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Conserved domains on  [gi|1927152830|ref|XP_036938845|]
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ATP-dependent RNA helicase A [Acanthopagrus latus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 356-589 8.28e-158

DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


:

Pssm-ID: 350730 [Multi-domain]  Cd Length: 234  Bit Score: 472.01  E-value: 8.28e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  356 VPWSPPQVNWNPWTSSNIDEGPLAFCTPEQISGDLHDELMYQLDHDENLQKILSERDQLPVKQFEEEIMATIDSNPVVII 435
Cdd:cd17972      1 VPWSPPQSNWNPWTSSNIDEGPLAFATPEQISMDLKNELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVII 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  436 RGATGCGKTTQVPQYILDRFIKGGRASDCNIVVTQPRRISAVSVAERVAYERAEDLGKSCGYSVRFESVLPRPHASILFC 515
Cdd:cd17972     81 RGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRPHASILFC 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927152830  516 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSATIDTTMFREYFFNSPIIEV 589
Cdd:cd17972    161 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
412-911 7.06e-115

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG1643:

Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 379.81  E-value: 7.06e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  412 DQLPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDR-FIKGGRasdcnIVVTQPRRISAVSVAERVAYERAED 490
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELgWGAGGR-----IGMLEPRRLAARAAAERMAEELGEP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  491 LGKSCGYSVRFESVLpRPHASILFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAY-PEVRVIL 567
Cdd:COG1643     83 VGETVGYRVRFEDKV-SAATRIEVVTEGILLRELQRdpELEGVDTVIFDEFHERSLNADLLLALLLDLQPALrPDLKLLV 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  568 MSATIDTTMFREYFFNSPIIEVFGRTFPVQeyfledciqmTNFIPPPMDRKkkdkdeeggeddtncnvicgpeysaetkr 647
Cdd:COG1643    162 MSATLDAERFARLLGDAPVIESSGRTYPVE----------VRYRPLPADER----------------------------- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  648 smaqineketsfELVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLEtnPHFGSNrYRILPLHSQIPREEQRRVFE 725
Cdd:COG1643    203 ------------DLEDAVADAVREAlaEEPGDILVFLPGEREIRRTAEALR--GRLPPD-TEILPLYGRLSAAEQDRAFA 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  726 PVPDNITKVILSTNIAETSITINDVVYVIDSCKQKVKLFtSHNN-MTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSH 804
Cdd:COG1643    268 PAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRY-DPRSgVTRLPTERISQASANQRAGRAGRLAPGICYRLWSE 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  805 ARFERLETHMTPEIFRTPLHEVALSIKLLRLGAIGHFlsKAIEPPPLDAVIEAEHTLKELDALDSNDELTPLGRILARLP 884
Cdd:COG1643    347 EDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLP 424

                          490       500
                   ....*....|....*....|....*..
gi 1927152830  885 IEPRLGKMMIMGCIFHVGDAMCTISAA 911
Cdd:COG1643    425 LDPRLARMLLAAAELGCLREAAILAAL 451
DSRM_DHX9_rpt1 cd19854
first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; ...
 3-71 1.70e-43

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: 152.04  E-value: 1.70e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927152830    3 DIKNFLYAWCGKKKLTPNYDIRAAGNKNRQKFMCEVRVDGFNYIGMGNSTNKKDAQTNAARDFVNYLVR 71
Cdd:cd19854      1 EIKAFLYAWCGKKKLTPEYDIKEAGNKHRQRFKCEVRVEGFDYVGTGNATNKKDAQTNAARDFLNYLVR 69
DSRM_DHX9_rpt2 cd19855
second double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; ...
 204-278 2.96e-43

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


:

Pssm-ID: 380684  Cd Length: 75  Bit Score: 151.60  E-value: 2.96e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927152830  204 LENAKARLNQFFQKEKTSAEYKYSQVGPDHNRSFIAEMQLFVRQLGRRITAREHGSNKKLAAQSCALSLVRQLYH 278
Cdd:cd19855      1 LDNAKSRLNEFLQKNKIPAEYKYTSVGPDHNRSFIAELSIFVKQLGKTIYARETGSNKKLASQSCALSLVRQLYH 75
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1019-1098 5.22e-19

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


:

Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 82.69  E-value: 5.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830 1019 LLTFGLYPNVCYHKEKRKILTT--EGRNALIHKSSVNCpfssHDITYPSPFFVFSEKIRTRAISAKGMTLVSPLQLLLFA 1096
Cdd:pfam07717    4 ALAAGLYPNVARRDPKGKGYTTlsDNQRVFIHPSSVLF----NEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFA 79


                   ..
gi 1927152830 1097 CK 1098
Cdd:pfam07717   80 PH 81
 
Name Accession Description Interval E-value
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 356-589 8.28e-158

DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350730 [Multi-domain]  Cd Length: 234  Bit Score: 472.01  E-value: 8.28e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  356 VPWSPPQVNWNPWTSSNIDEGPLAFCTPEQISGDLHDELMYQLDHDENLQKILSERDQLPVKQFEEEIMATIDSNPVVII 435
Cdd:cd17972      1 VPWSPPQSNWNPWTSSNIDEGPLAFATPEQISMDLKNELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVII 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  436 RGATGCGKTTQVPQYILDRFIKGGRASDCNIVVTQPRRISAVSVAERVAYERAEDLGKSCGYSVRFESVLPRPHASILFC 515
Cdd:cd17972     81 RGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRPHASILFC 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927152830  516 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSATIDTTMFREYFFNSPIIEV 589
Cdd:cd17972    161 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
412-911 7.06e-115

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 379.81  E-value: 7.06e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  412 DQLPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDR-FIKGGRasdcnIVVTQPRRISAVSVAERVAYERAED 490
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELgWGAGGR-----IGMLEPRRLAARAAAERMAEELGEP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  491 LGKSCGYSVRFESVLpRPHASILFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAY-PEVRVIL 567
Cdd:COG1643     83 VGETVGYRVRFEDKV-SAATRIEVVTEGILLRELQRdpELEGVDTVIFDEFHERSLNADLLLALLLDLQPALrPDLKLLV 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  568 MSATIDTTMFREYFFNSPIIEVFGRTFPVQeyfledciqmTNFIPPPMDRKkkdkdeeggeddtncnvicgpeysaetkr 647
Cdd:COG1643    162 MSATLDAERFARLLGDAPVIESSGRTYPVE----------VRYRPLPADER----------------------------- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  648 smaqineketsfELVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLEtnPHFGSNrYRILPLHSQIPREEQRRVFE 725
Cdd:COG1643    203 ------------DLEDAVADAVREAlaEEPGDILVFLPGEREIRRTAEALR--GRLPPD-TEILPLYGRLSAAEQDRAFA 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  726 PVPDNITKVILSTNIAETSITINDVVYVIDSCKQKVKLFtSHNN-MTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSH 804
Cdd:COG1643    268 PAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRY-DPRSgVTRLPTERISQASANQRAGRAGRLAPGICYRLWSE 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  805 ARFERLETHMTPEIFRTPLHEVALSIKLLRLGAIGHFlsKAIEPPPLDAVIEAEHTLKELDALDSNDELTPLGRILARLP 884
Cdd:COG1643    347 EDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLP 424

                          490       500
                   ....*....|....*....|....*..
gi 1927152830  885 IEPRLGKMMIMGCIFHVGDAMCTISAA 911
Cdd:COG1643    425 LDPRLARMLLAAAELGCLREAAILAAL 451
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 414-896 9.53e-73

ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 260.47  E-value: 9.53e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGRasdcnIVVTQPRRISAVSVAERVAYERAEDLGK 493
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGGK-----IIMLEPRRLAARSAAQRLASQLGEAVGQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  494 SCGYSVRFES-VLPRPHASILfcTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPE-VRVILMS 569
Cdd:TIGR01970   76 TVGYRVRGENkVSRRTRLEVV--TEGILTRMIQDdpELDGVGALIFDEFHERSLDADLGLALALDVQSSLREdLKILAMS 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  570 ATIDTTMFREYFFNSPIIEVFGRTFPVQEYFLedciqmtnfippPMDRKKKdkdeeggeddtncnvicgpeysaetkrsm 649
Cdd:TIGR01970  154 ATLDGERLSSLLPDAPVVESEGRSFPVEIRYL------------PLRGDQR----------------------------- 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  650 aqineketsfeLVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLetNPHFGSnRYRILPLHSQIPREEQRRVFEPV 727
Cdd:TIGR01970  193 -----------LEDAVSRAVEHAlaSETGSILVFLPGQAEIRRVQEQL--AERLDS-DVLICPLYGELSLAAQDRAIKPD 258

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  728 PDNITKVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSHARF 807
Cdd:TIGR01970  259 PQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQH 338

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  808 ERLETHMTPEIFRTPLheVALSIKLLRLGAIGHFLSKAIEPPPLDAVIEAEHTLKELDALDSNDELTPLGRILARLPIEP 887
Cdd:TIGR01970  339 QRLPAQDEPEILQADL--SGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHP 416


                   ....*....
gi 1927152830  888 RLGKMMIMG 896
Cdd:TIGR01970  417 RLAAMLLSA 425
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 412-912 7.76e-70

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 257.68  E-value: 7.76e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  412 DQLPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILD--RFIKGgrasdcNIVVTQPRRISAVSVAERVAYERAE 489
Cdd:PRK11131    71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLElgRGVKG------LIGHTQPRRLAARTVANRIAEELET 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  490 DLGKSCGYSVRFESvlprpHAS----ILFCTVGVLLRKLEAGiRGISH---VIVDEIHERDINTDFLMVVLRDVVQAYPE 562
Cdd:PRK11131   145 ELGGCVGYKVRFND-----QVSdntmVKLMTDGILLAEIQQD-RLLMQydtIIIDEAHERSLNIDFILGYLKELLPRRPD 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  563 VRVILMSATIDTTMFREYFFNSPIIEVFGRTFPVQeyfledciqmTNFIPPPMDRKKKDKDEeggeddtncnvicgpeys 642
Cdd:PRK11131   219 LKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVE----------VRYRPIVEEADDTERDQ------------------ 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  643 aetkrsmaqineketsfelVEALLRYIETLQV--AGAVLIFLPGWNLIYSMQRHLETN--PHfgsnrYRILPLHSQIPRE 718
Cdd:PRK11131   271 -------------------LQAIFDAVDELGRegPGDILIFMSGEREIRDTADALNKLnlRH-----TEILPLYARLSNS 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  719 EQRRVFEPVPDNitKVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFC 798
Cdd:PRK11131   327 EQNRVFQSHSGR--RIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGIC 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  799 FHLCSHARFERLETHMTPEIFRTPLHEVALSIKLLRLGAIGHFlsKAIEPPPLDAVIEAEHTLKELDALDSND-----EL 873
Cdd:PRK11131   405 IRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEELGAITTDEqasayKL 482

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1927152830  874 TPLGRILARLPIEPRLGKMMI----MGCIFHVgdaMCTISAAS 912
Cdd:PRK11131   483 TPLGRQLAQLPVDPRLARMVLeaqkHGCVREV---MIITSALS 522
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 594-802 5.43e-69

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 228.96  E-value: 5.43e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  594 FPVQEYFLEDCIQMTNfipppmdrkkkdkdeeggeddtncnvicgpeysaetkrsMAQINEKETSFELVEALLRYIETLQ 673
Cdd:cd18791      1 FPVEVYYLEDILELLG---------------------------------------ISSEKEDPDYVDAAVRLILQIHRTE 41

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  674 VAGAVLIFLPGWNLIYSMQRHLETNPHFGS-NRYRILPLHSQIPREEQRRVFEPVPDNITKVILSTNIAETSITINDVVY 752
Cdd:cd18791     42 EPGDILVFLPGQEEIERLCELLREELLSPDlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVY 121

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1927152830  753 VIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLC 802
Cdd:cd18791    122 VIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DSRM_DHX9_rpt1 cd19854
first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; ...
 3-71 1.70e-43

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: 152.04  E-value: 1.70e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927152830    3 DIKNFLYAWCGKKKLTPNYDIRAAGNKNRQKFMCEVRVDGFNYIGMGNSTNKKDAQTNAARDFVNYLVR 71
Cdd:cd19854      1 EIKAFLYAWCGKKKLTPEYDIKEAGNKHRQRFKCEVRVEGFDYVGTGNATNKKDAQTNAARDFLNYLVR 69
DSRM_DHX9_rpt2 cd19855
second double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; ...
 204-278 2.96e-43

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


Pssm-ID: 380684  Cd Length: 75  Bit Score: 151.60  E-value: 2.96e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927152830  204 LENAKARLNQFFQKEKTSAEYKYSQVGPDHNRSFIAEMQLFVRQLGRRITAREHGSNKKLAAQSCALSLVRQLYH 278
Cdd:cd19855      1 LDNAKSRLNEFLQKNKIPAEYKYTSVGPDHNRSFIAELSIFVKQLGKTIYARETGSNKKLASQSCALSLVRQLYH 75
DEXDc smart00487
DEAD-like helicases superfamily;
423-595 7.51e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.95  E-value: 7.51e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830   423 IMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGrasDCNIVVTQPRRISAVSVAERVAYERAEDLGKSCGY----- 497
Cdd:smart00487   17 IEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK---GGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLyggds 93

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830   498 SVRFESVLPRPHASILFCTVGVLLRKLEAG---IRGISHVIVDEIHERDiNTDFLMVVLRDVVQAYPEVRVILMSATI-- 572
Cdd:smart00487   94 KREQLRKLESGKTDILVTTPGRLLDLLENDklsLSNVDLVILDEAHRLL-DGGFGDQLEKLLKLLPKNVQLLLLSATPpe 172

                           170       180
                    ....*....|....*....|...
gi 1927152830   573 DTTMFREYFFNSPIIEVFGRTFP 595
Cdd:smart00487  173 EIENLLELFLNDPVFIDVGFTPL 195
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 863-944 8.70e-22

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 90.41  E-value: 8.70e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830   863 ELDALDSNDELTPLGRILARLPIEPRLGKMMIMGCIFHVGDAMCTISAASCFPEPFVSE-GKRLGFVHRNFSGSRfSDHV 941
Cdd:smart00847    1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEkREDADAARRRFADPE-SDHL 79


                    ...
gi 1927152830   942 ALL 944
Cdd:smart00847   80 TLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 857-943 2.00e-20

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 87.29  E-value: 2.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  857 AEHTLKELDALDSNDELTPLGRILARLPIEPRLGKMMIMGCIFHVGDAMCTISAASCFPEPFVSEG-------------- 922
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNfldprsaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 1927152830  923 KRLGF--VHRNFSGSRF-SDHVAL 943
Cdd:pfam04408   81 RRAADekARAKFARLDLeGDHLTL 104
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1019-1098 5.22e-19

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 82.69  E-value: 5.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830 1019 LLTFGLYPNVCYHKEKRKILTT--EGRNALIHKSSVNCpfssHDITYPSPFFVFSEKIRTRAISAKGMTLVSPLQLLLFA 1096
Cdd:pfam07717    4 ALAAGLYPNVARRDPKGKGYTTlsDNQRVFIHPSSVLF----NEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFA 79


                   ..
gi 1927152830 1097 CK 1098
Cdd:pfam07717   80 PH 81
DSRM smart00358
Double-stranded RNA binding motif;
5-69 2.21e-16

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 74.61  E-value: 2.21e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927152830     5 KNFLYAWCGKKKLTPNYD-IRAAGNKNRQKFMCEVRVDGFnYIGMGNSTNKKDAQTNAARDFVNYL 69
Cdd:smart00358    2 KSLLQELAQKRKLPPEYElVKEEGPDHAPRFTVTVKVGGK-RTGEGEGSSKKEAKQRAAEAALRSL 66
DSRM smart00358
Double-stranded RNA binding motif;
207-277 7.40e-13

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 64.59  E-value: 7.40e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927152830   207 AKARLNQFFQKEKTSAEYKY-SQVGPDHNRSFIAEMQLfvrqlGRRITAREHGSNKKLAAQSCALSLVRQLY 277
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELvKEEGPDHAPRFTVTVKV-----GGKRTGEGEGSSKKEAKQRAAEAALRSLK 67
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 5-69 3.45e-12

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: 62.63  E-value: 3.45e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927152830    5 KNFLYAWCGKKKLTPNYD-IRAAGNKNRQKFMCEVRVDGFNYiGMGNSTNKKDAQTNAARDFVNYL 69
Cdd:pfam00035    2 KSLLQEYAQKNGKPPPYEyVSEEGPPHSPKFTVTVKVDGKLY-GSGTGSSKKEAEQLAAEKALEKL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 207-276 2.35e-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: 57.63  E-value: 2.35e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927152830  207 AKARLNQFFQKEKTSAEYKY-SQVGPDHNRSFIAEMQLfvrqlGRRITAREHGSNKKLAAQSCALSLVRQL 276
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYvSEEGPPHSPKFTVTVKV-----DGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 421-575 5.19e-08

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 53.79  E-value: 5.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  421 EEIMATIDSNPVVIIRGATGCGKTT--QVPqyILDRFIK---GGRAsdcnIVVTqPRRISAVSVaervaYERAEDLGKSC 495
Cdd:pfam00270    5 AEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKldnGPQA----LVLA-PTRELAEQI-----YEELKKLGKGL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  496 GYSVRFE----------SVLPRPHasILFCTVGVLLR--KLEAGIRGISHVIVDEIHErdINTDFLMVVLRDVV-QAYPE 562
Cdd:pfam00270   73 GLKVASLlggdsrkeqlEKLKGPD--ILVGTPGRLLDllQERKLLKNLKLLVLDEAHR--LLDMGFGPDLEEILrRLPKK 148

                          170
                   ....*....|...
gi 1927152830  563 VRVILMSATIDTT 575
Cdd:pfam00270  149 RQILLLSATLPRN 161
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
206-276 8.59e-04

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 42.39  E-value: 8.59e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927152830  206 NAKARLNQFFQKEKTSA-EYK-YSQVGPDHNRSFIAEmqlfVRqLGRRITAREHGSNKKLAAQSCALSLVRQL 276
Cdd:COG0571    158 DYKTALQEWLQARGLPLpEYEvVEEEGPDHAKTFTVE----VL-VGGKVLGEGTGRSKKEAEQAAAKAALEKL 225
 
Name Accession Description Interval E-value
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 356-589 8.28e-158

DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350730 [Multi-domain]  Cd Length: 234  Bit Score: 472.01  E-value: 8.28e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  356 VPWSPPQVNWNPWTSSNIDEGPLAFCTPEQISGDLHDELMYQLDHDENLQKILSERDQLPVKQFEEEIMATIDSNPVVII 435
Cdd:cd17972      1 VPWSPPQSNWNPWTSSNIDEGPLAFATPEQISMDLKNELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVII 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  436 RGATGCGKTTQVPQYILDRFIKGGRASDCNIVVTQPRRISAVSVAERVAYERAEDLGKSCGYSVRFESVLPRPHASILFC 515
Cdd:cd17972     81 RGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRPHASILFC 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927152830  516 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSATIDTTMFREYFFNSPIIEV 589
Cdd:cd17972    161 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
412-911 7.06e-115

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 379.81  E-value: 7.06e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  412 DQLPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDR-FIKGGRasdcnIVVTQPRRISAVSVAERVAYERAED 490
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELgWGAGGR-----IGMLEPRRLAARAAAERMAEELGEP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  491 LGKSCGYSVRFESVLpRPHASILFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAY-PEVRVIL 567
Cdd:COG1643     83 VGETVGYRVRFEDKV-SAATRIEVVTEGILLRELQRdpELEGVDTVIFDEFHERSLNADLLLALLLDLQPALrPDLKLLV 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  568 MSATIDTTMFREYFFNSPIIEVFGRTFPVQeyfledciqmTNFIPPPMDRKkkdkdeeggeddtncnvicgpeysaetkr 647
Cdd:COG1643    162 MSATLDAERFARLLGDAPVIESSGRTYPVE----------VRYRPLPADER----------------------------- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  648 smaqineketsfELVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLEtnPHFGSNrYRILPLHSQIPREEQRRVFE 725
Cdd:COG1643    203 ------------DLEDAVADAVREAlaEEPGDILVFLPGEREIRRTAEALR--GRLPPD-TEILPLYGRLSAAEQDRAFA 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  726 PVPDNITKVILSTNIAETSITINDVVYVIDSCKQKVKLFtSHNN-MTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSH 804
Cdd:COG1643    268 PAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRY-DPRSgVTRLPTERISQASANQRAGRAGRLAPGICYRLWSE 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  805 ARFERLETHMTPEIFRTPLHEVALSIKLLRLGAIGHFlsKAIEPPPLDAVIEAEHTLKELDALDSNDELTPLGRILARLP 884
Cdd:COG1643    347 EDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLP 424

                          490       500
                   ....*....|....*....|....*..
gi 1927152830  885 IEPRLGKMMIMGCIFHVGDAMCTISAA 911
Cdd:COG1643    425 LDPRLARMLLAAAELGCLREAAILAAL 451
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 430-589 1.46e-78

DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 255.46  E-value: 1.46e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  430 NPVVIIRGATGCGKTTQVPQYILDRFIKGGRasDCNIVVTQPRRISAVSVAERVAYERAEDLGKSCGYSVRFESVLPrPH 509
Cdd:cd17917      1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGG--KGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTS-SK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  510 ASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSATIDTTMFREYFFNSPII 587
Cdd:cd17917     78 TRIKFCTDGILLRELLSDplLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVI 157


                   ..
gi 1927152830  588 EV 589
Cdd:cd17917    158 HI 159
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 414-896 9.53e-73

ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 260.47  E-value: 9.53e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGRasdcnIVVTQPRRISAVSVAERVAYERAEDLGK 493
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGGK-----IIMLEPRRLAARSAAQRLASQLGEAVGQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  494 SCGYSVRFES-VLPRPHASILfcTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPE-VRVILMS 569
Cdd:TIGR01970   76 TVGYRVRGENkVSRRTRLEVV--TEGILTRMIQDdpELDGVGALIFDEFHERSLDADLGLALALDVQSSLREdLKILAMS 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  570 ATIDTTMFREYFFNSPIIEVFGRTFPVQEYFLedciqmtnfippPMDRKKKdkdeeggeddtncnvicgpeysaetkrsm 649
Cdd:TIGR01970  154 ATLDGERLSSLLPDAPVVESEGRSFPVEIRYL------------PLRGDQR----------------------------- 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  650 aqineketsfeLVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLetNPHFGSnRYRILPLHSQIPREEQRRVFEPV 727
Cdd:TIGR01970  193 -----------LEDAVSRAVEHAlaSETGSILVFLPGQAEIRRVQEQL--AERLDS-DVLICPLYGELSLAAQDRAIKPD 258

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  728 PDNITKVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSHARF 807
Cdd:TIGR01970  259 PQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQH 338

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  808 ERLETHMTPEIFRTPLheVALSIKLLRLGAIGHFLSKAIEPPPLDAVIEAEHTLKELDALDSNDELTPLGRILARLPIEP 887
Cdd:TIGR01970  339 QRLPAQDEPEILQADL--SGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHP 416


                   ....*....
gi 1927152830  888 RLGKMMIMG 896
Cdd:TIGR01970  417 RLAAMLLSA 425
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 414-589 3.56e-72

DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350734 [Multi-domain]  Cd Length: 178  Bit Score: 238.15  E-value: 3.56e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGRASDCNIVVTQPRRISAVSVAERVAYERAEDLGK 493
Cdd:cd17976      1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  494 SCGYSVRFESVLPRPHASILFCTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSAT 571
Cdd:cd17976     81 NVGYQVRLESRPPPRGGALLFCTVGVLLKKLQsnPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160

                          170
                   ....*....|....*...
gi 1927152830  572 IDTTMFREYFFNSPIIEV 589
Cdd:cd17976    161 GDNQRLSRYFGGCPVVRV 178
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 412-912 7.76e-70

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 257.68  E-value: 7.76e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  412 DQLPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILD--RFIKGgrasdcNIVVTQPRRISAVSVAERVAYERAE 489
Cdd:PRK11131    71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLElgRGVKG------LIGHTQPRRLAARTVANRIAEELET 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  490 DLGKSCGYSVRFESvlprpHAS----ILFCTVGVLLRKLEAGiRGISH---VIVDEIHERDINTDFLMVVLRDVVQAYPE 562
Cdd:PRK11131   145 ELGGCVGYKVRFND-----QVSdntmVKLMTDGILLAEIQQD-RLLMQydtIIIDEAHERSLNIDFILGYLKELLPRRPD 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  563 VRVILMSATIDTTMFREYFFNSPIIEVFGRTFPVQeyfledciqmTNFIPPPMDRKKKDKDEeggeddtncnvicgpeys 642
Cdd:PRK11131   219 LKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVE----------VRYRPIVEEADDTERDQ------------------ 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  643 aetkrsmaqineketsfelVEALLRYIETLQV--AGAVLIFLPGWNLIYSMQRHLETN--PHfgsnrYRILPLHSQIPRE 718
Cdd:PRK11131   271 -------------------LQAIFDAVDELGRegPGDILIFMSGEREIRDTADALNKLnlRH-----TEILPLYARLSNS 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  719 EQRRVFEPVPDNitKVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFC 798
Cdd:PRK11131   327 EQNRVFQSHSGR--RIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGIC 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  799 FHLCSHARFERLETHMTPEIFRTPLHEVALSIKLLRLGAIGHFlsKAIEPPPLDAVIEAEHTLKELDALDSND-----EL 873
Cdd:PRK11131   405 IRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEELGAITTDEqasayKL 482

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1927152830  874 TPLGRILARLPIEPRLGKMMI----MGCIFHVgdaMCTISAAS 912
Cdd:PRK11131   483 TPLGRQLAQLPVDPRLARMVLeaqkHGCVREV---MIITSALS 522
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 594-802 5.43e-69

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 228.96  E-value: 5.43e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  594 FPVQEYFLEDCIQMTNfipppmdrkkkdkdeeggeddtncnvicgpeysaetkrsMAQINEKETSFELVEALLRYIETLQ 673
Cdd:cd18791      1 FPVEVYYLEDILELLG---------------------------------------ISSEKEDPDYVDAAVRLILQIHRTE 41

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  674 VAGAVLIFLPGWNLIYSMQRHLETNPHFGS-NRYRILPLHSQIPREEQRRVFEPVPDNITKVILSTNIAETSITINDVVY 752
Cdd:cd18791     42 EPGDILVFLPGQEEIERLCELLREELLSPDlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVY 121

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1927152830  753 VIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLC 802
Cdd:cd18791    122 VIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 414-589 1.39e-67

DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350739 [Multi-domain]  Cd Length: 180  Bit Score: 225.49  E-value: 1.39e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGRASDCNIVVTQPRRISAVSVAERVAYERAED--L 491
Cdd:cd17981      1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAEScgL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  492 GKSCGYSVRFESVLPRPHASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMS 569
Cdd:cd17981     81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDphLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160

                          170       180
                   ....*....|....*....|
gi 1927152830  570 ATIDTTMFREYFFNSPIIEV 589
Cdd:cd17981    161 ATLNAEKFSDYFNNCPMIHI 180
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 413-894 2.16e-65

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 238.29  E-value: 2.16e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  413 QLPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGRasdcnIVVTQPRRISAVSVAERVAYERAEDLG 492
Cdd:PRK11664     3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLLQHGGINGK-----IIMLEPRRLAARNVAQRLAEQLGEKPG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  493 KSCGYSVRFES-VLPRPHASILfcTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPE-VRVILM 568
Cdd:PRK11664    78 ETVGYRMRAESkVGPNTRLEVV--TEGILTRMIQrdPELSGVGLVILDEFHERSLQADLALALLLDVQQGLRDdLKLLIM 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  569 SATIDTTMFREYFFNSPIIEVFGRTFPVQEYFLedciqmtnfippPMdrKKKDKDEEggeddtncnvicgpeysaetkrS 648
Cdd:PRK11664   156 SATLDNDRLQQLLPDAPVIVSEGRSFPVERRYQ------------PL--PAHQRFDE----------------------A 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  649 MAQineketsfeLVEALLRyietlQVAGAVLIFLPGWNLIYSMQRHLEtnpHFGSNRYRILPLHSQIPREEQRRVFEPVP 728
Cdd:PRK11664   200 VAR---------ATAELLR-----QESGSLLLFLPGVGEIQRVQEQLA---SRVASDVLLCPLYGALSLAEQQKAILPAP 262

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  729 DNITKVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSHARFE 808
Cdd:PRK11664   263 AGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAE 342

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  809 RLETHMTPEIFRTPLHEVALSikLLRLGAigHFLS--KAIEPPPLDAVIEAEHTLKELDALDSNDELTPLGRILARLPIE 886
Cdd:PRK11664   343 RAAAQSEPEILHSDLSGLLLE--LLQWGC--HDPAqlSWLDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGND 418


                   ....*...
gi 1927152830  887 PRLGKMMI 894
Cdd:PRK11664   419 PRLAAMLV 426
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 414-589 4.19e-62

DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350743 [Multi-domain]  Cd Length: 177  Bit Score: 209.70  E-value: 4.19e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGRASDCNIVVTQPRRISAVSVAERVAYERAEDLGK 493
Cdd:cd17985      1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  494 SCGYSVRFESVLPRPhASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSAT 571
Cdd:cd17985     81 SVGYQIRLESVKSSA-TRLLYCTTGVLLRRLEGDptLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSAT 159

                          170
                   ....*....|....*...
gi 1927152830  572 IDTTMFREYFFNSPIIEV 589
Cdd:cd17985    160 LNAELFSDYFNSCPVIHI 177
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 414-589 1.80e-56

DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 193.51  E-value: 1.80e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGraSDCNIVVTQPRRISAVSVAERVAYERAEDLGK 493
Cdd:cd17987      1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANG--IPCRIFCTQPRRLAAIAVAERVAAERGEKIGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  494 SCGYSVRFESVLpRPHASILFCTVGVLLRKLEAG---IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSA 570
Cdd:cd17987     79 TVGYQIRLESRV-SPKTLLTFCTNGVLLRTLMAGdsaLSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSA 157

                          170
                   ....*....|....*....
gi 1927152830  571 TIDTTMFREYFFNSPIIEV 589
Cdd:cd17987    158 ALDVNLFIRYFGSCPVIYI 176
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 414-581 5.76e-54

DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350746 [Multi-domain]  Cd Length: 180  Bit Score: 186.17  E-value: 5.76e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKggRASDCNIVVTQPRRISAVSVAERVAYERAEDLGK 493
Cdd:cd17988      1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYK--RGKYCNIVVTQPRRIAAISIARRVSQEREWTLGS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  494 SCGYSVRFESVLPRpHASILFCTVGVLLRKL--EAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYP-EVRVILMSA 570
Cdd:cd17988     79 LVGYQVGLERPASE-ETRLIYCTTGVLLQKLinNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSrHVKIILMSA 157

                          170
                   ....*....|.
gi 1927152830  571 TIDTTMFREYF 581
Cdd:cd17988    158 TISCKEFADYF 168
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
 414-589 4.20e-52

DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of the 43S pre-initiation complex involved in translation initiation of mRNAs with structured 5'-UTRs. DHX29 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350733 [Multi-domain]  Cd Length: 183  Bit Score: 181.27  E-value: 4.20e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYIL-DRFIKGGRASDCNIVVTQPRRISAVSVAERVAYERAEDLG 492
Cdd:cd17975      1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLeDLLLNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  493 KS-----CGYSVRFESVLPRPhASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRV 565
Cdd:cd17975     81 PGgknslCGYQIRMESRTGEA-TRLLYCTTGVLLRKLQEDglLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHL 159

                          170       180
                   ....*....|....*....|....
gi 1927152830  566 ILMSATIDTTMFREYFFNSPIIEV 589
Cdd:cd17975    160 ILMSATVDCEKFSSYFTHCPILRI 183
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 414-589 4.15e-51

DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350737 [Multi-domain]  Cd Length: 170  Bit Score: 177.63  E-value: 4.15e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDrfikggrASDCNIVVTQPRRISAVSVAERVAYERAEDLGK 493
Cdd:cd17979      1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLA-------AGFRHIACTQPRRIACISLAKRVAFESLNQYGS 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  494 SCGYSVRFESVlPRPHASILFCTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSAT 571
Cdd:cd17979     74 KVAYQIRFERT-RTLATKLLFLTEGLLLRQIQrdASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSAT 152

                          170
                   ....*....|....*...
gi 1927152830  572 IDTTMFREYFFNSPIIEV 589
Cdd:cd17979    153 INIELFSGYFEGAPVVQV 170
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 414-587 1.65e-48

DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438710 [Multi-domain]  Cd Length: 178  Bit Score: 170.61  E-value: 1.65e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGRAsdcnIVVTQPRRISAVSVAERVAYERAEDLGK 493
Cdd:cd17978      1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGM----IGITQPRRVAAVSVAKRVAEEMGVELGQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  494 SCGYSVRFESVlPRPHASILFCTVGVLLRK--LEAGIRGISHVIVDEIHERDINTDFLMVVLRDV-----VQAYPEVRVI 566
Cdd:cd17978     77 LVGYSVRFDDV-TSEETRIKYMTDGMLLREaiGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAqrrrkEQKLSPLKVI 155

                          170       180
                   ....*....|....*....|.
gi 1927152830  567 LMSATIDTTMFREYFFNSPII 587
Cdd:cd17978    156 IMSATLDADLFSEYFNGAPVL 176
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
 402-589 6.63e-45

DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. DHX15 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438709 [Multi-domain]  Cd Length: 187  Bit Score: 160.66  E-value: 6.63e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  402 ENLQKILSERDQLPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGRASdcNIVVTQPRRISAVSVAE 481
Cdd:cd17973      1 QRYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKK--LVACTQPRRVAAMSVAQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  482 RVAYERAEDLGKSCGYSVRFESvLPRPHASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQA 559
Cdd:cd17973     79 RVAEEMDVKLGEEVGYSIRFED-CSSAKTILKYMTDGMLLREAMSDplLSRYSVIILDEAHERTLATDILMGLLKEVVRR 157

                          170       180       190
                   ....*....|....*....|....*....|
gi 1927152830  560 YPEVRVILMSATIDTTMFREYFFNSPIIEV 589
Cdd:cd17973    158 RPDLKLIVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 414-584 8.24e-44

DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350738 [Multi-domain]  Cd Length: 185  Bit Score: 157.63  E-value: 8.24e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDR-FIKGGRAsdcnIVVTQPRRISAVSVAERVAYERAEDLG 492
Cdd:cd17980      1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAgWTAGGRV----VGCTQPRRVAAVTVAGRVAEEMGAVLG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  493 KSCGYSVRFESVLPRPHASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSA 570
Cdd:cd17980     77 HEVGYCIRFDDCTDPQATRIKFLTDGMLVREMMLDplLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASA 156

                          170
                   ....*....|....
gi 1927152830  571 TIDTTMFREyFFNS 584
Cdd:cd17980    157 TLDAEKFRD-FFNQ 169
DSRM_DHX9_rpt1 cd19854
first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; ...
 3-71 1.70e-43

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: 152.04  E-value: 1.70e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927152830    3 DIKNFLYAWCGKKKLTPNYDIRAAGNKNRQKFMCEVRVDGFNYIGMGNSTNKKDAQTNAARDFVNYLVR 71
Cdd:cd19854      1 EIKAFLYAWCGKKKLTPEYDIKEAGNKHRQRFKCEVRVEGFDYVGTGNATNKKDAQTNAARDFLNYLVR 69
DSRM_DHX9_rpt2 cd19855
second double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; ...
 204-278 2.96e-43

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


Pssm-ID: 380684  Cd Length: 75  Bit Score: 151.60  E-value: 2.96e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927152830  204 LENAKARLNQFFQKEKTSAEYKYSQVGPDHNRSFIAEMQLFVRQLGRRITAREHGSNKKLAAQSCALSLVRQLYH 278
Cdd:cd19855      1 LDNAKSRLNEFLQKNKIPAEYKYTSVGPDHNRSFIAELSIFVKQLGKTIYARETGSNKKLASQSCALSLVRQLYH 75
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
 414-589 3.40e-42

DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpA belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350747 [Multi-domain]  Cd Length: 173  Bit Score: 152.22  E-value: 3.40e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRfikgGRASDCNIVVTQPRRISAVSVAERVAYERAEDLGK 493
Cdd:cd17989      1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLEL----GRGIRGLIGHTQPRRLAARSVAERIAEELKTELGG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  494 SCGYSVRFESVLpRPHASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSAT 571
Cdd:cd17989     77 AVGYKVRFTDQT-SDETCVKLMTDGILLAETQTDryLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSAT 155

                          170
                   ....*....|....*...
gi 1927152830  572 IDTTMFREYFFNSPIIEV 589
Cdd:cd17989    156 IDAERFSRHFNNAPIIEV 173
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
 410-589 6.09e-42

DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350729 [Multi-domain]  Cd Length: 179  Bit Score: 151.87  E-value: 6.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  410 ERDQLPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYIldrfIKGGRASDCNIVVTQPRRISAVSVAERVAYERAE 489
Cdd:cd17971      2 QRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYL----AEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  490 DLGKSCGYSVRFESVlPRPHASILFCTVGVLLRK--LEAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVIL 567
Cdd:cd17971     78 CLGQEVGYTIRFEDC-TSPETVIKYMTDGMLLREclIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIV 156

                          170       180
                   ....*....|....*....|..
gi 1927152830  568 MSATIDTTMFREYFFNSPIIEV 589
Cdd:cd17971    157 TSATLDAVKFSQYFYEAPIFTI 178
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 414-589 1.90e-41

DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350732 [Multi-domain]  Cd Length: 174  Bit Score: 150.35  E-value: 1.90e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDR-FIKGGRASDCnivvTQPRRISAVSVAERVAYERAEDLG 492
Cdd:cd17974      1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAgYTKGGGKIGC----TQPRRVAAMSVAARVAEEMGVKLG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  493 KSCGYSVRFESVlPRPHASILFCTVGVLLRKL--EAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSA 570
Cdd:cd17974     77 NEVGYSIRFEDC-TSEKTVLKYMTDGMLLREFltEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSA 155

                          170
                   ....*....|....*....
gi 1927152830  571 TIDTTMFREYFFNSPIIEV 589
Cdd:cd17974    156 TMDAEKFSAFFDDAPIFRI 174
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
 414-589 5.95e-40

DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350740 [Multi-domain]  Cd Length: 191  Bit Score: 146.73  E-value: 5.95e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDR-FIKGGRASDCNIVVTQPRRISAVSVAERVAYERAeDLG 492
Cdd:cd17982      1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAgFGSPESDNPGMIGITQPRRVAAVSMAKRVAEELN-VFG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  493 KSCGYSVRFESVLpRPHASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVV-----------QA 559
Cdd:cd17982     80 KEVSYQIRYDSTV-SENTKIKFMTDGVLLKEIQTDflLRKYSVIIIDEAHERSVNTDILIGMLSRIVplraklylqdqTV 158

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1927152830  560 YPeVRVILMSATIDTTMFRE--YFFNS--PIIEV 589
Cdd:cd17982    159 KP-LKLVIMSATLRVEDFTEnkLLFPRppPVIKV 191
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
 414-589 1.36e-38

DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as PRP16) is involved in pre-mRNA splicing. DHX38 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350741 [Multi-domain]  Cd Length: 173  Bit Score: 142.22  E-value: 1.36e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYIL-DRFIKGGRasdcnIVVTQPRRISAVSVAERVAYERAEDLG 492
Cdd:cd17983      1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHeDGYTDYGM-----IGCTQPRRVAAMSVAKRVSEEMGVELG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  493 KSCGYSVRFESVlPRPHASILFCTVGVLLRK--LEAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILMSA 570
Cdd:cd17983     76 EEVGYAIRFEDC-TSENTVIKYMTDGILLREslRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSA 154

                          170
                   ....*....|....*....
gi 1927152830  571 TIDTTMFREYFFNSPIIEV 589
Cdd:cd17983    155 TMDADKFADFFGNVPIFTI 173
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 414-589 1.35e-37

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 139.00  E-value: 1.35e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRF-IKGGRasdcnIVVTQPRRISAVSVAERVAYERAEDLG 492
Cdd:cd17990      1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELwIAGGK-----IIVLEPRRVAARAAARRLATLLGEAPG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  493 KSCGYSVRFESVLPRpHASILFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAY-PEVRVILMS 569
Cdd:cd17990     76 ETVGYRVRGESRVGR-RTRVEVVTEGVLLRRLQRdpELSGVGAVILDEFHERSLDADLALALLLEVQQLLrDDLRLLAMS 154

                          170       180
                   ....*....|....*....|
gi 1927152830  570 ATIDTTMFREYFFNSPIIEV 589
Cdd:cd17990    155 ATLDGDGLAALLPEAPVVES 174
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
 414-589 1.48e-32

DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350742 [Multi-domain]  Cd Length: 178  Bit Score: 124.97  E-value: 1.48e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILdrfiKGGRASDCNIVVTQPRRISAVSVAERVAYERAEDLGK 493
Cdd:cd17984      1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLY----EAGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  494 SCGYSVRFESVLPRPHAsILFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYP-----EVRVI 566
Cdd:cd17984     77 KVGYQVRFDDCSSKETA-IKYMTDGCLLRHILAdpNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVV 155

                          170       180
                   ....*....|....*....|...
gi 1927152830  567 LMSATIDTTMFREYFFNSPIIEV 589
Cdd:cd17984    156 VMSATLELAKLSAFFGNCPVFDI 178
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 433-571 3.50e-26

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 105.56  E-value: 3.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  433 VIIRGATGCGKTTQVPQYILDRFIKGGrasdCNIVVTQPRRISAVSVAERvaYERAEDLGKSCGYSVRFESVLPR----- 507
Cdd:cd00046      4 VLITAPTGSGKTLAALLAALLLLLKKG----KKVLVLVPTKALALQTAER--LRELFGPGIRVAVLVGGSSAEEReknkl 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927152830  508 PHASILFCTVGVLLRKLEA----GIRGISHVIVDEIHERDINTDF-LMVVLRDVVQAYPEVRVILMSAT 571
Cdd:cd00046     78 GDADIIIATPDMLLNLLLRedrlFLKDLKLIIVDEAHALLIDSRGaLILDLAVRKAGLKNAQVILLSAT 146
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
 414-589 2.01e-23

DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 98.74  E-value: 2.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDrFIKGGRASDCNIVVTQPRRISAVSVAERVAYERAEDLGK 493
Cdd:cd17977      1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAE-YCLSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIGH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  494 SCGYSVRFESVLPrpHASIL-FCTVGVLLRKLEA----GIRGIshVIVDEIHERDINTDFLMVVLRDVVQAYPEVRVILM 568
Cdd:cd17977     80 EVGYVIPFENCCT--NETILrYCTDDMLLREMMSdpllESYGV--IILDDAHERTVSTDVLLGLLKDVLLSRPELKLVII 155

                          170       180
                   ....*....|....*....|.
gi 1927152830  569 SATIDTTMFREYFFNSPIIEV 589
Cdd:cd17977    156 TCPHLSSKLLSYYGNVPLIEV 176
DEXDc smart00487
DEAD-like helicases superfamily;
423-595 7.51e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.95  E-value: 7.51e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830   423 IMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGrasDCNIVVTQPRRISAVSVAERVAYERAEDLGKSCGY----- 497
Cdd:smart00487   17 IEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK---GGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLyggds 93

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830   498 SVRFESVLPRPHASILFCTVGVLLRKLEAG---IRGISHVIVDEIHERDiNTDFLMVVLRDVVQAYPEVRVILMSATI-- 572
Cdd:smart00487   94 KREQLRKLESGKTDILVTTPGRLLDLLENDklsLSNVDLVILDEAHRLL-DGGFGDQLEKLLKLLPKNVQLLLLSATPpe 172

                           170       180
                    ....*....|....*....|...
gi 1927152830   573 DTTMFREYFFNSPIIEVFGRTFP 595
Cdd:smart00487  173 EIENLLELFLNDPVFIDVGFTPL 195
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 863-944 8.70e-22

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 90.41  E-value: 8.70e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830   863 ELDALDSNDELTPLGRILARLPIEPRLGKMMIMGCIFHVGDAMCTISAASCFPEPFVSE-GKRLGFVHRNFSGSRfSDHV 941
Cdd:smart00847    1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEkREDADAARRRFADPE-SDHL 79


                    ...
gi 1927152830   942 ALL 944
Cdd:smart00847   80 TLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 857-943 2.00e-20

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 87.29  E-value: 2.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  857 AEHTLKELDALDSNDELTPLGRILARLPIEPRLGKMMIMGCIFHVGDAMCTISAASCFPEPFVSEG-------------- 922
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNfldprsaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 1927152830  923 KRLGF--VHRNFSGSRF-SDHVAL 943
Cdd:pfam04408   81 RRAADekARAKFARLDLeGDHLTL 104
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
 414-589 2.15e-20

DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 (DQX1) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350744 [Multi-domain]  Cd Length: 177  Bit Score: 89.96  E-value: 2.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  414 LPVKQFEEEIMATIDSNP-VVIIRGATGCGKTTQVPQYILD-----RFIKGgrasdcNIVVTQPRRISAVSVAERVAYER 487
Cdd:cd17986      1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEfalsrGFQKG------QVTVTQPHPLAARSLALRVADEM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  488 AEDLGKSCGYSVRFESVLPrPHASILFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRV 565
Cdd:cd17986     75 DLNLGHEVGYSIPQEDCTG-PNTILRFCWDRLLLQEMTStpLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRV 153

                          170       180
                   ....*....|....*....|....
gi 1927152830  566 ILMSATIDTTMFREYFFNSPIIEV 589
Cdd:cd17986    154 VVVTSPALEPKLRAFWGNPPVVHV 177
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 422-796 2.85e-20

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 96.97  E-value: 2.85e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  422 EIMATIDSNPVVIIRGATGCGKTTQVPQYIL---------DRFIKGGR-ASDCNIVVTQPRrisavsvaerVAYER--AE 489
Cdd:PHA02653   171 KIFEAWISRKPVVLTGGTGVGKTSQVPKLLLwfnylfggfDNLDKIDPnFIERPIVLSLPR----------VALVRlhSI 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  490 DLGKSCGY--------SVRFESVL-------PRPHAsILFCTVGVLLRKLeagiRGISHVIVDEIHERDINTDFLMVVLR 554
Cdd:PHA02653   241 TLLKSLGFdeidgspiSLKYGSIPdelintnPKPYG-LVFSTHKLTLNKL----FDYGTVIIDEVHEHDQIGDIIIAVAR 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  555 dvvQAYPEVR-VILMSATI--DTTMFREYFFNSPIIEVFGRT-FPVQEyfledcIQMTNFIPPPMDRKkkdkdeeggedd 630
Cdd:PHA02653   316 ---KHIDKIRsLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISE------VYVKNKYNPKNKRA------------ 374

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  631 tncnvicgpeYSAETKRSMaqineketsfelVEALLRYieTLQVAGAVLIFLPGWNLIYSMQRHLET-NPHfgsnrYRIL 709
Cdd:PHA02653   375 ----------YIEEEKKNI------------VTALKKY--TPPKGSSGIVFVASVSQCEEYKKYLEKrLPI-----YDFY 425

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  710 PLHSQIPREEQrrVFEPVPDNI-TKVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMtnyatvWASKTNLEQRKG 788
Cdd:PHA02653   426 IIHGKVPNIDE--ILEKVYSSKnPSIIISTPYLESSVTIRNATHVYDTGRVYVPEPFGGKEM------FISKSMRTQRKG 497


                   ....*...
gi 1927152830  789 RAGRVRPG 796
Cdd:PHA02653   498 RVGRVSPG 505
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1019-1098 5.22e-19

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 82.69  E-value: 5.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830 1019 LLTFGLYPNVCYHKEKRKILTT--EGRNALIHKSSVNCpfssHDITYPSPFFVFSEKIRTRAISAKGMTLVSPLQLLLFA 1096
Cdd:pfam07717    4 ALAAGLYPNVARRDPKGKGYTTlsDNQRVFIHPSSVLF----NEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFA 79


                   ..
gi 1927152830 1097 CK 1098
Cdd:pfam07717   80 PH 81
DSRM smart00358
Double-stranded RNA binding motif;
5-69 2.21e-16

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 74.61  E-value: 2.21e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927152830     5 KNFLYAWCGKKKLTPNYD-IRAAGNKNRQKFMCEVRVDGFnYIGMGNSTNKKDAQTNAARDFVNYL 69
Cdd:smart00358    2 KSLLQELAQKRKLPPEYElVKEEGPDHAPRFTVTVKVGGK-RTGEGEGSSKKEAKQRAAEAALRSL 66
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 660-793 5.00e-15

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 72.24  E-value: 5.00e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  660 ELVEALLRYIETLQVaGAVLIFLPgwnliysMQRHLETNPHFGSNRYRILPLHSQIPREEQRRVFEPVPDNITKVILSTN 739
Cdd:pfam00271    1 EKLEALLELLKKERG-GKVLIFSQ-------TKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATD 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1927152830  740 IAETSITINDVVYVIDsckqkvklFTSHNNMTNYatvwasktnlEQRKGRAGRV 793
Cdd:pfam00271   73 VAERGLDLPDVDLVIN--------YDLPWNPASY----------IQRIGRAGRA 108
HELICc smart00490
helicase superfamily c-terminal domain;
700-792 2.91e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.16  E-value: 2.91e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830   700 HFGSNRYRILPLHSQIPREEQRRVFEPVPDNITKVILSTNIAETSITINDVVYVIDSCkqkvklftshnnmtnyatVWAS 779
Cdd:smart00490    6 LLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYD------------------LPWS 67

                            90
                    ....*....|...
gi 1927152830   780 KTNLEQRKGRAGR 792
Cdd:smart00490   68 PASYIQRIGRAGR 80
DSRM smart00358
Double-stranded RNA binding motif;
207-277 7.40e-13

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 64.59  E-value: 7.40e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927152830   207 AKARLNQFFQKEKTSAEYKY-SQVGPDHNRSFIAEMQLfvrqlGRRITAREHGSNKKLAAQSCALSLVRQLY 277
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELvKEEGPDHAPRFTVTVKV-----GGKRTGEGEGSSKKEAKQRAAEAALRSLK 67
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 5-69 3.45e-12

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: 62.63  E-value: 3.45e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927152830    5 KNFLYAWCGKKKLTPNYD-IRAAGNKNRQKFMCEVRVDGFNYiGMGNSTNKKDAQTNAARDFVNYL 69
Cdd:pfam00035    2 KSLLQEYAQKNGKPPPYEyVSEEGPPHSPKFTVTVKVDGKLY-GSGTGSSKKEAEQLAAEKALEKL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 207-276 2.35e-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: 57.63  E-value: 2.35e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927152830  207 AKARLNQFFQKEKTSAEYKY-SQVGPDHNRSFIAEMQLfvrqlGRRITAREHGSNKKLAAQSCALSLVRQL 276
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYvSEEGPPHSPKFTVTVKV-----DGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 421-575 5.19e-08

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 53.79  E-value: 5.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  421 EEIMATIDSNPVVIIRGATGCGKTT--QVPqyILDRFIK---GGRAsdcnIVVTqPRRISAVSVaervaYERAEDLGKSC 495
Cdd:pfam00270    5 AEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKldnGPQA----LVLA-PTRELAEQI-----YEELKKLGKGL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  496 GYSVRFE----------SVLPRPHasILFCTVGVLLR--KLEAGIRGISHVIVDEIHErdINTDFLMVVLRDVV-QAYPE 562
Cdd:pfam00270   73 GLKVASLlggdsrkeqlEKLKGPD--ILVGTPGRLLDllQERKLLKNLKLLVLDEAHR--LLDMGFGPDLEEILrRLPKK 148

                          170
                   ....*....|...
gi 1927152830  563 VRVILMSATIDTT 575
Cdd:pfam00270  149 RQILLLSATLPRN 161
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 11-63 1.09e-07

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: 49.59  E-value: 1.09e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1927152830   11 WCGKKKL-TPNYDIRAAGNKNRQKFMCEVRVDGFNYIGMGNStnKKDAQTNAAR 63
Cdd:cd00048      3 LCQKNKWpPPEYETVEEGGPHNPRFTCTVTVNGQTFEGEGKS--KKEAKQAAAE 54
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 439-573 4.62e-07

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 51.49  E-value: 4.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  439 TGCGKTTQVPQYILDRFIKGGRasdcNIVVTQPRRisAVsVAERVAY--ERAEDLGKSCG--YSVRFESVLPRPHASILF 514
Cdd:cd17921     26 TSSGKTLIAELAILRALATSGG----KAVYIAPTR--AL-VNQKEADlrERFGPLGKNVGllTGDPSVNKLLLAEADILV 98

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927152830  515 CT---VGVLLRKL-EAGIRGISHVIVDEIH-----ERDIntdFLMVVLRDVVQAYPEVRVILMSATID 573
Cdd:cd17921     99 ATpekLDLLLRNGgERLIQDVRLVVVDEAHligdgERGV---VLELLLSRLLRINKNARFVGLSATLP 163
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 211-276 3.16e-06

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: 45.72  E-value: 3.16e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927152830  211 LNQFFQKEKTSAEYKYSQVGPDHNRSFIAemQLFVrqlGRRITAREHGSNKKLAAQSCALSLVRQL 276
Cdd:cd19875      7 LNEYCQKRGLSLEFVDVSVGPDHCPGFTA--SATI---DGIVFASATGTSKKEAKRAAAKLALKKL 67
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
 206-276 3.21e-06

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: 45.95  E-value: 3.21e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927152830  206 NAKARLNQFFQKEKTSA-EYKY-SQVGPDHNRSFIAEMqlfvrQLGRRITAREHGSNKKLAAQSCALSLVRQL 276
Cdd:cd10845      2 DYKTALQEYLQKRGLPLpEYELvEEEGPDHNKTFTVEV-----KVNGKVIGEGTGRSKKEAEQAAAKAALEKL 69
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
 3-69 6.19e-06

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: 45.18  E-value: 6.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927152830    3 DIKNFLYAWC-GKKKLTPNYDIRAA-GNKNRQKFMCEVRVDGfNYIGMGNSTNKKDAQTNAARDFVNYL 69
Cdd:cd10845      2 DYKTALQEYLqKRGLPLPEYELVEEeGPDHNKTFTVEVKVNG-KVIGEGTGRSKKEAEQAAAKAALEKL 69
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
399-796 1.30e-05

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 49.64  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  399 DHDENLQKILSERDQLPVKQFE---------EEIMATIDSNP-VVIIRGATGCGKTTqVPQYILDRFIKGGRAsdcnIVV 468
Cdd:COG1061     59 ERELAEAEALEAGDEASGTSFElrpyqqealEALLAALERGGgRGLVVAPTGTGKTV-LALALAAELLRGKRV----LVL 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  469 TqPRRISAVSVAERVAyeraEDLGKSCGYSVRFESvlprpHASILFCTVGVLLRK--LEAGIRGISHVIVDEIHErdINT 546
Cdd:COG1061    134 V-PRRELLEQWAEELR----RFLGDPLAGGGKKDS-----DAPITVATYQSLARRahLDELGDRFGLVIIDEAHH--AGA 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  547 DflmvVLRDVVQAYPEVRVILMSATIdttmFREYFFNSPIIEVFGRTFpvqEYFLEDCIQMtNFIPPPmdRKKKDKDEEG 626
Cdd:COG1061    202 P----SYRRILEAFPAAYRLGLTATP----FRSDGREILLFLFDGIVY---EYSLKEAIED-GYLAPP--EYYGIRVDLT 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  627 GEDDtncnvicgpEYSAETKRSMAQINEKETsfELVEALLRYIETLQVAGAVLIFLPGWNLIYSMQRHLEtnphfgSNRY 706
Cdd:COG1061    268 DERA---------EYDALSERLREALAADAE--RKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLN------EAGI 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  707 RILPLHSQIPREEQRRVFEPVPDNITKVILSTNIAETSITINDVVYVIdsckqkvkLFTSHnnmtnyatvwASKTNLEQR 786
Cdd:COG1061    331 RAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI--------LLRPT----------GSPREFIQR 392

                          410
                   ....*....|
gi 1927152830  787 KGRAGRVRPG 796
Cdd:COG1061    393 LGRGLRPAPG 402
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 212-269 1.87e-05

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: 43.43  E-value: 1.87e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1927152830  212 NQFFQKEKTSA-EYKYSQVGPDHNRSFIAEMQLfvrqlgRRITAREHGSNKKLAAQSCA 269
Cdd:cd00048      1 NELCQKNKWPPpEYETVEEGGPHNPRFTCTVTV------NGQTFEGEGKSKKEAKQAAA 53
DSRM_Kanadaptin cd19856
double-stranded RNA binding motif of Kanadaptin and similar proteins; Kanadaptin (also known ...
 204-281 6.44e-05

double-stranded RNA binding motif of Kanadaptin and similar proteins; Kanadaptin (also known as human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP)) is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. The double-stranded RNA binding motif (DSRM) is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380685  Cd Length: 86  Bit Score: 42.60  E-value: 6.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  204 LENAKARLNQFFQKEKTSAEYKYSQVGPDHNRSFIAEMQLFVRQL-GRRITAREHGSNKKLAAQ-SCALSLVRQLYHLGV 281
Cdd:cd19856      5 LKDPKKALKGFFDREGEELEYEVEEQGSGRTRKYVCRIELPLDDAsGGPIVAEASVSGKKKEAVvACALEACRILDRHGL 84
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
 12-63 6.75e-05

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: 42.27  E-value: 6.75e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1927152830   12 CGKKKL-TPNYD-IRAAGNKNRQKFMCEVRVDGFNYIGMGNSTNKKDAQTNAAR 63
Cdd:cd19870     12 CNKRKWgPPEFRlVEESGPPHRKHFLFKVVVNGVEYQPSVASGNKKDAKAQAAT 65
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 12-63 4.75e-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: 39.68  E-value: 4.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1927152830   12 CGKKKLTPNYDIRA-AGNKNRQKFMCEVRVDGFNYiGMGNSTNKKDAQTNAAR 63
Cdd:cd20314     11 CQKERLTVKYEEEKrSGPTHKPRFFCKYIIDGKEY-PEGEGKSKKEAKQAAAR 62
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
206-276 8.59e-04

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 42.39  E-value: 8.59e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927152830  206 NAKARLNQFFQKEKTSA-EYK-YSQVGPDHNRSFIAEmqlfVRqLGRRITAREHGSNKKLAAQSCALSLVRQL 276
Cdd:COG0571    158 DYKTALQEWLQARGLPLpEYEvVEEEGPDHAKTFTVE----VL-VGGKVLGEGTGRSKKEAEQAAAKAALEKL 225
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 8-69 1.38e-03

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: 38.40  E-value: 1.38e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927152830    8 LYAWCGKKKLTPNYDIRAAGNKNRQKFMCEVRVDGfNYIGMGNSTNKKDAQTNAARDFVNYL 69
Cdd:cd19875      7 LNEYCQKRGLSLEFVDVSVGPDHCPGFTASATIDG-IVFASATGTSKKEAKRAAAKLALKKL 67
DSRM_PRKRA-like_rpt1 cd19862
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
 8-72 1.39e-03

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


Pssm-ID: 380691 [Multi-domain]  Cd Length: 70  Bit Score: 38.40  E-value: 1.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927152830    8 LYAWCGKKKLTPNYD-IRAAGNKNRQKFMCEVRVDGFNYIGMGNStnKKDAQTNAARDFVNYLVRI 72
Cdd:cd19862      7 LQELCAKRGITPKYElISSEGAVHEPTFTFRVTVGDITATGSGTS--KKKAKHAAAENALEQLKGS 70
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 420-572 5.25e-03

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 39.24  E-value: 5.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  420 EEEIMATIDSNPVVIIRGATGCGKTTQVPQYILDRFIKGGRAsdcniVVTQPRRisAVSVAERVAYERAEDLGKSCGYSV 499
Cdd:cd18028      7 AEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKA-----LYLVPLR--ALASEKYEEFKKLEEIGLKVGIST 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927152830  500 -RFESVLPR-PHASILFCT---VGVLLRKLEAGIRGISHVIVDEIH-----ERDINTDFLMVVLRDVvqaYPEVRVILMS 569
Cdd:cd18028     80 gDYDEDDEWlGDYDIIVATyekFDSLLRHSPSWLRDVGVVVVDEIHlisdeERGPTLESIVARLRRL---NPNTQIIGLS 156


                   ...
gi 1927152830  570 ATI 572
Cdd:cd18028    157 ATI 159
DSRM_RNT1p-like cd19876
double-stranded RNA binding motif of Saccharomyces cerevisiae ribonuclease 3 (RNT1p) and ...
 5-69 5.58e-03

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: 36.93  E-value: 5.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927152830    5 KNFLYAWCGKKKLTPNYDIRAAGNKNRQKFMCEVRVDGfNYIGMGNSTNKKDAQTNAARDFVNYL 69
Cdd:cd19876      5 KQKLYSLIGPASLKPEYVVVKKEGGNDPNYTVACRING-EVLGTGVGRSIKKAGQRAAMSALSNK 68
 
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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