrion-specific ribosomal protein mL44 subfamily, which is composed of mitochondrial 54S ribosomal protein L3 (MRPL3) and mitochondrial 39S ribosomal protein L44 (MRPL44). Members of this family contain an RNase III domain and a C-terminal double-stranded RNA binding motif (DSRM). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380682 [Multi-domain]  Cd Length: 69  Bit Score: 57.89  E-value: 1.09e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1126170404 677 KHPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYqpTIAS-PNKKHAKAQAATVALQAM 746
Cdd:cd10845     1 KDYKTALQEYLQKRGLPLPEYELVEEEGPDHNKTFTVEVKVNGKVI--GEGTgRSKKEAEQAAAKAALEKL 69
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
684-743 2.67e-10

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: 56.52  E-value: 2.67e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 684 MEICNKRKWMPPEFVLVHdSGPDHKKNFLFKVRINSEEYQPTiaSPNKKHAKAQAATVAL 743
Cdd:cd00048     1 NELCQKNKWPPPEYETVE-EGGPHNPRFTCTVTVNGQTFEGE--GKSKKEAKQAAAEKAL 57
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
679-744 4.13e-10

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


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 56.08  E-value: 4.13e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126170404 679 PVSALMEICNKRKWMPPeFVLVHDSGPDHKKNFLFKVRINSEEYQPTIASpNKKHAKAQAATVALQ 744
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPP-YEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGS-SKKEAEQLAAEKALE 64
DSRM_PRKRA-like_rpt2 cd19863
second double-stranded RNA binding motif of PRKRA, TARBP2 and similar proteins; The family ...
678-739 3.46e-09

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


Pssm-ID: 380692  Cd Length: 67  Bit Score: 53.54  E-value: 3.46e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126170404 678 HPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRInsEEYQPTIASPNKKHAKAQAA 739
Cdd:cd19863     1 NPVGILQELCVQRRWRLPEYEVEQESGPPHEKEFTIACRV--ENFSETGSGKSKKLAKRAAA 60
DSRM_DRADA_rpt2 cd19914
second double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
677-746 3.98e-09

second double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) and similar proteins; DRADA (EC 3.5.4.37; also known as 136 kDa double-stranded RNA-binding protein (p136), interferon-inducible protein 4 (IFI-4), K88DSRBP, ADAR1, G1P1, or ADAR) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. Vertebrate DRADA contains three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380743  Cd Length: 71  Bit Score: 53.70  E-value: 3.98e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 677 KHPVSALMEiCNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYQPTIAsPNKKHAKAQAATVALQAM 746
Cdd:cd19914     1 KNPISVLME-HSQKSGNMCEFQLLSQEGPPHDPKFTYCVKVGEQTFPSVVA-NSKKVAKQMAAEEAVKEL 68
DSRM_A1CF cd19900
double-stranded RNA binding motif of APOBEC1 complementation factor (A1CF) and similar ...
677-748 9.31e-09

double-stranded RNA binding motif of APOBEC1 complementation factor (A1CF) and similar proteins; A1CF (also known as APOBEC1-stimulating protein) is an essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the posttranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. A1CF binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. It contains three RNA recognition motifs (RRMs) and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380729  Cd Length: 81  Bit Score: 52.86  E-value: 9.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 677 KHPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRI--------NSEEYQPTIASPNKKHAKAQAATVALQAMGL 748
Cdd:cd19900     1 KSPPQILEEICQKNNWGQPVYQLHSTIGPDQRQLFLYKVTIpalasqypNITPFQPNKLCRSVEEAKSYAAEYTLQQLGI 80
DSRM_A1CF-like cd19872
double-stranded RNA binding motif of APOBEC1 complementation factor (A1CF), RNA-binding ...
678-747 1.11e-08

double-stranded RNA binding motif of APOBEC1 complementation factor (A1CF), RNA-binding protein 46 (RBM46) and similar proteins; The family includes two dsRNA-binding motif-containing proteins, A1CF and RBM46. A1CF (also known as APOBEC1-stimulating protein) is an essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the posttranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. A1CF binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. RBM46 (also called cancer/testis antigen 68 (CT68), or RNA-binding motif protein 46) plays a novel role in the regulation of embryonic stem cell (ESC) differentiation by regulating the degradation of beta-catenin mRNA. It also regulates trophectoderm specification by stabilizing Cdx2 mRNA in early mouse embryos. Members of this family contain three RNA recognition motifs (RRMs) and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380701  Cd Length: 75  Bit Score: 52.29  E-value: 1.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126170404 678 HPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYQPTIASPNK-----KHAKAQAATVALQAMG 747
Cdd:cd19872     1 NPVQILEEICQKNGWGEPVYQLLSTSSNNEVQLFIYKVTIPNLPNGRLTFQPDKlcrtpEEAKVLAAEFVLAQLG 75
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
668-747 1.40e-08

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 55.88  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 668 DTTGKDLSGKHPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYqpTIAS-PNKKHAKAQAATVALQAM 746
Cdd:COG0571   148 EEIAPGGAGKDYKTALQEWLQARGLPLPEYEVVEEEGPDHAKTFTVEVLVGGKVL--GEGTgRSKKEAEQAAAKAALEKL 225

                  .
gi 1126170404 747 G 747
Cdd:COG0571   226 G 226
DSRM_DRADA cd19902
double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) ...
677-746 2.18e-08

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: 51.52  E-value: 2.18e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 677 KHPVSALMEICNKRKwMPPEFVLVHDSGPDHKKNFLFKVRINSEEYqPTIASPNKKHAKAQAATVALQAM 746
Cdd:cd19902     1 KNPVSALMEYAQSRG-VTAEIEVLSQSGPPHNPRFKAAVFVGGRRF-PSVEASSKKDAKQEAADLALRAL 68
DSRM_PRKRA-like_rpt1 cd19862
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
677-746 3.11e-08

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


Pssm-ID: 380691 [Multi-domain]  Cd Length: 70  Bit Score: 51.11  E-value: 3.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 677 KHPVSALMEICNKRKWmPPEFVLVHDSGPDHKKNFLFKVRInsEEYQPTIASPNKKHAKAQAATVALQAM 746
Cdd:cd19862     1 KTPISVLQELCAKRGI-TPKYELISSEGAVHEPTFTFRVTV--GDITATGSGTSKKKAKHAAAENALEQL 67
DSRM_ADAD1 cd19905
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) ...
677-746 7.06e-08

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: 49.96  E-value: 7.06e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 677 KHPVSALMEICnKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYQPTIASpNKKHAKAQAATVALQAM 746
Cdd:cd19905     1 KNPVSALHEYA-QMTRLKLSFKETVTTGNVAGPYFAFCAVVDGIEYPTGVGK-TKKEAKANAAKIALDEL 68
DSRM_STAU_rpt4 cd19860
fourth double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
678-747 1.43e-07

fourth double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins; Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the fourth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380689  Cd Length: 68  Bit Score: 48.87  E-value: 1.43e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 678 HPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEeyQPTIASPNKKHAKAQAATVALQAMG 747
Cdd:cd19860     1 NPISRLIQIQQARKEKEPVYSLVAERGTPRRREFVMQVTVGDK--TATGTGPNKKLAKRNAAEAMLELLG 68
RSRP pfam17069
Arginine/Serine-Rich protein 1; RSRP1 is an eukaryotic protein family. Its function is unknown.
229-428 2.21e-07

Arginine/Serine-Rich protein 1; RSRP1 is an eukaryotic protein family. Its function is unknown.


Pssm-ID: 293674 [Multi-domain]  Cd Length: 299  Bit Score: 53.24  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 229 GECRSRSLSKDRLKSQEHRSGSGKHSRSRSKSHDRHHKHRHRSSSRERHRHKGSSRHRSRSRHRSRSRQGSRHRSRSRHR 308
Cdd:pfam17069  26 SSSRLSSRSRSRSSSRSSRSHSRSSSRFSSRSRSRPRRSRSRSRSRRRHQRKYRRYSRSYSRSRSRSRRRRYYRRSRYRY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 309 SGSHDRYRHRSRSHEKHRHRSRS------GERYPNRAKERH------HRSRSPNHSRSRTP--TERIDKAKLLEIAKANA 374
Cdd:pfam17069 106 SRRYYRSPSRSRSRSRSRSRGRSyyaiwrGSRYYGFGRTVYpersprWRSRSRTRSRSRTPfrLSEKERMELLEIAKANA 185
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1126170404 375 INQFRAGMIPAHLPIPSMTPEEELAKKSGGKTVEELTKFCKFLSEKEKAGDEDE 428
Cdd:pfam17069 186 AKALGTQNLDLPASLREMEQAKERSRGGVSSSGDKEERVRVDLSEQKTADDEAE 239
DSRM_DRADA_rpt1 cd19913
first double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
677-744 2.58e-07

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: 48.33  E-value: 2.58e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126170404 677 KHPVSALMEICnKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYQPTIASpNKKHAKAQAATVALQ 744
Cdd:cd19913     1 KNPVSGLMEYA-QFLGQTCEFLLLEQSGPSHDPRFKFQAVIDGRRFPPAEAS-SKKVAKKDAAAIALK 66
DSRM_DGCR8_rpt1 cd19867
first double-stranded RNA binding motif of DiGeorge syndrome critical region 8 (DGCR8) and ...
673-750 9.18e-07

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: 46.94  E-value: 9.18e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126170404 673 DLSGKHPVSALMEICNKRKWMPPEFvlVHDSGPDHKKNFLFKVRINSEEYQPTIASpNKKHAKAQAATVALQAmgLIP 750
Cdd:cd19867     2 NPDGKSPVCILHEYCQRVLKVQPEY--NFTETENAATPFSAEVFINGVEYGSGEAS-SKKLAKQKAARATLEI--LIP 74
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
680-746 2.13e-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: 45.84  E-value: 2.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126170404 680 VSALMEICNKRKWMPpEFVLVHDSGPDHKKNFLFKVRINSEEYqPTIASPNKKHAKAQAATVALQAM 746
Cdd:cd19903     4 MGKLNEYCQKQKVVL-DYVEVPTSGPSHDPRFTFQVVIDGKEY-PEGEGKSKKEAKQAAAKLALEIL 68
DSRM_PRKRA_rpt2 cd19891
second double-stranded RNA binding motif of protein activator of the interferon-induced ...
679-739 7.20e-06

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


Pssm-ID: 380720  Cd Length: 67  Bit Score: 44.16  E-value: 7.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1126170404 679 PVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRInsEEYQPTIASPNKKHAKAQAA 739
Cdd:cd19891     2 PIGSLQELAVQKGWRLPEYTLAQESGPPHKREFTITCRV--ETFVETGTGTSKKVAKRNAA 60
DSRM_DHX9_rpt1 cd19854
first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; ...
683-739 7.69e-06

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: 44.18  E-value: 7.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1126170404 683 LMEICNKRKwMPPEFVlVHDSGPDHKKNFLFKVRINSEEYQPTIASPNKKHAKAQAA 739
Cdd:cd19854     6 LYAWCGKKK-LTPEYD-IKEAGNKHRQRFKCEVRVEGFDYVGTGNATNKKDAQTNAA 60
DSRM_DRADA_rpt3 cd19915
third double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
677-746 1.28e-05

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: 43.78  E-value: 1.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 677 KHPVSALMEICnKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYqPTIASPNKKHAKAQAATVALQAM 746
Cdd:cd19915     1 TNPVSGLLEYA-RSKGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWF-PAVCAHNKKQGKQEAADAALRVL 68
DSRM_RED1_rpt2 cd19898
second double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar ...
675-746 1.79e-05

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: 43.25  E-value: 1.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126170404 675 SGKHPVSALMEIcnkRKWMPPEFVlvHDSGPDHKKNFLFKVRINSEEYQPTiaSPNKKHAKAQAATVALQAM 746
Cdd:cd19898     1 SGKNPVMILNEL---RPGLKYEFV--SESGESHAKNFVMSVTVDGQTFEGS--GRNKKLAKARAAQAALAKL 65
DSRM_STRBP_RED-like_rpt2 cd19866
second double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This ...
677-744 2.61e-05

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


Pssm-ID: 380695  Cd Length: 63  Bit Score: 42.54  E-value: 2.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126170404 677 KHPVsalMEICNKRKWMppEFVLVHDSGPDHKKNFLFKVRINSEEYQPTiaSPNKKHAKAQAATVALQ 744
Cdd:cd19866     1 KNPV---MLLNELRPGL--KYKCLSESGESHAKSFVMSVTVDGQTFEGT--GRSKKLAKAAAAQAALA 61
DSRM_STAU2_rpt4 cd19886
fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen ...
676-747 3.38e-05

fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins; Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fourth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380715  Cd Length: 86  Bit Score: 43.02  E-value: 3.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126170404 676 GKHPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEeyQPTIASPNKKHAKAQAATVALQAMG 747
Cdd:cd19886     2 GMNPISRLAQIQQAKKEKEPEYVLLSERGMPRRREFVMQVKVGNE--VATGTGPNKKIAKRNAAEAMLLQLG 71
DSRM_DUS2L cd19871
double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) ...
679-748 6.24e-05

double-stranded RNA binding motif of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (DUS2L) and similar proteins; DUS2L (also known as dihydrouridine synthase 2 (DUS2), up-regulated in lung cancer protein 8 (URLC8), or tRNA-dihydrouridine synthase 2-like) catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. It negatively regulates the activation of EIF2AK2/PKR. DUS2L contains an N-terminal FMN-binding domain and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380700  Cd Length: 68  Bit Score: 41.49  E-value: 6.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 679 PVSALMEICNKRKWMPPEFVLVHDSGpdhKKNFLFKVRINSEEYQPTIASPNKKHAKAQAATVALQAMGL 748
Cdd:cd19871     2 PKMILNEWCRKNKLPQPVYETVQRPS---DRLFQSVVTVDGKKYTSSLWEKSKKLAEQAAAIVCLRALGL 68
DSRM_STAU1_rpt4 cd19885
fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen ...
676-754 1.42e-04

fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fourth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380714  Cd Length: 86  Bit Score: 41.23  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 676 GKHPVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRINSEEYQPTiaSPNKKHAKAQAATVALQAMGL-IPKDAP 754
Cdd:cd19885     9 GMNPISRLAQIQQAKKEKEPEYTLITERGLPRRREFVMQVKVGNQTAEGM--GPNKKVAKRNAAEKMLELLGFkVPQPQP 86
DSRM_STRBP_rpt1 cd19909
first double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) ...
679-747 1.69e-04

first double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) and similar proteins; STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. STRBP contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380738  Cd Length: 84  Bit Score: 40.78  E-value: 1.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126170404 679 PVSALMEICNKRKWMppEFVLVHDSGPDHKKNFLFKVRINSEEYQPTiaSPNKKHAKAQAATVALQAMG 747
Cdd:cd19909     5 PMNALMRLNQIRPGL--QYKLLSQSGPVHAPVFTMSVDVDGTTYEAS--GPSKKTAKLHVAVKVLQAMG 69
DSRM_AtDRB-like_rpt1 cd19907
first double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding ...
681-746 2.11e-04

first double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRBs)and similar proteins; This family includes a group of Arabidopsis thaliana double-stranded RNA-binding proteins (AtDRB1-5). They bind double-stranded RNA (dsRNA) and may be involved in RNA-mediated silencing. Members of this family contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380736 [Multi-domain]  Cd Length: 69  Bit Score: 40.15  E-value: 2.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126170404 681 SALMEICNKRKWMPPEFVLVHdSGPDHKKNFLFKVRINSEEYQPTIASPNKKHAKAQAATVALQAM 746
Cdd:cd19907     4 SQLQEYAQKSCLNLPVYACIR-EGPDHAPRFRATVTFNGVIFESPPGFPTLKAAEHSAAEVALNSL 68
DSRM_TARBP2_rpt2 cd10844
second double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and ...
679-743 2.81e-04

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


Pssm-ID: 380681  Cd Length: 67  Bit Score: 39.70  E-value: 2.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126170404 679 PVSALMEICNKRKWMPPEFVLVHDSGPDHKKNFLFKVRInsEEYQPTIASPNKKHAKAQAATVAL 743
Cdd:cd10844     2 PVGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRV--ERFIEIGSGTSKKLAKRNAAAKML 64
DSRM_STAU_rpt1 cd19857
first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
679-739 3.45e-04

first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins; Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380686  Cd Length: 64  Bit Score: 39.17  E-value: 3.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126170404 679 PVSALMEICNKRKwMPPEFVLVHDSGPDHKKNFLFKVRINSEE-YQPTIASPNK-KHAKAQAA 739
Cdd:cd19857     2 PMCLLNELARFNK-IRPQYTLVDEEGPAHKKTFTVKLTLGDEEeYEASGSSIKKaQHAAAEKA 63
G-patch_2 pfam12656
G-patch domain; Yeast Spp2, a G-patch protein and spliceosome component, interacts with the ...
606-649 3.57e-04

G-patch domain; Yeast Spp2, a G-patch protein and spliceosome component, interacts with the ATP-dependent DExH-box splicing factor Prp2. As this interaction involves the G-patch sequence in Spp2 and is required for the recruitment of Prp2 to the spliceosome before the first catalytic step of splicing, it is proposed that Spp2 might be an accessory factor that confers spliceosome specificity on Prp2.


Pssm-ID: 432700 [Multi-domain]  Cd Length: 61  Bit Score: 39.18  E-value: 3.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1126170404 606 PVqGGMGMQLMKKMGWKPGEGLGKGQTGVLEPLTLDVKTDRRGL 649
Cdd:pfam12656  13 PV-EEFGAAMLRGMGWKPGQGIGKNKKGDVKPKEYKRRPGGLGL 55
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
680-746 5.28e-04

double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380746  Cd Length: 68  Bit Score: 38.91  E-value: 5.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126170404 680 VSALMEICNKRKwMPPEFVLVHDSGPDHKKNFLFKVRINSEEYqPTIASPNKKHAKAQAATVALQAM 746
Cdd:cd20314     4 VSLLNEYCQKER-LTVKYEEEKRSGPTHKPRFFCKYIIDGKEY-PEGEGKSKKEAKQAAARLAYEEL 68
DSRM_STRBP_rpt2 cd19911
second double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) ...
677-746 6.27e-04

second double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) and similar proteins; STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. STRBP contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380740  Cd Length: 64  Bit Score: 38.58  E-value: 6.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 677 KHPVsalMEICNKRKWMppEFVLVHDSGPDHKKNFLFKVRINSEEYQPtiASPNKKHAKAQAATVALQAM 746
Cdd:cd19911     1 KNPV---MELNEKRRGL--KYELISETGGSHDKRFVMEVEVDGQKFRG--AGPNKKVAKASAALAALEKL 63
DSRM_STAU_rpt3 cd19859
third double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
679-746 6.62e-04

third double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins; Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380688  Cd Length: 65  Bit Score: 38.53  E-value: 6.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126170404 679 PVSALMEICNKRKwMPPEFVLVHDSGPDHKKNFLFKVRINSEEYQPTIASpnKKHAKAQAATVALQAM 746
Cdd:cd19859     1 EISLVHEIALKRN-LTVNFEVLRESGPPHMKNFITRCTVGSFVTEGEGNS--KKVSKKRAAEKMLEEL 65
DSRM_ILF3_rpt2 cd19912
second double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and ...
676-746 1.43e-03

second double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and similar proteins; ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. ILF3 contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380741  Cd Length: 72  Bit Score: 38.09  E-value: 1.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1126170404 676 GKHPVsalMEICNKRKWMppEFVLVHDSGPDHKKNFLFKVRINSEEYQPTiaSPNKKHAKAQAATVALQAM 746
Cdd:cd19912     6 GKNPV---MELNEKRRGL--KYELISETGGSHDKRFVMEVEVDGQKFQGA--GSNKKVAKAYAALAALEKL 69
DSRM_STRBP-like_rpt2 cd19897
second double-stranded RNA binding motif of STRBP, ILF3 and similar proteins; This family ...
677-746 1.70e-03

second double-stranded RNA binding motif of STRBP, ILF3 and similar proteins; This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3). STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Members of this STRBP/ILF3 group contain an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380726  Cd Length: 64  Bit Score: 37.34  E-value: 1.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 677 KHPVsalMEICNKRKWMPPEfvLVHDSGPDHKKNFLFKVRINSEEYQPtiASPNKKHAKAQAATVALQAM 746
Cdd:cd19897     1 KNPV---MELNEKRRGLKYE--LISETGGSHDKRFVMEVEVDGQKFQG--AGSNKKVAKANAALAALEKL 63
DSRM_STAU2_rpt3 cd19884
third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
677-746 2.84e-03

third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins; Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380713  Cd Length: 67  Bit Score: 36.91  E-value: 2.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 677 KHPVSALMEICNKRKwMPPEFVLVHDSGPDHKKNFLFKVRINseEYQPTIASPNKKHAKAQAATVALQAM 746
Cdd:cd19884     1 KSEISLVFEIALKRN-MPVSFEVIKESGPPHMKSFVTRVTVG--EFTAEGEGNSKKLSKKRAATSVLQEL 67
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
238-398 3.75e-03

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 40.65  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 238 KDRLKSQEhRSGSGKHSRSRSKshdrhhkhrhrsssrERHRHKGSSRHRS------RSRHRSRSRQGSRHRSRSRHRSGS 311
Cdd:TIGR01642   1 RDEEPDRE-REKSRGRDRDRSS---------------ERPRRRSRDRSRFrdrhrrSRERSYREDSRPRDRRRYDSRSPR 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 312 HDRYRHRSRSHEKHRHRSRSGERypNRAKERHHRSRSPNHSRSRTPTERI--DKAKL-LEIAKANAINQFRAGMIPAHLP 388
Cdd:TIGR01642  65 SLRYSSVRRSRDRPRRRSRSVRS--IEQHRRRLRDRSPSNQWRKDDKKRSlwDIKPPgYELVTADQAKASQVFSVPGTAP 142
                         170
                  ....*....|
gi 1126170404 389 IPSMTPEEEL 398
Cdd:TIGR01642 143 RPAMTDPEKL 152
DSRM_STAU1_rpt3 cd19883
third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
677-746 3.95e-03

third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380712  Cd Length: 67  Bit Score: 36.53  E-value: 3.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126170404 677 KHPVSALMEICNKRKwMPPEFVLVHDSGPDHKKNFLFKVRINseEYQPTIASPNKKHAKAQAATVALQAM 746
Cdd:cd19883     1 KSEISQVFEIALKRN-MPVNFEVTKETGPPHMKSFVTKVSVG--EFAGEGEGKSKKISKKNAAIAVLEEL 67
DSRM_AtDRB-like cd19878
double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins ...
681-747 6.11e-03

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: 35.96  E-value: 6.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126170404 681 SALMEICNKRKWMPPEFVLVHDsGPDHKKNFLFKVRINSEEYQPTIAsPNKKHAKAQAATVALQAMG 747
Cdd:cd19878     3 NLLQEYAQKKKIPLPKYESAKS-GPSHQPTFVSTVIVLGVRFSSEGA-KNKKQAEQSAAKVALKELG 67
 
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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