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Conserved domains on  [gi|2007651285|ref|XP_040002005|]
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ATP-dependent RNA helicase A isoform X1 [Xiphias gladius]

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 ...
 345-578 7.21e-157

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: 470.09  E-value: 7.21e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  345 VPWSPPQVNWNPWTSSNIDEGPLAYCTPEQISGDLHDELMCQLEHDDNLQKILAERDQLPVKQFEEEIMAAVDSSPVVII 424
Cdd:cd17972      1 VPWSPPQSNWNPWTSSNIDEGPLAFATPEQISMDLKNELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVII 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  425 RGATGCGKTTQVPQYILDRYIKGGRASDCNIVVTQPRRISAVSVAERVAYERGEDIGKSCGYSVRFESVLPRPHASVLFC 504
Cdd:cd17972     81 RGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRPHASILFC 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2007651285  505 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSATIDTTMFREYYFNCPIIEV 578
Cdd:cd17972    161 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
401-900 9.52e-116

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: 382.51  E-value: 9.52e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  401 DQLPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDR-YIKGGRasdcnIVVTQPRRISAVSVAERVAYERGED 479
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELgWGAGGR-----IGMLEPRRLAARAAAERMAEELGEP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  480 IGKSCGYSVRFESVLpRPHASVLFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAY-PEVRIIL 556
Cdd:COG1643     83 VGETVGYRVRFEDKV-SAATRIEVVTEGILLRELQRdpELEGVDTVIFDEFHERSLNADLLLALLLDLQPALrPDLKLLV 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  557 MSATIDTTMFREYYFNCPIIEVFGRTFPVQeyfledciqmTNFVPPPMDRKkkekdeeggdddtncnlicgpeytaetkh 636
Cdd:COG1643    162 MSATLDAERFARLLGDAPVIESSGRTYPVE----------VRYRPLPADER----------------------------- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  637 smaqineketsfELVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLEtnPHFGSNrYRILPLHSQIPREEQRKVFE 714
Cdd:COG1643    203 ------------DLEDAVADAVREAlaEEPGDILVFLPGEREIRRTAEALR--GRLPPD-TEILPLYGRLSAAEQDRAFA 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  715 PVPDNIRKVILSTNIAETSITINDVVYVIDSCKQKVKLFtSHNN-MTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSH 793
Cdd:COG1643    268 PAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRY-DPRSgVTRLPTERISQASANQRAGRAGRLAPGICYRLWSE 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  794 ARFERLETHMTPEIFRTPLHEVALSIKLLRLGAIGNFlsKAIEPPPLDAVIEAEHTLKELDALDTNDELTPLGRILARLP 873
Cdd:COG1643    347 EDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLP 424

                          490       500
                   ....*....|....*....|....*..
gi 2007651285  874 IEPRLGKMMIMGCIFHVGDAMCTISAA 900
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 1.72e-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: 1.72e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2007651285    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; ...
 193-267 8.96e-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: 150.06  E-value: 8.96e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2007651285  193 LENAKARLNQFFQKEKTSAEYKYSQVGPDHNRSFIAEMQLFVKQLGRRITAREHGSNKKLAAQSCALSLIRQLYH 267
Cdd:cd19855      1 LDNAKSRLNEFLQKNKIPAEYKYTSVGPDHNRSFIAELSIFVKQLGKTIYARETGSNKKLASQSCALSLVRQLYH 75
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1008-1087 2.48e-18

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: 80.76  E-value: 2.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285 1008 LLTFGSYPNVCYHKEKRKILTT--EGRNALIHKSSVNCpfssHDMTYPSPFFVFGEKIRTRAISAKGMTLVSPLQLLLFA 1085
Cdd:pfam07717    4 ALAAGLYPNVARRDPKGKGYTTlsDNQRVFIHPSSVLF----NEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFA 79


                   ..
gi 2007651285 1086 CK 1087
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 ...
 345-578 7.21e-157

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: 470.09  E-value: 7.21e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  345 VPWSPPQVNWNPWTSSNIDEGPLAYCTPEQISGDLHDELMCQLEHDDNLQKILAERDQLPVKQFEEEIMAAVDSSPVVII 424
Cdd:cd17972      1 VPWSPPQSNWNPWTSSNIDEGPLAFATPEQISMDLKNELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVII 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  425 RGATGCGKTTQVPQYILDRYIKGGRASDCNIVVTQPRRISAVSVAERVAYERGEDIGKSCGYSVRFESVLPRPHASVLFC 504
Cdd:cd17972     81 RGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRPHASILFC 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2007651285  505 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSATIDTTMFREYYFNCPIIEV 578
Cdd:cd17972    161 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
401-900 9.52e-116

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 382.51  E-value: 9.52e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  401 DQLPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDR-YIKGGRasdcnIVVTQPRRISAVSVAERVAYERGED 479
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELgWGAGGR-----IGMLEPRRLAARAAAERMAEELGEP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  480 IGKSCGYSVRFESVLpRPHASVLFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAY-PEVRIIL 556
Cdd:COG1643     83 VGETVGYRVRFEDKV-SAATRIEVVTEGILLRELQRdpELEGVDTVIFDEFHERSLNADLLLALLLDLQPALrPDLKLLV 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  557 MSATIDTTMFREYYFNCPIIEVFGRTFPVQeyfledciqmTNFVPPPMDRKkkekdeeggdddtncnlicgpeytaetkh 636
Cdd:COG1643    162 MSATLDAERFARLLGDAPVIESSGRTYPVE----------VRYRPLPADER----------------------------- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  637 smaqineketsfELVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLEtnPHFGSNrYRILPLHSQIPREEQRKVFE 714
Cdd:COG1643    203 ------------DLEDAVADAVREAlaEEPGDILVFLPGEREIRRTAEALR--GRLPPD-TEILPLYGRLSAAEQDRAFA 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  715 PVPDNIRKVILSTNIAETSITINDVVYVIDSCKQKVKLFtSHNN-MTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSH 793
Cdd:COG1643    268 PAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRY-DPRSgVTRLPTERISQASANQRAGRAGRLAPGICYRLWSE 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  794 ARFERLETHMTPEIFRTPLHEVALSIKLLRLGAIGNFlsKAIEPPPLDAVIEAEHTLKELDALDTNDELTPLGRILARLP 873
Cdd:COG1643    347 EDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLP 424

                          490       500
                   ....*....|....*....|....*..
gi 2007651285  874 IEPRLGKMMIMGCIFHVGDAMCTISAA 900
Cdd:COG1643    425 LDPRLARMLLAAAELGCLREAAILAAL 451
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 403-885 2.21e-75

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: 268.17  E-value: 2.21e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKGGRasdcnIVVTQPRRISAVSVAERVAYERGEDIGK 482
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGGK-----IIMLEPRRLAARSAAQRLASQLGEAVGQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  483 SCGYSVRFES-VLPRPHASVLfcTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPE-VRIILMS 558
Cdd:TIGR01970   76 TVGYRVRGENkVSRRTRLEVV--TEGILTRMIQDdpELDGVGALIFDEFHERSLDADLGLALALDVQSSLREdLKILAMS 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  559 ATIDTTMFREYYFNCPIIEVFGRTFPVqeyfledciqmtnfvpppmdrkkkekdeeggdddtncnlicgpeytaETKHSM 638
Cdd:TIGR01970  154 ATLDGERLSSLLPDAPVVESEGRSFPV-----------------------------------------------EIRYLP 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  639 AQINEKetsfeLVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLetNPHFGSnRYRILPLHSQIPREEQRKVFEPV 716
Cdd:TIGR01970  187 LRGDQR-----LEDAVSRAVEHAlaSETGSILVFLPGQAEIRRVQEQL--AERLDS-DVLICPLYGELSLAAQDRAIKPD 258

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  717 PDNIRKVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSHARF 796
Cdd:TIGR01970  259 PQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQH 338

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  797 ERLETHMTPEIFRTPLheVALSIKLLRLGAIGNFLSKAIEPPPLDAVIEAEHTLKELDALDTNDELTPLGRILARLPIEP 876
Cdd:TIGR01970  339 QRLPAQDEPEILQADL--SGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHP 416


                   ....*....
gi 2007651285  877 RLGKMMIMG 885
Cdd:TIGR01970  417 RLAAMLLSA 425
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 583-791 1.61e-70

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: 233.19  E-value: 1.61e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  583 FPVQEYFLEDCIQMTNfvpppmdrkkkekdeeggdddtncnlicgpeytaetkhsMAQINEKETSFELVEALLRYIETLQ 662
Cdd:cd18791      1 FPVEVYYLEDILELLG---------------------------------------ISSEKEDPDYVDAAVRLILQIHRTE 41

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  663 VAGAVLIFLPGWNLIYSMQRHLETNPHFGS-NRYRILPLHSQIPREEQRKVFEPVPDNIRKVILSTNIAETSITINDVVY 741
Cdd:cd18791     42 EPGDILVFLPGQEEIERLCELLREELLSPDlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVY 121

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2007651285  742 VIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLC 791
Cdd:cd18791    122 VIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 402-883 3.57e-70

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 252.54  E-value: 3.57e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  402 QLPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKGGRasdcnIVVTQPRRISAVSVAERVAYERGEDIG 481
Cdd:PRK11664     3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLLQHGGINGK-----IIMLEPRRLAARNVAQRLAEQLGEKPG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  482 KSCGYSVRFES-VLPRPHASVLfcTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPE-VRIILM 557
Cdd:PRK11664    78 ETVGYRMRAESkVGPNTRLEVV--TEGILTRMIQrdPELSGVGLVILDEFHERSLQADLALALLLDVQQGLRDdLKLLIM 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  558 SATIDTTMFREYYFNCPIIEVFGRTFPVqeyfledciqmtnfvpppmdrkkkekdeeggdddtncnlicgpeytaETKHS 637
Cdd:PRK11664   156 SATLDNDRLQQLLPDAPVIVSEGRSFPV-----------------------------------------------ERRYQ 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  638 MAQINEKetsfeLVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLEtnpHFGSNRYRILPLHSQIPREEQRKVFEP 715
Cdd:PRK11664   189 PLPAHQR-----FDEAVARATAELlrQESGSLLLFLPGVGEIQRVQEQLA---SRVASDVLLCPLYGALSLAEQQKAILP 260

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  716 VPDNIRKVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSHAR 795
Cdd:PRK11664   261 APAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQ 340

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  796 FERLETHMTPEIFRTPLHEVALSikLLRLGAIGNFLSKAIEPPPLDAVIEAEHTLKELDALDTNDELTPLGRILARLPIE 875
Cdd:PRK11664   341 AERAAAQSEPEILHSDLSGLLLE--LLQWGCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGND 418


                   ....*...
gi 2007651285  876 PRLGKMMI 883
Cdd:PRK11664   419 PRLAAMLV 426
DSRM_DHX9_rpt1 cd19854
first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; ...
 3-71 1.72e-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: 1.72e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2007651285    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; ...
 193-267 8.96e-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: 150.06  E-value: 8.96e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2007651285  193 LENAKARLNQFFQKEKTSAEYKYSQVGPDHNRSFIAEMQLFVKQLGRRITAREHGSNKKLAAQSCALSLIRQLYH 267
Cdd:cd19855      1 LDNAKSRLNEFLQKNKIPAEYKYTSVGPDHNRSFIAELSIFVKQLGKTIYARETGSNKKLASQSCALSLVRQLYH 75
DEXDc smart00487
DEAD-like helicases superfamily;
412-584 6.04e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.95  E-value: 6.04e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285   412 IMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKGGrasDCNIVVTQPRRISAVSVAERVA----YERGEDIGKSCGYS 487
Cdd:smart00487   17 IEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK---GGRVLVLVPTRELAEQWAEELKklgpSLGLKVVGLYGGDS 93

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285   488 VRFE-SVLPRPHASVLFCTVGVLLRKLEAG---IRGISHVIVDEIHERDiNTDFLMVVLRDVVQAYPEVRIILMSATI-- 561
Cdd:smart00487   94 KREQlRKLESGKTDILVTTPGRLLDLLENDklsLSNVDLVILDEAHRLL-DGGFGDQLEKLLKLLPKNVQLLLLSATPpe 172

                           170       180
                    ....*....|....*....|...
gi 2007651285   562 DTTMFREYYFNCPIIEVFGRTFP 584
Cdd:smart00487  173 EIENLLELFLNDPVFIDVGFTPL 195
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 852-933 5.05e-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: 91.18  E-value: 5.05e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285   852 ELDALDTNDELTPLGRILARLPIEPRLGKMMIMGCIFHVGDAMCTISAASCFPEPFINE-GKRLGFVHRNFAGSRfSDHV 930
Cdd:smart00847    1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEkREDADAARRRFADPE-SDHL 79


                    ...
gi 2007651285   931 ALL 933
Cdd:smart00847   80 TLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 846-932 2.68e-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: 2.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  846 AEHTLKELDALDTNDELTPLGRILARLPIEPRLGKMMIMGCIFHVGDAMCTISAASCFPEPFINEG-------------- 911
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNfldprsaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 2007651285  912 KRLGF--VHRNFAGSRF-SDHVAL 932
Cdd:pfam04408   81 RRAADekARAKFARLDLeGDHLTL 104
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1008-1087 2.48e-18

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: 80.76  E-value: 2.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285 1008 LLTFGSYPNVCYHKEKRKILTT--EGRNALIHKSSVNCpfssHDMTYPSPFFVFGEKIRTRAISAKGMTLVSPLQLLLFA 1085
Cdd:pfam07717    4 ALAAGLYPNVARRDPKGKGYTTlsDNQRVFIHPSSVLF----NEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFA 79


                   ..
gi 2007651285 1086 CK 1087
Cdd:pfam07717   80 PH 81
DSRM smart00358
Double-stranded RNA binding motif;
5-69 2.23e-16

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 74.61  E-value: 2.23e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007651285     5 KNFLYAWCGKKKLTPNYD-IRAAGNKNRQKFMCEVRVDGFnYIGMGNSTNKKDAQTNAARDFVNYL 69
Cdd:smart00358    2 KSLLQELAQKRKLPPEYElVKEEGPDHAPRFTVTVKVGGK-RTGEGEGSSKKEAKQRAAEAALRSL 66
DSRM smart00358
Double-stranded RNA binding motif;
196-266 9.65e-13

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 64.21  E-value: 9.65e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2007651285   196 AKARLNQFFQKEKTSAEYKY-SQVGPDHNRSFIAEmqlfVKqLGRRITAREHGSNKKLAAQSCALSLIRQLY 266
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELvKEEGPDHAPRFTVT----VK-VGGKRTGEGEGSSKKEAKQRAAEAALRSLK 67
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 5-69 3.49e-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: 3.49e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007651285    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 ...
 196-265 1.11e-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: 58.40  E-value: 1.11e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2007651285  196 AKARLNQFFQKEKTSAEYKY-SQVGPDHNRSFIAEMQLfvkqlGRRITAREHGSNKKLAAQSCALSLIRQL 265
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYvSEEGPPHSPKFTVTVKV-----DGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 422-564 6.87e-06

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: 47.62  E-value: 6.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  422 VIIRGATGCGKTT--QVP--QYILDRYiKGGRAsdcnIVVTqPRRISAVSVAERVAyERGEDIGKSC-----GYSVRFE- 491
Cdd:pfam00270   17 VLVQAPTGSGKTLafLLPalEALDKLD-NGPQA----LVLA-PTRELAEQIYEELK-KLGKGLGLKVasllgGDSRKEQl 89

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007651285  492 SVLPRPHasVLFCTVGVLLR--KLEAGIRGISHVIVDEIHErdINTDFLMVVLRDVV-QAYPEVRIILMSATIDTT 564
Cdd:pfam00270   90 EKLKGPD--ILVGTPGRLLDllQERKLLKNLKLLVLDEAHR--LLDMGFGPDLEEILrRLPKKRQILLLSATLPRN 161
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
195-265 4.28e-04

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 43.16  E-value: 4.28e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2007651285  195 NAKARLNQFFQKEKTSA-EYK-YSQVGPDHNRSFIAEmqlfVKqLGRRITAREHGSNKKLAAQSCALSLIRQL 265
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 ...
 345-578 7.21e-157

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: 470.09  E-value: 7.21e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  345 VPWSPPQVNWNPWTSSNIDEGPLAYCTPEQISGDLHDELMCQLEHDDNLQKILAERDQLPVKQFEEEIMAAVDSSPVVII 424
Cdd:cd17972      1 VPWSPPQSNWNPWTSSNIDEGPLAFATPEQISMDLKNELMYQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVII 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  425 RGATGCGKTTQVPQYILDRYIKGGRASDCNIVVTQPRRISAVSVAERVAYERGEDIGKSCGYSVRFESVLPRPHASVLFC 504
Cdd:cd17972     81 RGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRPHASILFC 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2007651285  505 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSATIDTTMFREYYFNCPIIEV 578
Cdd:cd17972    161 TVGVLLRKLEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
401-900 9.52e-116

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 382.51  E-value: 9.52e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  401 DQLPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDR-YIKGGRasdcnIVVTQPRRISAVSVAERVAYERGED 479
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELgWGAGGR-----IGMLEPRRLAARAAAERMAEELGEP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  480 IGKSCGYSVRFESVLpRPHASVLFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAY-PEVRIIL 556
Cdd:COG1643     83 VGETVGYRVRFEDKV-SAATRIEVVTEGILLRELQRdpELEGVDTVIFDEFHERSLNADLLLALLLDLQPALrPDLKLLV 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  557 MSATIDTTMFREYYFNCPIIEVFGRTFPVQeyfledciqmTNFVPPPMDRKkkekdeeggdddtncnlicgpeytaetkh 636
Cdd:COG1643    162 MSATLDAERFARLLGDAPVIESSGRTYPVE----------VRYRPLPADER----------------------------- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  637 smaqineketsfELVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLEtnPHFGSNrYRILPLHSQIPREEQRKVFE 714
Cdd:COG1643    203 ------------DLEDAVADAVREAlaEEPGDILVFLPGEREIRRTAEALR--GRLPPD-TEILPLYGRLSAAEQDRAFA 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  715 PVPDNIRKVILSTNIAETSITINDVVYVIDSCKQKVKLFtSHNN-MTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSH 793
Cdd:COG1643    268 PAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRY-DPRSgVTRLPTERISQASANQRAGRAGRLAPGICYRLWSE 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  794 ARFERLETHMTPEIFRTPLHEVALSIKLLRLGAIGNFlsKAIEPPPLDAVIEAEHTLKELDALDTNDELTPLGRILARLP 873
Cdd:COG1643    347 EDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLP 424

                          490       500
                   ....*....|....*....|....*..
gi 2007651285  874 IEPRLGKMMIMGCIFHVGDAMCTISAA 900
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) ...
 421-578 1.01e-77

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: 253.15  E-value: 1.01e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  421 VVIIRGATGCGKTTQVPQYILDRYIKGGRasDCNIVVTQPRRISAVSVAERVAYERGEDIGKSCGYSVRFESVLPrPHAS 500
Cdd:cd17917      3 VVVIVGETGSGKTTQVPQFLLEDGLAKGG--KGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTS-SKTR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  501 VLFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSATIDTTMFREYYFNCPIIEV 578
Cdd:cd17917     80 IKFCTDGILLRELLSDplLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 403-885 2.21e-75

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: 268.17  E-value: 2.21e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKGGRasdcnIVVTQPRRISAVSVAERVAYERGEDIGK 482
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGGK-----IIMLEPRRLAARSAAQRLASQLGEAVGQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  483 SCGYSVRFES-VLPRPHASVLfcTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPE-VRIILMS 558
Cdd:TIGR01970   76 TVGYRVRGENkVSRRTRLEVV--TEGILTRMIQDdpELDGVGALIFDEFHERSLDADLGLALALDVQSSLREdLKILAMS 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  559 ATIDTTMFREYYFNCPIIEVFGRTFPVqeyfledciqmtnfvpppmdrkkkekdeeggdddtncnlicgpeytaETKHSM 638
Cdd:TIGR01970  154 ATLDGERLSSLLPDAPVVESEGRSFPV-----------------------------------------------EIRYLP 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  639 AQINEKetsfeLVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLetNPHFGSnRYRILPLHSQIPREEQRKVFEPV 716
Cdd:TIGR01970  187 LRGDQR-----LEDAVSRAVEHAlaSETGSILVFLPGQAEIRRVQEQL--AERLDS-DVLICPLYGELSLAAQDRAIKPD 258

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  717 PDNIRKVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSHARF 796
Cdd:TIGR01970  259 PQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQH 338

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  797 ERLETHMTPEIFRTPLheVALSIKLLRLGAIGNFLSKAIEPPPLDAVIEAEHTLKELDALDTNDELTPLGRILARLPIEP 876
Cdd:TIGR01970  339 QRLPAQDEPEILQADL--SGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHP 416


                   ....*....
gi 2007651285  877 RLGKMMIMG 885
Cdd:TIGR01970  417 RLAAMLLSA 425
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 403-578 2.28e-73

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: 241.62  E-value: 2.28e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKGGRASDCNIVVTQPRRISAVSVAERVAYERGEDIGK 482
Cdd:cd17976      1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  483 SCGYSVRFESVLPRPHASVLFCTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSAT 560
Cdd:cd17976     81 NVGYQVRLESRPPPRGGALLFCTVGVLLKKLQsnPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160

                          170
                   ....*....|....*...
gi 2007651285  561 IDTTMFREYYFNCPIIEV 578
Cdd:cd17976    161 GDNQRLSRYFGGCPVVRV 178
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 583-791 1.61e-70

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: 233.19  E-value: 1.61e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  583 FPVQEYFLEDCIQMTNfvpppmdrkkkekdeeggdddtncnlicgpeytaetkhsMAQINEKETSFELVEALLRYIETLQ 662
Cdd:cd18791      1 FPVEVYYLEDILELLG---------------------------------------ISSEKEDPDYVDAAVRLILQIHRTE 41

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  663 VAGAVLIFLPGWNLIYSMQRHLETNPHFGS-NRYRILPLHSQIPREEQRKVFEPVPDNIRKVILSTNIAETSITINDVVY 741
Cdd:cd18791     42 EPGDILVFLPGQEEIERLCELLREELLSPDlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVY 121

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2007651285  742 VIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLC 791
Cdd:cd18791    122 VIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 402-883 3.57e-70

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 252.54  E-value: 3.57e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  402 QLPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKGGRasdcnIVVTQPRRISAVSVAERVAYERGEDIG 481
Cdd:PRK11664     3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLLQHGGINGK-----IIMLEPRRLAARNVAQRLAEQLGEKPG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  482 KSCGYSVRFES-VLPRPHASVLfcTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPE-VRIILM 557
Cdd:PRK11664    78 ETVGYRMRAESkVGPNTRLEVV--TEGILTRMIQrdPELSGVGLVILDEFHERSLQADLALALLLDVQQGLRDdLKLLIM 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  558 SATIDTTMFREYYFNCPIIEVFGRTFPVqeyfledciqmtnfvpppmdrkkkekdeeggdddtncnlicgpeytaETKHS 637
Cdd:PRK11664   156 SATLDNDRLQQLLPDAPVIVSEGRSFPV-----------------------------------------------ERRYQ 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  638 MAQINEKetsfeLVEALLRYIETL--QVAGAVLIFLPGWNLIYSMQRHLEtnpHFGSNRYRILPLHSQIPREEQRKVFEP 715
Cdd:PRK11664   189 PLPAHQR-----FDEAVARATAELlrQESGSLLLFLPGVGEIQRVQEQLA---SRVASDVLLCPLYGALSLAEQQKAILP 260

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  716 VPDNIRKVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFCFHLCSHAR 795
Cdd:PRK11664   261 APAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQ 340

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  796 FERLETHMTPEIFRTPLHEVALSikLLRLGAIGNFLSKAIEPPPLDAVIEAEHTLKELDALDTNDELTPLGRILARLPIE 875
Cdd:PRK11664   341 AERAAAQSEPEILHSDLSGLLLE--LLQWGCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGND 418


                   ....*...
gi 2007651285  876 PRLGKMMI 883
Cdd:PRK11664   419 PRLAAMLV 426
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 401-901 8.01e-68

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 251.52  E-value: 8.01e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  401 DQLPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILD--RYIKGgrasdcNIVVTQPRRISAVSVAERVAYERGE 478
Cdd:PRK11131    71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLElgRGVKG------LIGHTQPRRLAARTVANRIAEELET 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  479 DIGKSCGYSVRFESvlprpHAS----VLFCTVGVLLRKLEAGiRGISH---VIVDEIHERDINTDFLMVVLRDVVQAYPE 551
Cdd:PRK11131   145 ELGGCVGYKVRFND-----QVSdntmVKLMTDGILLAEIQQD-RLLMQydtIIIDEAHERSLNIDFILGYLKELLPRRPD 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  552 VRIILMSATIDTTMFREYYFNCPIIEVFGRTFPVQEYFledciqmtnfvpppmdRKKKEKDEEGGDDDtncnlicgpeyt 631
Cdd:PRK11131   219 LKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRY----------------RPIVEEADDTERDQ------------ 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  632 aetkhsmaqineketsfelVEALLRYIETLQV--AGAVLIFLPGWNLIYSMQRHLETN--PHfgsnrYRILPLHSQIPRE 707
Cdd:PRK11131   271 -------------------LQAIFDAVDELGRegPGDILIFMSGEREIRDTADALNKLnlRH-----TEILPLYARLSNS 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  708 EQRKVFEpvPDNIRKVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMTNYATVWASKTNLEQRKGRAGRVRPGFC 787
Cdd:PRK11131   327 EQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGIC 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  788 FHLCSHARFERLETHMTPEIFRTPLHEVALSIKLLRLGAIGNFlsKAIEPPPLDAVIEAEHTLKELDALDTND-----EL 862
Cdd:PRK11131   405 IRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEELGAITTDEqasayKL 482

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2007651285  863 TPLGRILARLPIEPRLGKMMI----MGCIFHVgdaMCTISAAS 901
Cdd:PRK11131   483 TPLGRQLAQLPVDPRLARMVLeaqkHGCVREV---MIITSALS 522
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 403-578 2.92e-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: 224.34  E-value: 2.92e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKGGRASDCNIVVTQPRRISAVSVAERVAYERGED--I 480
Cdd:cd17981      1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAEScgL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  481 GKSCGYSVRFESVLPRPHASVLFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMS 558
Cdd:cd17981     81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDphLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160

                          170       180
                   ....*....|....*....|
gi 2007651285  559 ATIDTTMFREYYFNCPIIEV 578
Cdd:cd17981    161 ATLNAEKFSDYFNNCPMIHI 180
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 403-578 1.82e-61

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: 207.77  E-value: 1.82e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKGGRASDCNIVVTQPRRISAVSVAERVAYERGEDIGK 482
Cdd:cd17985      1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  483 SCGYSVRFESVLPRPhASVLFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSAT 560
Cdd:cd17985     81 SVGYQIRLESVKSSA-TRLLYCTTGVLLRRLEGDptLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSAT 159

                          170
                   ....*....|....*...
gi 2007651285  561 IDTTMFREYYFNCPIIEV 578
Cdd:cd17985    160 LNAELFSDYFNSCPVIHI 177
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 403-578 1.36e-57

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: 196.59  E-value: 1.36e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKGGraSDCNIVVTQPRRISAVSVAERVAYERGEDIGK 482
Cdd:cd17987      1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANG--IPCRIFCTQPRRLAAIAVAERVAAERGEKIGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  483 SCGYSVRFESVLpRPHASVLFCTVGVLLRKLEAG---IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSA 559
Cdd:cd17987     79 TVGYQIRLESRV-SPKTLLTFCTNGVLLRTLMAGdsaLSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSA 157

                          170
                   ....*....|....*....
gi 2007651285  560 TIDTTMFREYYFNCPIIEV 578
Cdd:cd17987    158 ALDVNLFIRYFGSCPVIYI 176
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
 403-578 4.73e-53

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: 183.96  E-value: 4.73e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYIL-DRYIKGGRASDCNIVVTQPRRISAVSVAERVAYERGEDIG 481
Cdd:cd17975      1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLeDLLLNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  482 KS-----CGYSVRFESVLPRPhASVLFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRI 554
Cdd:cd17975     81 PGgknslCGYQIRMESRTGEA-TRLLYCTTGVLLRKLQEDglLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHL 159

                          170       180
                   ....*....|....*....|....
gi 2007651285  555 ILMSATIDTTMFREYYFNCPIIEV 578
Cdd:cd17975    160 ILMSATVDCEKFSSYFTHCPILRI 183
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 403-577 6.94e-53

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: 183.09  E-value: 6.94e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKggRASDCNIVVTQPRRISAVSVAERVAYERGEDIGK 482
Cdd:cd17988      1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYK--RGKYCNIVVTQPRRIAAISIARRVSQEREWTLGS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  483 SCGYSVRFESVLPRpHASVLFCTVGVLLRKL--EAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYP-EVRIILMSA 559
Cdd:cd17988     79 LVGYQVGLERPASE-ETRLIYCTTGVLLQKLinNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSrHVKIILMSA 157

                          170
                   ....*....|....*...
gi 2007651285  560 TIDTTMFREyYFNCPIIE 577
Cdd:cd17988    158 TISCKEFAD-YFTTPNNP 174
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 403-578 7.60e-49

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: 171.47  E-value: 7.60e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDryikggrASDCNIVVTQPRRISAVSVAERVAYERGEDIGK 482
Cdd:cd17979      1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLA-------AGFRHIACTQPRRIACISLAKRVAFESLNQYGS 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  483 SCGYSVRFESVlPRPHASVLFCTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSAT 560
Cdd:cd17979     74 KVAYQIRFERT-RTLATKLLFLTEGLLLRQIQrdASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSAT 152

                          170
                   ....*....|....*...
gi 2007651285  561 IDTTMFREYYFNCPIIEV 578
Cdd:cd17979    153 INIELFSGYFEGAPVVQV 170
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 403-576 3.92e-47

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: 166.76  E-value: 3.92e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKGGRAsdcnIVVTQPRRISAVSVAERVAYERGEDIGK 482
Cdd:cd17978      1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGM----IGITQPRRVAAVSVAKRVAEEMGVELGQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  483 SCGYSVRFESVlPRPHASVLFCTVGVLLRK--LEAGIRGISHVIVDEIHERDINTDFLMVVLRDV-----VQAYPEVRII 555
Cdd:cd17978     77 LVGYSVRFDDV-TSEETRIKYMTDGMLLREaiGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAqrrrkEQKLSPLKVI 155

                          170       180
                   ....*....|....*....|.
gi 2007651285  556 LMSATIDTTMFREYYFNCPII 576
Cdd:cd17978    156 IMSATLDADLFSEYFNGAPVL 176
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 403-570 3.93e-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: 158.40  E-value: 3.93e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDR-YIKGGRAsdcnIVVTQPRRISAVSVAERVAYERGEDIG 481
Cdd:cd17980      1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAgWTAGGRV----VGCTQPRRVAAVTVAGRVAEEMGAVLG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  482 KSCGYSVRFESVLPRPHASVLFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSA 559
Cdd:cd17980     77 HEVGYCIRFDDCTDPQATRIKFLTDGMLVREMMLDplLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASA 156

                          170
                   ....*....|.
gi 2007651285  560 TIDTTMFREYY 570
Cdd:cd17980    157 TLDAEKFRDFF 167
DSRM_DHX9_rpt1 cd19854
first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; ...
 3-71 1.72e-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: 1.72e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2007651285    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; ...
 193-267 8.96e-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: 150.06  E-value: 8.96e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2007651285  193 LENAKARLNQFFQKEKTSAEYKYSQVGPDHNRSFIAEMQLFVKQLGRRITAREHGSNKKLAAQSCALSLIRQLYH 267
Cdd:cd19855      1 LDNAKSRLNEFLQKNKIPAEYKYTSVGPDHNRSFIAELSIFVKQLGKTIYARETGSNKKLASQSCALSLVRQLYH 75
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
 394-578 1.01e-42

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: 154.50  E-value: 1.01e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  394 QKILAERDQLPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILD-RYIKGGRASdcnIVVTQPRRISAVSVAERV 472
Cdd:cd17973      4 FEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDdELPHQPKKL---VACTQPRRVAAMSVAQRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  473 AYERGEDIGKSCGYSVRFESvLPRPHASVLFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYP 550
Cdd:cd17973     81 AEEMDVKLGEEVGYSIRFED-CSSAKTILKYMTDGMLLREAMSDplLSRYSVIILDEAHERTLATDILMGLLKEVVRRRP 159

                          170       180
                   ....*....|....*....|....*...
gi 2007651285  551 EVRIILMSATIDTTMFREYYFNCPIIEV 578
Cdd:cd17973    160 DLKLIVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
 398-578 2.37e-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: 153.02  E-value: 2.37e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  398 AERDQLPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYIldryIKGGRASDCNIVVTQPRRISAVSVAERVAYERG 477
Cdd:cd17971      1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYL----AEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  478 EDIGKSCGYSVRFESVlPRPHASVLFCTVGVLLRK--LEAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRII 555
Cdd:cd17971     77 CCLGQEVGYTIRFEDC-TSPETVIKYMTDGMLLREclIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLI 155

                          170       180
                   ....*....|....*....|...
gi 2007651285  556 LMSATIDTTMFREYYFNCPIIEV 578
Cdd:cd17971    156 VTSATLDAVKFSQYFYEAPIFTI 178
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 403-578 2.33e-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: 149.96  E-value: 2.33e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDR-YIKGGRASDCnivvTQPRRISAVSVAERVAYERGEDIG 481
Cdd:cd17974      1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAgYTKGGGKIGC----TQPRRVAAMSVAARVAEEMGVKLG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  482 KSCGYSVRFESVlPRPHASVLFCTVGVLLRKL--EAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSA 559
Cdd:cd17974     77 NEVGYSIRFEDC-TSEKTVLKYMTDGMLLREFltEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSA 155

                          170
                   ....*....|....*....
gi 2007651285  560 TIDTTMFREYYFNCPIIEV 578
Cdd:cd17974    156 TMDAEKFSAFFDDAPIFRI 174
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
 403-578 6.33e-41

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: 148.76  E-value: 6.33e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDRyikgGRASDCNIVVTQPRRISAVSVAERVAYERGEDIGK 482
Cdd:cd17989      1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLEL----GRGIRGLIGHTQPRRLAARSVAERIAEELKTELGG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  483 SCGYSVRFESVLpRPHASVLFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSAT 560
Cdd:cd17989     77 AVGYKVRFTDQT-SDETCVKLMTDGILLAETQTDryLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSAT 155

                          170
                   ....*....|....*...
gi 2007651285  561 IDTTMFREYYFNCPIIEV 578
Cdd:cd17989    156 IDAERFSRHFNNAPIIEV 173
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 403-578 3.00e-39

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: 144.01  E-value: 3.00e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDR-YIKGGRasdcnIVVTQPRRISAVSVAERVAYERGEDIG 481
Cdd:cd17990      1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAElWIAGGK-----IIVLEPRRVAARAAARRLATLLGEAPG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  482 KSCGYSVRFESVLPRpHASVLFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAY-PEVRIILMS 558
Cdd:cd17990     76 ETVGYRVRGESRVGR-RTRVEVVTEGVLLRRLQRdpELSGVGAVILDEFHERSLDADLALALLLEVQQLLrDDLRLLAMS 154

                          170       180
                   ....*....|....*....|
gi 2007651285  559 ATIDTTMFREYYFNCPIIEV 578
Cdd:cd17990    155 ATLDGDGLAALLPEAPVVES 174
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
 403-568 1.43e-38

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: 142.49  E-value: 1.43e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILDR-YIKGGRASDCNIVVTQPRRISAVSVAERVAYERGeDIG 481
Cdd:cd17982      1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAgFGSPESDNPGMIGITQPRRVAAVSMAKRVAEELN-VFG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  482 KSCGYSVRFESVLpRPHASVLFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLMVVLRDVV-----------QA 548
Cdd:cd17982     80 KEVSYQIRYDSTV-SENTKIKFMTDGVLLKEIQTDflLRKYSVIIIDEAHERSVNTDILIGMLSRIVplraklylqdqTV 158

                          170       180
                   ....*....|....*....|
gi 2007651285  549 YPeVRIILMSATIDTTMFRE 568
Cdd:cd17982    159 KP-LKLVIMSATLRVEDFTE 177
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
 403-578 1.15e-37

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: 139.52  E-value: 1.15e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYIL-DRYIKGGRasdcnIVVTQPRRISAVSVAERVAYERGEDIG 481
Cdd:cd17983      1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHeDGYTDYGM-----IGCTQPRRVAAMSVAKRVSEEMGVELG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  482 KSCGYSVRFESVlPRPHASVLFCTVGVLLRK--LEAGIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSA 559
Cdd:cd17983     76 EEVGYAIRFEDC-TSENTVIKYMTDGILLREslRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSA 154

                          170
                   ....*....|....*....
gi 2007651285  560 TIDTTMFREYYFNCPIIEV 578
Cdd:cd17983    155 TMDADKFADFFGNVPIFTI 173
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
 403-578 2.55e-33

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: 127.28  E-value: 2.55e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQYILdryiKGGRASDCNIVVTQPRRISAVSVAERVAYERGEDIGK 482
Cdd:cd17984      1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLY----EAGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  483 SCGYSVRFESVLPRPHAsVLFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYP-----EVRII 555
Cdd:cd17984     77 KVGYQVRFDDCSSKETA-IKYMTDGCLLRHILAdpNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVV 155

                          170       180
                   ....*....|....*....|...
gi 2007651285  556 LMSATIDTTMFREYYFNCPIIEV 578
Cdd:cd17984    156 VMSATLELAKLSAFFGNCPVFDI 178
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 422-560 1.34e-24

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: 100.94  E-value: 1.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  422 VIIRGATGCGKTTQVPQYILDRYIKGGrasdCNIVVTQPRRISAVSVAERVAYERGEDIgkSCGYSVRFESVLPR----- 496
Cdd:cd00046      4 VLITAPTGSGKTLAALLAALLLLLKKG----KKVLVLVPTKALALQTAERLRELFGPGI--RVAVLVGGSSAEEReknkl 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2007651285  497 PHASVLFCTVGVLLRKLEA----GIRGISHVIVDEIHERDINTDF-LMVVLRDVVQAYPEVRIILMSAT 560
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 ...
 403-578 3.65e-24

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: 100.67  E-value: 3.65e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDSSPVVIIRGATGCGKTTQVPQY-----ILDRYIKGGrasdcnIVVTQPRRISAVSVAERVAYERG 477
Cdd:cd17977      1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWcaeycLSAHYQHGV------VVCTQVHKQTAVWLALRVADEMD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  478 EDIGKSCGYSVRFESVLPrpHASVL-FCTVGVLLRKLEA----GIRGIshVIVDEIHERDINTDFLMVVLRDVVQAYPEV 552
Cdd:cd17977     75 VNIGHEVGYVIPFENCCT--NETILrYCTDDMLLREMMSdpllESYGV--IILDDAHERTVSTDVLLGLLKDVLLSRPEL 150

                          170       180
                   ....*....|....*....|....*.
gi 2007651285  553 RIILMSATIDTTMFREYYFNCPIIEV 578
Cdd:cd17977    151 KLVIITCPHLSSKLLSYYGNVPLIEV 176
DEXDc smart00487
DEAD-like helicases superfamily;
412-584 6.04e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.95  E-value: 6.04e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285   412 IMAAVDSSPVVIIRGATGCGKTTQVPQYILDRYIKGGrasDCNIVVTQPRRISAVSVAERVA----YERGEDIGKSCGYS 487
Cdd:smart00487   17 IEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK---GGRVLVLVPTRELAEQWAEELKklgpSLGLKVVGLYGGDS 93

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285   488 VRFE-SVLPRPHASVLFCTVGVLLRKLEAG---IRGISHVIVDEIHERDiNTDFLMVVLRDVVQAYPEVRIILMSATI-- 561
Cdd:smart00487   94 KREQlRKLESGKTDILVTTPGRLLDLLENDklsLSNVDLVILDEAHRLL-DGGFGDQLEKLLKLLPKNVQLLLLSATPpe 172

                           170       180
                    ....*....|....*....|...
gi 2007651285   562 DTTMFREYYFNCPIIEVFGRTFP 584
Cdd:smart00487  173 EIENLLELFLNDPVFIDVGFTPL 195
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 852-933 5.05e-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: 91.18  E-value: 5.05e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285   852 ELDALDTNDELTPLGRILARLPIEPRLGKMMIMGCIFHVGDAMCTISAASCFPEPFINE-GKRLGFVHRNFAGSRfSDHV 930
Cdd:smart00847    1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEkREDADAARRRFADPE-SDHL 79


                    ...
gi 2007651285   931 ALL 933
Cdd:smart00847   80 TLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 846-932 2.68e-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: 2.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  846 AEHTLKELDALDTNDELTPLGRILARLPIEPRLGKMMIMGCIFHVGDAMCTISAASCFPEPFINEG-------------- 911
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNfldprsaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 2007651285  912 KRLGF--VHRNFAGSRF-SDHVAL 932
Cdd:pfam04408   81 RRAADekARAKFARLDLeGDHLTL 104
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 411-785 8.17e-20

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 95.43  E-value: 8.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  411 EIMAAVDSSPVVIIRGATGCGKTTQVPQYIL-DRYIKGG---------RASDCNIVVTQPRrisavsvaerVAYER--GE 478
Cdd:PHA02653   171 KIFEAWISRKPVVLTGGTGVGKTSQVPKLLLwFNYLFGGfdnldkidpNFIERPIVLSLPR----------VALVRlhSI 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  479 DIGKSCGY--------SVRFESVL-------PRPHASVlFCTVGVLLRKLeagiRGISHVIVDEIHERDINTDFLMVVLR 543
Cdd:PHA02653   241 TLLKSLGFdeidgspiSLKYGSIPdelintnPKPYGLV-FSTHKLTLNKL----FDYGTVIIDEVHEHDQIGDIIIAVAR 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  544 dvvQAYPEVR-IILMSATI--DTTMFREYYFNCPIIEVFGRT-FPVQEyfledcIQMTNFVPPPMDRKkkekdeeggddd 619
Cdd:PHA02653   316 ---KHIDKIRsLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISE------VYVKNKYNPKNKRA------------ 374

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  620 tncnlicgpeYTAETKHSMaqineketsfelVEALLRYieTLQVAGAVLIFLPGWNLIYSMQRHLET-NPHfgsnrYRIL 698
Cdd:PHA02653   375 ----------YIEEEKKNI------------VTALKKY--TPPKGSSGIVFVASVSQCEEYKKYLEKrLPI-----YDFY 425

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  699 PLHSQIPREEQrkVFEPVPDNIR-KVILSTNIAETSITINDVVYVIDSCKQKVKLFTSHNNMtnyatvWASKTNLEQRKG 777
Cdd:PHA02653   426 IIHGKVPNIDE--ILEKVYSSKNpSIIISTPYLESSVTIRNATHVYDTGRVYVPEPFGGKEM------FISKSMRTQRKG 497


                   ....*...
gi 2007651285  778 RAGRVRPG 785
Cdd:PHA02653   498 RVGRVSPG 505
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
 403-578 1.55e-19

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: 87.65  E-value: 1.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  403 LPVKQFEEEIMAAVDS-SPVVIIRGATGCGKTTQVPQYILDrYIKGGRASDCNIVVTQPRRISAVSVAERVAYERGEDIG 481
Cdd:cd17986      1 LPIWAAKFTFLEQLESpSGIVLVSGEPGSGKSTQVPQWCAE-FALSRGFQKGQVTVTQPHPLAARSLALRVADEMDLNLG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  482 KSCGYSVRFESVLPrPHASVLFCTVGVLLRKLEA--GIRGISHVIVDEIHERDINTDFLMVVLRDVVQAYPEVRIILMSA 559
Cdd:cd17986     80 HEVGYSIPQEDCTG-PNTILRFCWDRLLLQEMTStpLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTS 158

                          170
                   ....*....|....*....
gi 2007651285  560 TIDTTMFREYYFNCPIIEV 578
Cdd:cd17986    159 PALEPKLRAFWGNPPVVHV 177
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1008-1087 2.48e-18

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: 80.76  E-value: 2.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285 1008 LLTFGSYPNVCYHKEKRKILTT--EGRNALIHKSSVNCpfssHDMTYPSPFFVFGEKIRTRAISAKGMTLVSPLQLLLFA 1085
Cdd:pfam07717    4 ALAAGLYPNVARRDPKGKGYTTlsDNQRVFIHPSSVLF----NEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFA 79


                   ..
gi 2007651285 1086 CK 1087
Cdd:pfam07717   80 PH 81
DSRM smart00358
Double-stranded RNA binding motif;
5-69 2.23e-16

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 74.61  E-value: 2.23e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007651285     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, ...
 649-782 4.20e-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: 72.63  E-value: 4.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  649 ELVEALLRYIETLQVaGAVLIFLPgwnliysMQRHLETNPHFGSNRYRILPLHSQIPREEQRKVFEPVPDNIRKVILSTN 728
Cdd:pfam00271    1 EKLEALLELLKKERG-GKVLIFSQ-------TKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATD 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2007651285  729 IAETSITINDVVYVIDsckqkvklFTSHNNMTNYatvwasktnlEQRKGRAGRV 782
Cdd:pfam00271   73 VAERGLDLPDVDLVIN--------YDLPWNPASY----------IQRIGRAGRA 108
HELICc smart00490
helicase superfamily c-terminal domain;
689-781 1.69e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.93  E-value: 1.69e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285   689 HFGSNRYRILPLHSQIPREEQRKVFEPVPDNIRKVILSTNIAETSITINDVVYVIDSCkqkvklftshnnmtnyatVWAS 768
Cdd:smart00490    6 LLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYD------------------LPWS 67

                            90
                    ....*....|...
gi 2007651285   769 KTNLEQRKGRAGR 781
Cdd:smart00490   68 PASYIQRIGRAGR 80
DSRM smart00358
Double-stranded RNA binding motif;
196-266 9.65e-13

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 64.21  E-value: 9.65e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2007651285   196 AKARLNQFFQKEKTSAEYKY-SQVGPDHNRSFIAEmqlfVKqLGRRITAREHGSNKKLAAQSCALSLIRQLY 266
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELvKEEGPDHAPRFTVT----VK-VGGKRTGEGEGSSKKEAKQRAAEAALRSLK 67
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 5-69 3.49e-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: 3.49e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007651285    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 ...
 196-265 1.11e-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: 58.40  E-value: 1.11e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2007651285  196 AKARLNQFFQKEKTSAEYKY-SQVGPDHNRSFIAEMQLfvkqlGRRITAREHGSNKKLAAQSCALSLIRQL 265
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYvSEEGPPHSPKFTVTVKV-----DGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 11-63 1.11e-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: 1.11e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2007651285   11 WCGKKKL-TPNYDIRAAGNKNRQKFMCEVRVDGFNYIGMGNStnKKDAQTNAAR 63
Cdd:cd00048      3 LCQKNKWpPPEYETVEEGGPHNPRFTCTVTVNGQTFEGEGKS--KKEAKQAAAE 54
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
 195-265 1.59e-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: 46.72  E-value: 1.59e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2007651285  195 NAKARLNQFFQKEKTSA-EYKY-SQVGPDHNRSFIAEMqlfvkQLGRRITAREHGSNKKLAAQSCALSLIRQL 265
Cdd:cd10845      2 DYKTALQEYLQKRGLPLpEYELvEEEGPDHNKTFTVEV-----KVNGKVIGEGTGRSKKEAEQAAAKAALEKL 69
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 428-562 2.73e-06

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: 49.18  E-value: 2.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  428 TGCGKTTQVPQYILDRYIKGGRasdcNIVVTQPRRisAVsVAERVAY--ERGEDIGKSCG--YSVRFESVLPRPHASVLF 503
Cdd:cd17921     26 TSSGKTLIAELAILRALATSGG----KAVYIAPTR--AL-VNQKEADlrERFGPLGKNVGllTGDPSVNKLLLAEADILV 98

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2007651285  504 CT---VGVLLRKL-EAGIRGISHVIVDEIH-----ERDIntdFLMVVLRDVVQAYPEVRIILMSATID 562
Cdd:cd17921     99 ATpekLDLLLRNGgERLIQDVRLVVVDEAHligdgERGV---VLELLLSRLLRINKNARFVGLSATLP 163
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 200-265 2.81e-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: 46.11  E-value: 2.81e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007651285  200 LNQFFQKEKTSAEYKYSQVGPDHNRSFIAEmqlfVKqLGRRITAREHGSNKKLAAQSCALSLIRQL 265
Cdd:cd19875      7 LNEYCQKRGLSLEFVDVSVGPDHCPGFTAS----AT-IDGIVFASATGTSKKEAKRAAAKLALKKL 67
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 422-564 6.87e-06

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: 47.62  E-value: 6.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  422 VIIRGATGCGKTT--QVP--QYILDRYiKGGRAsdcnIVVTqPRRISAVSVAERVAyERGEDIGKSC-----GYSVRFE- 491
Cdd:pfam00270   17 VLVQAPTGSGKTLafLLPalEALDKLD-NGPQA----LVLA-PTRELAEQIYEELK-KLGKGLGLKVasllgGDSRKEQl 89

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007651285  492 SVLPRPHasVLFCTVGVLLR--KLEAGIRGISHVIVDEIHErdINTDFLMVVLRDVV-QAYPEVRIILMSATIDTT 564
Cdd:pfam00270   90 EKLKGPD--ILVGTPGRLLDllQERKLLKNLKLLVLDEAHR--LLDMGFGPDLEEILrRLPKKRQILLLSATLPRN 161
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
 3-69 7.63e-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: 44.79  E-value: 7.63e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2007651285    3 DIKNFLYAWC-GKKKLTPNYDIRAA-GNKNRQKFMCEVRVDGfNYIGMGNSTNKKDAQTNAARDFVNYL 69
Cdd:cd10845      2 DYKTALQEYLqKRGLPLPEYELVEEeGPDHNKTFTVEVKVNG-KVIGEGTGRSKKEAEQAAAKAALEKL 69
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 201-258 1.89e-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: 1.89e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2007651285  201 NQFFQKEKTSA-EYKYSQVGPDHNRSFIAEMQLfvkqlgRRITAREHGSNKKLAAQSCA 258
Cdd:cd00048      1 NELCQKNKWPPpEYETVEEGGPHNPRFTCTVTV------NGQTFEGEGKSKKEAKQAAA 53
DSRM_Kanadaptin cd19856
double-stranded RNA binding motif of Kanadaptin and similar proteins; Kanadaptin (also known ...
 193-270 3.73e-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: 43.37  E-value: 3.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  193 LENAKARLNQFFQKEKTSAEYKYSQVGPDHNRSFIAEMQLFVKQL-GRRITAREHGSNKKLAAQ-SCALSLIRQLYHLGV 270
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 6.97e-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: 6.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2007651285   12 CGKKKL-TPNYD-IRAAGNKNRQKFMCEVRVDGFNYIGMGNSTNKKDAQTNAAR 63
Cdd:cd19870     12 CNKRKWgPPEFRlVEESGPPHRKHFLFKVVVNGVEYQPSVASGNKKDAKAQAAT 65
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
423-785 1.13e-04

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 46.56  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  423 IIRGATGCGKTTqVPQYILDRYIKGGRAsdcnIVVTqPRRISAVSVAERvaYERGEDIGKSCGYSvrfesvlPRPHASVL 502
Cdd:COG1061    104 LVVAPTGTGKTV-LALALAAELLRGKRV----LVLV-PRRELLEQWAEE--LRRFLGDPLAGGGK-------KDSDAPIT 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  503 FCTVGVLLRK--LEAGIRGISHVIVDEIHErdINTDflmvVLRDVVQAYPEVRIILMSATIdttmFREYYFNCPIIEVFG 580
Cdd:COG1061    169 VATYQSLARRahLDELGDRFGLVIIDEAHH--AGAP----SYRRILEAFPAAYRLGLTATP----FRSDGREILLFLFDG 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  581 RTFpvqEYFLEDCIQMtNFVPPP--MDRKKKEKDEEGgdddtncnlicgpEYTAETKHSMAQINEKETsfELVEALLRYI 658
Cdd:COG1061    239 IVY---EYSLKEAIED-GYLAPPeyYGIRVDLTDERA-------------EYDALSERLREALAADAE--RKDKILRELL 299

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  659 ETLQVAGAVLIFLPGWNLIYSMQRHLEtnphfgSNRYRILPLHSQIPREEQRKVFEPVPDNIRKVILSTNIAETSITIND 738
Cdd:COG1061    300 REHPDDRKTLVFCSSVDHAEALAELLN------EAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPR 373

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2007651285  739 VVYVIdsckqkvkLFTSHnnmtnyatvwASKTNLEQRKGRAGRVRPG 785
Cdd:COG1061    374 LDVAI--------LLRPT----------GSPREFIQRLGRGLRPAPG 402
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
195-265 4.28e-04

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 43.16  E-value: 4.28e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2007651285  195 NAKARLNQFFQKEKTSA-EYK-YSQVGPDHNRSFIAEmqlfVKqLGRRITAREHGSNKKLAAQSCALSLIRQL 265
Cdd:COG0571    158 DYKTALQEWLQARGLPLpEYEvVEEEGPDHAKTFTVE----VL-VGGKVLGEGTGRSKKEAEQAAAKAALEKL 225
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 12-63 4.80e-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: 4.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2007651285   12 CGKKKLTPNYDIRA-AGNKNRQKFMCEVRVDGFNYiGMGNSTNKKDAQTNAAR 63
Cdd:cd20314     11 CQKERLTVKYEEEKrSGPTHKPRFFCKYIIDGKEY-PEGEGKSKKEAKQAAAR 62
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
 421-578 5.11e-04

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member 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: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 41.77  E-value: 5.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  421 VVIIRGATGCGKTTQV-PQYILDRYIKGGRasdcnIVVTQPRRISAVSVAErvaYERGEDIGKSCGySVRFESVLPRPha 499
Cdd:cd17931      3 LTVLDLHPGAGKTTRVlPQIIREAIKKRLR-----TLVLAPTRVVAAEMYE---ALRGLPIRYRTG-AVKEEHGGNEI-- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007651285  500 sVLFCTVGVLLRKLEAGIRGISH--VIVDEIHERDINTDFLMVVLRDVVQAyPEVRIILMSATIDTTMFREYYFNCPIIE 577
Cdd:cd17931     72 -VDYMCHGTFTCRLLSPKRVPNYnlIIMDEAHFTDPASIAARGYIHTRVEM-GEAAVIFMTATPPGTVTPFPQSNHPIED 149


                   .
gi 2007651285  578 V 578
Cdd:cd17931    150 F 150
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
 8-69 1.39e-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: 1.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2007651285    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 ...
 8-71 1.72e-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: 1.72e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2007651285    8 LYAWCGKKKLTPNYD-IRAAGNKNRQKFMCEVRVDGFNYIGMGNStnKKDAQTNAARDFVNYLVR 71
Cdd:cd19862      7 LQELCAKRGITPKYElISSEGAVHEPTFTFRVTVGDITATGSGTS--KKKAKHAAAENALEQLKG 69
DSRM_RNT1p-like cd19876
double-stranded RNA binding motif of Saccharomyces cerevisiae ribonuclease 3 (RNT1p) and ...
 5-69 5.64e-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: 5.64e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2007651285    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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