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Conserved domains on  [gi|30694379|ref|NP_175298|]
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DEA(D/H)-box RNA helicase family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
299-822 4.05e-120

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: 391.75  E-value: 4.05e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILEseieAARGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:COG1643   10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPR-RPDLKLILMSAT 457
Cdd:COG1643   86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSAT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  458 LNAELFSSYFGGAPAMHIPGFTYPVRAHFLEdyLETSGYRLTTynqiddygeektwkmqkqaqfkkrksLISSAVEDALE 537
Cdd:COG1643  166 LDAERFARLLGDAPVIESSGRTYPVEVRYRP--LPADERDLED--------------------------AVADAVREALA 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  538 aadfkgynfrtrdslscwspdsigfnlienvlchivkgERPGAVLVFMTGWDDINSLKNQLEAHsLLGDpnkVLLLACHG 617
Cdd:COG1643  218 --------------------------------------EEPGDILVFLPGEREIRRTAEALRGR-LPPD---TEILPLYG 255

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  618 SMASSEQRLIFDRPPEGIRKIVLATNMAETSITINDVVYVIDCGKAKETSYDALNNTPCLLPSWISKaaarqrrgragrV 697
Cdd:COG1643  256 RLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQasanqragragrL 335

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  698 MPGECYHLYPRCVYEAFADYQQPELLRTPLQSLCLQIKSLGLGSISEFlsRALQPPEALSVQNAVEYLKIIGALDDDENL 777
Cdd:COG1643  336 APGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRL 413

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 30694379  778 TPLGKNLSMLPVEPKLGKMLILGAIFNCLDPVMTVVAGLSVRDPF 822
Cdd:COG1643  414 TPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR 458
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 916-998 1.79e-21

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: 89.62  E-value: 1.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    916 VRAIICAGMFPGVCSVVNKEKSITLKTmEDGQVLLYSSSVNGNVPMIPFPWLVFNDKVKVNSVFLRDSTAVSDSVLLLFG 995
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLS-DNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFA 79


                   ...
gi 30694379    996 DKI 998
Cdd:pfam07717   80 PHI 82
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 1106-1160 4.14e-06

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: 44.97  E-value: 4.14e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30694379 1106 QTLLARAGHGSPVYKTRQLK---NNQFRSMVTFNGLDFMGKPCgSKKNAEKDAAHEAL 1160
Cdd:cd00048    1 NELCQKNKWPPPEYETVEEGgphNPRFTCTVTVNGQTFEGEGK-SKKEAKQAAAEKAL 57
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
299-822 4.05e-120

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 391.75  E-value: 4.05e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILEseieAARGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:COG1643   10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPR-RPDLKLILMSAT 457
Cdd:COG1643   86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSAT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  458 LNAELFSSYFGGAPAMHIPGFTYPVRAHFLEdyLETSGYRLTTynqiddygeektwkmqkqaqfkkrksLISSAVEDALE 537
Cdd:COG1643  166 LDAERFARLLGDAPVIESSGRTYPVEVRYRP--LPADERDLED--------------------------AVADAVREALA 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  538 aadfkgynfrtrdslscwspdsigfnlienvlchivkgERPGAVLVFMTGWDDINSLKNQLEAHsLLGDpnkVLLLACHG 617
Cdd:COG1643  218 --------------------------------------EEPGDILVFLPGEREIRRTAEALRGR-LPPD---TEILPLYG 255

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  618 SMASSEQRLIFDRPPEGIRKIVLATNMAETSITINDVVYVIDCGKAKETSYDALNNTPCLLPSWISKaaarqrrgragrV 697
Cdd:COG1643  256 RLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQasanqragragrL 335

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  698 MPGECYHLYPRCVYEAFADYQQPELLRTPLQSLCLQIKSLGLGSISEFlsRALQPPEALSVQNAVEYLKIIGALDDDENL 777
Cdd:COG1643  336 APGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRL 413

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 30694379  778 TPLGKNLSMLPVEPKLGKMLILGAIFNCLDPVMTVVAGLSVRDPF 822
Cdd:COG1643  414 TPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR 458
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
 299-895 1.05e-100

RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273900 [Multi-domain]  Cd Length: 1283  Bit Score: 348.30  E-value: 1.05e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILEseieAARGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:TIGR01967   66 LPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLE----LGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGE 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATL 458
Cdd:TIGR01967  142 KVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATI 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    459 NAELFSSYFGGAPAMHIPGFTYPVRahfledyletsgyrlTTYNQIDDYGEEktwkmqkqaqfkkrkslISSAVEDALea 538
Cdd:TIGR01967  222 DPERFSRHFNNAPIIEVSGRTYPVE---------------VRYRPLVEEQED-----------------DDLDQLEAI-- 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    539 adfkgynFRTRDSLScwspdsigfnlienvlchivkGERPGAVLVFMTGWDDINSLKNQLEAHSLLGdpnkVLLLACHGS 618
Cdd:TIGR01967  268 -------LDAVDELF---------------------AEGPGDILIFLPGEREIRDAAEILRKRNLRH----TEILPLYAR 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    619 MASSEQRLIFdRPPEGiRKIVLATNMAETSITINDVVYVIDCGKAKETSYDALNNTPCLLPSWISKAAARQRRGRAGRVM 698
Cdd:TIGR01967  316 LSNKEQQRVF-QPHSG-RRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVA 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    699 PGECYHLYPRCVYEAFADYQQPELLRTPLQSLCLQIKSLGLGSISEFlsRALQPPEALSVQNAVEYLKIIGALDDDE--- 775
Cdd:TIGR01967  394 PGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAF--PFIEAPDPRAIRDGFRLLEELGALDDDEaep 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    776 NLTPLGKNLSMLPVEPKLGKMLILGAIFNCLDPVMTVVAGLSVRDPFLMPFDKKDLAETARSKFSGRDySDHLTLVRAYN 855
Cdd:TIGR01967  472 QLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPR-SDFLSRVNLWR 550

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 30694379    856 GWKDAErthsgydycwKNFLSSQTLKAmdsMRKQFFNLLK 895
Cdd:TIGR01967  551 HIEEQR----------QALSANQFRNA---CRKQYLNYLR 577
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 261-876 1.13e-95

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 333.95  E-value: 1.13e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   261 NSLARERILRPRSLQLKSKQQQWVDSPEGQKMVGFRKTLPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILEse 340
Cdd:PRK11131   35 NPDAQQAIFQEIAKEIAQAAQRVLLREAARPEITYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE-- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   341 ieAARGATCSIICTQPRRISAISVSERVAAERGEQIGESVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHV 420
Cdd:PRK11131  113 --LGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTI 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   421 VVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATLNAELFSSYFGGAPAMHIPGFTYPVRahfledyletsgyrlTT 500
Cdd:PRK11131  191 IIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVE---------------VR 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   501 YNQIDDyGEEKTWKMQKQAqfkkrkslISSAVEDaleaadfkgynfrtrdslscwspdsigfnlienvLCHivkgERPGA 580
Cdd:PRK11131  256 YRPIVE-EADDTERDQLQA--------IFDAVDE----------------------------------LGR----EGPGD 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   581 VLVFMTGWDDINSLKNQLEAHSLLGdpNKVLLLacHGSMASSEQRLIFDrpPEGIRKIVLATNMAETSITINDVVYVIDC 660
Cdd:PRK11131  289 ILIFMSGEREIRDTADALNKLNLRH--TEILPL--YARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDP 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   661 GKAKETSYDALNNTPCLLPSWISKAAARQRRGRAGRVMPGECYHLYPRCVYEAFADYQQPELLRTPLQSLCLQIKSLGLG 740
Cdd:PRK11131  363 GTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLG 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   741 SISEFlsRALQPPEALSVQNAVEYLKIIGALDDDEN-----LTPLGKNLSMLPVEPKLGKMLILGAIFNCLDPVMTVVAG 815
Cdd:PRK11131  443 DIAAF--PFVEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSA 520

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694379   816 LSVRDPFLMPFDKKDLAETARSKFSGRDySDHLTLVRAYNGWKDAERTHSGYDY---CWKNFLS 876
Cdd:PRK11131  521 LSIQDPRERPMDKQQASDEKHRRFADKE-SDFLAFVNLWNYLQEQQKALSSNQFrrlCRTDYLN 583
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 315-475 6.44e-94

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: 297.06  E-value: 6.44e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  315 NQVVVVSGETGCGKTTQLPQYILESEIeaARGATCSIICTQPRRISAISVSERVAAERGEQIGESVGYKVRLEGMRGRDT 394
Cdd:cd17917    1 NQVVVIVGETGSGKTTQVPQFLLEDGL--AKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  395 RLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATLNAELFSSYFGGAPAMH 474
Cdd:cd17917   79 RIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIH 158


                 .
gi 30694379  475 I 475
Cdd:cd17917  159 I 159
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 761-850 4.45e-31

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: 117.72  E-value: 4.45e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    761 AVEYLKIIGALDDDENLTPLGKNLSMLPVEPKLGKMLILGAIFNCLDPVMTVVAGLSVRDPFLMPFD------------- 827
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 30694379    828 KKDLAETARSKFSGRD-YSDHLTL 850
Cdd:pfam04408   81 RRAADEKARAKFARLDlEGDHLTL 104
DEXDc smart00487
DEAD-like helicases superfamily;
305-481 3.51e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 107.19  E-value: 3.51e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379     305 KDALLKAIAANQVVVVSGETGCGKTTQLPQYILESeieAARGATCSIICTQPRRISAISVSERVAAERGEQIGESVGY-- 382
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEA---LKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLyg 90

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379     383 ----KVRLEGMRGRDTRLLFCTTGVLLRRLLVDR-SLKGVTHVVVDEIHERGmNEDFLLIVLKDLLPRRPDLKLILMSAT 457
Cdd:smart00487   91 gdskREQLRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLL-DGGFGDQLEKLLKLLPKNVQLLLLSAT 169

                           170       180
                    ....*....|....*....|....*.
gi 30694379     458 L--NAELFSSYFGGAPAMHIPGFTYP 481
Cdd:smart00487  170 PpeEIENLLELFLNDPVFIDVGFTPL 195
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 916-998 1.79e-21

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: 89.62  E-value: 1.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    916 VRAIICAGMFPGVCSVVNKEKSITLKTmEDGQVLLYSSSVNGNVPMIPFPWLVFNDKVKVNSVFLRDSTAVSDSVLLLFG 995
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLS-DNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFA 79


                   ...
gi 30694379    996 DKI 998
Cdd:pfam07717   80 PHI 82
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 1106-1160 4.14e-06

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: 44.97  E-value: 4.14e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30694379 1106 QTLLARAGHGSPVYKTRQLK---NNQFRSMVTFNGLDFMGKPCgSKKNAEKDAAHEAL 1160
Cdd:cd00048    1 NELCQKNKWPPPEYETVEEGgphNPRFTCTVTVNGQTFEGEGK-SKKEAKQAAAEKAL 57
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 1102-1163 5.94e-06

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: 44.91  E-value: 5.94e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694379   1102 KNQLQTLLARAGHGSPVYKTRQL---KNNQFRSMVTFNGLDFMGKPCGSKKNAEKDAAHEALLWL 1163
Cdd:pfam00035    2 KSLLQEYAQKNGKPPPYEYVSEEgppHSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
1094-1167 8.91e-04

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 42.39  E-value: 8.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694379 1094 QNSGGENNKNQLQTLLARAGHGSPVYKTRQLK----NNQFRSMVTFNGlDFMGKPCG-SKKNAEKDAAHEALLWLQGES 1167
Cdd:COG0571  152 PGGAGKDYKTALQEWLQARGLPLPEYEVVEEEgpdhAKTFTVEVLVGG-KVLGEGTGrSKKEAEQAAAKAALEKLGKKE 229
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
299-822 4.05e-120

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 391.75  E-value: 4.05e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILEseieAARGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:COG1643   10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPR-RPDLKLILMSAT 457
Cdd:COG1643   86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSAT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  458 LNAELFSSYFGGAPAMHIPGFTYPVRAHFLEdyLETSGYRLTTynqiddygeektwkmqkqaqfkkrksLISSAVEDALE 537
Cdd:COG1643  166 LDAERFARLLGDAPVIESSGRTYPVEVRYRP--LPADERDLED--------------------------AVADAVREALA 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  538 aadfkgynfrtrdslscwspdsigfnlienvlchivkgERPGAVLVFMTGWDDINSLKNQLEAHsLLGDpnkVLLLACHG 617
Cdd:COG1643  218 --------------------------------------EEPGDILVFLPGEREIRRTAEALRGR-LPPD---TEILPLYG 255

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  618 SMASSEQRLIFDRPPEGIRKIVLATNMAETSITINDVVYVIDCGKAKETSYDALNNTPCLLPSWISKaaarqrrgragrV 697
Cdd:COG1643  256 RLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQasanqragragrL 335

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  698 MPGECYHLYPRCVYEAFADYQQPELLRTPLQSLCLQIKSLGLGSISEFlsRALQPPEALSVQNAVEYLKIIGALDDDENL 777
Cdd:COG1643  336 APGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRL 413

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 30694379  778 TPLGKNLSMLPVEPKLGKMLILGAIFNCLDPVMTVVAGLSVRDPF 822
Cdd:COG1643  414 TPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR 458
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
 299-895 1.05e-100

RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273900 [Multi-domain]  Cd Length: 1283  Bit Score: 348.30  E-value: 1.05e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILEseieAARGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:TIGR01967   66 LPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLE----LGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGE 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATL 458
Cdd:TIGR01967  142 KVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATI 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    459 NAELFSSYFGGAPAMHIPGFTYPVRahfledyletsgyrlTTYNQIDDYGEEktwkmqkqaqfkkrkslISSAVEDALea 538
Cdd:TIGR01967  222 DPERFSRHFNNAPIIEVSGRTYPVE---------------VRYRPLVEEQED-----------------DDLDQLEAI-- 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    539 adfkgynFRTRDSLScwspdsigfnlienvlchivkGERPGAVLVFMTGWDDINSLKNQLEAHSLLGdpnkVLLLACHGS 618
Cdd:TIGR01967  268 -------LDAVDELF---------------------AEGPGDILIFLPGEREIRDAAEILRKRNLRH----TEILPLYAR 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    619 MASSEQRLIFdRPPEGiRKIVLATNMAETSITINDVVYVIDCGKAKETSYDALNNTPCLLPSWISKAAARQRRGRAGRVM 698
Cdd:TIGR01967  316 LSNKEQQRVF-QPHSG-RRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVA 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    699 PGECYHLYPRCVYEAFADYQQPELLRTPLQSLCLQIKSLGLGSISEFlsRALQPPEALSVQNAVEYLKIIGALDDDE--- 775
Cdd:TIGR01967  394 PGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAF--PFIEAPDPRAIRDGFRLLEELGALDDDEaep 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    776 NLTPLGKNLSMLPVEPKLGKMLILGAIFNCLDPVMTVVAGLSVRDPFLMPFDKKDLAETARSKFSGRDySDHLTLVRAYN 855
Cdd:TIGR01967  472 QLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPR-SDFLSRVNLWR 550

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 30694379    856 GWKDAErthsgydycwKNFLSSQTLKAmdsMRKQFFNLLK 895
Cdd:TIGR01967  551 HIEEQR----------QALSANQFRNA---CRKQYLNYLR 577
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 261-876 1.13e-95

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 333.95  E-value: 1.13e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   261 NSLARERILRPRSLQLKSKQQQWVDSPEGQKMVGFRKTLPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILEse 340
Cdd:PRK11131   35 NPDAQQAIFQEIAKEIAQAAQRVLLREAARPEITYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE-- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   341 ieAARGATCSIICTQPRRISAISVSERVAAERGEQIGESVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHV 420
Cdd:PRK11131  113 --LGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTI 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   421 VVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATLNAELFSSYFGGAPAMHIPGFTYPVRahfledyletsgyrlTT 500
Cdd:PRK11131  191 IIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVE---------------VR 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   501 YNQIDDyGEEKTWKMQKQAqfkkrkslISSAVEDaleaadfkgynfrtrdslscwspdsigfnlienvLCHivkgERPGA 580
Cdd:PRK11131  256 YRPIVE-EADDTERDQLQA--------IFDAVDE----------------------------------LGR----EGPGD 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   581 VLVFMTGWDDINSLKNQLEAHSLLGdpNKVLLLacHGSMASSEQRLIFDrpPEGIRKIVLATNMAETSITINDVVYVIDC 660
Cdd:PRK11131  289 ILIFMSGEREIRDTADALNKLNLRH--TEILPL--YARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDP 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   661 GKAKETSYDALNNTPCLLPSWISKAAARQRRGRAGRVMPGECYHLYPRCVYEAFADYQQPELLRTPLQSLCLQIKSLGLG 740
Cdd:PRK11131  363 GTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLG 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   741 SISEFlsRALQPPEALSVQNAVEYLKIIGALDDDEN-----LTPLGKNLSMLPVEPKLGKMLILGAIFNCLDPVMTVVAG 815
Cdd:PRK11131  443 DIAAF--PFVEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSA 520

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694379   816 LSVRDPFLMPFDKKDLAETARSKFSGRDySDHLTLVRAYNGWKDAERTHSGYDY---CWKNFLS 876
Cdd:PRK11131  521 LSIQDPRERPMDKQQASDEKHRRFADKE-SDFLAFVNLWNYLQEQQKALSSNQFrrlCRTDYLN 583
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 315-475 6.44e-94

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: 297.06  E-value: 6.44e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  315 NQVVVVSGETGCGKTTQLPQYILESEIeaARGATCSIICTQPRRISAISVSERVAAERGEQIGESVGYKVRLEGMRGRDT 394
Cdd:cd17917    1 NQVVVIVGETGSGKTTQVPQFLLEDGL--AKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  395 RLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATLNAELFSSYFGGAPAMH 474
Cdd:cd17917   79 RIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIH 158


                 .
gi 30694379  475 I 475
Cdd:cd17917  159 I 159
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 299-475 8.19e-83

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: 267.48  E-value: 8.19e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIEAARGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:cd17985    1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATL 458
Cdd:cd17985   81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160

                        170
                 ....*....|....*..
gi 30694379  459 NAELFSSYFGGAPAMHI 475
Cdd:cd17985  161 NAELFSDYFNSCPVIHI 177
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 299-475 3.92e-75

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: 246.29  E-value: 3.92e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIEAARGATCSIICTQPRRISAISVSERVAAERGEQ--I 376
Cdd:cd17981    1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAEScgL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  377 GESVGYKVRLEGMRGRD-TRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMS 455
Cdd:cd17981   81 GNSTGYQIRLESRKPRKqGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160

                        170       180
                 ....*....|....*....|
gi 30694379  456 ATLNAELFSSYFGGAPAMHI 475
Cdd:cd17981  161 ATLNAEKFSDYFNNCPMIHI 180
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 273-475 1.13e-70

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: 235.88  E-value: 1.13e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  273 SLQLKSKQQ-QWVDSPEGQKMVGFRKTLPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIEAARGATCSI 351
Cdd:cd17972   32 SMDLKNELMyQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNI 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  352 ICTQPRRISAISVSERVAAERGEQIGESVGYKVRLEGMRGRD-TRLLFCTTGVLLRRLlvDRSLKGVTHVVVDEIHERGM 430
Cdd:cd17972  112 VVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRPhASILFCTVGVLLRKL--EAGIRGISHVIVDEIHERDI 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 30694379  431 NEDFLLIVLKDLLPRRPDLKLILMSATLNAELFSSYFGGAPAMHI 475
Cdd:cd17972  190 NTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 299-475 4.42e-68

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: 226.21  E-value: 4.42e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIEAARGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:cd17976    1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGM-RGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSAT 457
Cdd:cd17976   81 NVGYQVRLESRpPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160

                        170
                 ....*....|....*...
gi 30694379  458 LNAELFSSYFGGAPAMHI 475
Cdd:cd17976  161 GDNQRLSRYFGGCPVVRV 178
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 299-475 9.93e-68

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: 225.48  E-value: 9.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEieAARGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:cd17987    1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDC--YANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLV-DRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSAT 457
Cdd:cd17987   79 TVGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAA 158

                        170
                 ....*....|....*...
gi 30694379  458 LNAELFSSYFGGAPAMHI 475
Cdd:cd17987  159 LDVNLFIRYFGSCPVIYI 176
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 307-801 2.82e-66

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: 240.82  E-value: 2.82e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    307 ALLKAIAANQVVVVSGETGCGKTTQLPQYILeseieAARGATCSIICTQPRRISAISVSERVAAERGEQIGESVGYKVRL 386
Cdd:TIGR01970    9 ALRDALAAHPQVVLEAPPGAGKSTAVPLALL-----DAPGIGGKIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYRVRG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    387 EGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPR-RPDLKLILMSATLNAELFSS 465
Cdd:TIGR01970   84 ENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSATLDGERLSS 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    466 YFGGAPAMHIPGFTYPVRAHFLedyletsgyrlttynqiddygeektwKMQKQAQFKKRkslISSAVEDALEaadfkgyn 545
Cdd:TIGR01970  164 LLPDAPVVESEGRSFPVEIRYL--------------------------PLRGDQRLEDA---VSRAVEHALA-------- 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    546 frtrdslscwspdsigfnlienvlchivkgERPGAVLVFMTGWDDINSLKNQLEahSLLGdpNKVLLLACHGSMASSEQR 625
Cdd:TIGR01970  207 ------------------------------SETGSILVFLPGQAEIRRVQEQLA--ERLD--SDVLICPLYGELSLAAQD 252

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    626 LIFDRPPEGIRKIVLATNMAETSITINDVVYVIDCGKAKETSYDALNNTPCLLPSWISKAAARQRRGRAGRVMPGECYHL 705
Cdd:TIGR01970  253 RAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRL 332

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    706 YPRCVYEAFADYQQPELLRTPLQSLCLQIKSLGLGSISEFlsRALQPPEALSVQNAVEYLKIIGALDDDENLTPLGKNLS 785
Cdd:TIGR01970  333 WSEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDL--RWLDAPPSVALAAARQLLQRLGALDAQGRLTAHGKAMA 410

                          490
                   ....*....|....*.
gi 30694379    786 MLPVEPKLGKMLILGA 801
Cdd:TIGR01970  411 ALGCHPRLAAMLLSAH 426
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
 299-475 2.76e-61

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: 207.46  E-value: 2.76e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILEsEIEAARGAT--CSIICTQPRRISAISVSERVAAERGEQI 376
Cdd:cd17975    1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLE-DLLLNGGTAqkCNIVCTQPRRISAMSLATRVCEELGCES 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  377 GES-----VGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKL 451
Cdd:cd17975   80 GPGgknslCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHL 159

                        170       180
                 ....*....|....*....|....
gi 30694379  452 ILMSATLNAELFSSYFGGAPAMHI 475
Cdd:cd17975  160 ILMSATVDCEKFSSYFTHCPILRI 183
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 299-475 2.63e-60

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: 203.83  E-value: 2.63e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIEaargatcSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:cd17979    1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFR-------HIACTQPRRIACISLAKRVAFESLNQYGS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATL 458
Cdd:cd17979   74 KVAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATI 153

                        170
                 ....*....|....*..
gi 30694379  459 NAELFSSYFGGAPAMHI 475
Cdd:cd17979  154 NIELFSGYFEGAPVVQV 170
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 299-475 9.74e-58

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: 196.81  E-value: 9.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIeaARGATCSIicTQPRRISAISVSERVAAERGEQIGE 378
Cdd:cd17978    1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGF--ARGGMIGI--TQPRRVAAVSVAKRVAEEMGVELGQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRR-----PDLKLIL 453
Cdd:cd17978   77 LVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVII 156

                        170       180
                 ....*....|....*....|..
gi 30694379  454 MSATLNAELFSSYFGGAPAMHI 475
Cdd:cd17978  157 MSATLDADLFSEYFNGAPVLYI 178
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 299-468 1.07e-57

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: 196.95  E-value: 1.07e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIEaaRGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:cd17988    1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYK--RGKYCNIVVTQPRRIAAISIARRVSQEREWTLGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPD-LKLILMSAT 457
Cdd:cd17988   79 LVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSAT 158

                        170
                 ....*....|.
gi 30694379  458 LNAELFSSYFG 468
Cdd:cd17988  159 ISCKEFADYFT 169
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
 296-476 1.23e-57

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: 196.55  E-value: 1.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  296 RKTLPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYIleseIEAARGATCSIICTQPRRISAISVSERVAAERGEQ 375
Cdd:cd17971    3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYL----AEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  376 IGESVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMS 455
Cdd:cd17971   79 LGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTS 158

                        170       180
                 ....*....|....*....|.
gi 30694379  456 ATLNAELFSSYFGGAPAMHIP 476
Cdd:cd17971  159 ATLDAVKFSQYFYEAPIFTIP 179
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 555-706 8.87e-56

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: 190.82  E-value: 8.87e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  555 WSPDSIGFNLIENVLCHIVKGERPGAVLVFMTGWDDINSLKNQLEAHSLLGDPNKVLLLACHGSMASSEQRLIFDRPPEG 634
Cdd:cd18791   20 EKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDLGKLLVLPLHSSLPPEEQQRVFEPPPPG 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694379  635 IRKIVLATNMAETSITINDVVYVIDCGKAKETSYDALNNTPCLLPSWISKAAARQRRGRAGRVMPGECYHLY 706
Cdd:cd18791  100 VRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
 299-475 1.16e-55

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: 190.74  E-value: 1.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILEseieAARGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:cd17989    1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLE----LGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATL 458
Cdd:cd17989   77 AVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATI 156

                        170
                 ....*....|....*..
gi 30694379  459 NAELFSSYFGGAPAMHI 475
Cdd:cd17989  157 DAERFSRHFNNAPIIEV 173
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 299-798 8.13e-55

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 205.93  E-value: 8.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIEAARgatcsIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:PRK11664    4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLLQHGGINGK-----IIMLEPRRLAARNVAQRLAEQLGEKPGE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNED----FLLIVLKDLlprRPDLKLILM 454
Cdd:PRK11664   79 TVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADlalaLLLDVQQGL---RDDLKLLIM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   455 SATLNAELFSSYFGGAPAMHIPGFTYPVrahfledylETSGYRLTTYNQIDDygeektwkmqkqaqfkkrksLISSAVED 534
Cdd:PRK11664  156 SATLDNDRLQQLLPDAPVIVSEGRSFPV---------ERRYQPLPAHQRFDE--------------------AVARATAE 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   535 ALEaadfkgynfrtrdslscwspdsigfnlienvlchivkgERPGAVLVFMTGWDDINSLKNQLEaHSLLGDpnkVLLLA 614
Cdd:PRK11664  207 LLR--------------------------------------QESGSLLLFLPGVGEIQRVQEQLA-SRVASD---VLLCP 244

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   615 CHGSMASSEQRLIFDRPPEGIRKIVLATNMAETSITINDVVYVIDCGKAKETSYDALNNTPCLLPSWISKAAARQRRGRA 694
Cdd:PRK11664  245 LYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRA 324

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379   695 GRVMPGECYHLYPRCVYEAFADYQQPELLRTPLQSLCLQIKSLGLGSISEfLSRALQPPEAlSVQNAVEYLKIIGALDDD 774
Cdd:PRK11664  325 GRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLELLQWGCHDPAQ-LSWLDQPPAA-ALAAAKRLLQQLGALDGQ 402

                         490       500
                  ....*....|....*....|....
gi 30694379   775 ENLTPLGKNLSMLPVEPKLGKMLI 798
Cdd:PRK11664  403 GRLTARGRKMAALGNDPRLAAMLV 426
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
 296-475 2.01e-53

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: 184.93  E-value: 2.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  296 RKTLPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIEAARGAtcSIICTQPRRISAISVSERVAAERGEQ 375
Cdd:cd17973   10 RRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKK--LVACTQPRRVAAMSVAQRVAEEMDVK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  376 IGESVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMS 455
Cdd:cd17973   88 LGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIVMS 167

                        170       180
                 ....*....|....*....|
gi 30694379  456 ATLNAELFSSYFGGAPAMHI 475
Cdd:cd17973  168 ATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
 299-475 1.13e-51

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: 179.20  E-value: 1.13e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESeieaARGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:cd17983    1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHED----GYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATL 458
Cdd:cd17983   77 EVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATM 156

                        170
                 ....*....|....*..
gi 30694379  459 NAELFSSYFGGAPAMHI 475
Cdd:cd17983  157 DADKFADFFGNVPIFTI 173
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 299-475 5.36e-51

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: 177.31  E-value: 5.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIEAARGATCsiiCTQPRRISAISVSERVAAERGEQIGE 378
Cdd:cd17974    1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGKIG---CTQPRRVAAMSVAARVAEEMGVKLGN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSATL 458
Cdd:cd17974   78 EVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATM 157

                        170
                 ....*....|....*..
gi 30694379  459 NAELFSSYFGGAPAMHI 475
Cdd:cd17974  158 DAEKFSAFFDDAPIFRI 174
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 299-471 4.14e-50

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: 174.83  E-value: 4.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYIL-ESEIEAARgatcsIICTQPRRISAISVSERVAAERGEQIG 377
Cdd:cd17990    1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLaELWIAGGK-----IIVLEPRRVAARAAARRLATLLGEAPG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  378 ESVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLP-RRPDLKLILMSA 456
Cdd:cd17990   76 ETVGYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSA 155

                        170
                 ....*....|....*
gi 30694379  457 TLNAELFSSYFGGAP 471
Cdd:cd17990  156 TLDGDGLAALLPEAP 170
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 299-467 1.47e-49

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: 173.81  E-value: 1.47e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIeAARGATcsIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:cd17980    1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGW-TAGGRV--VGCTQPRRVAAVTVAGRVAEEMGAVLGH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRD-TRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSAT 457
Cdd:cd17980   78 EVGYCIRFDDCTDPQaTRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASAT 157

                        170
                 ....*....|
gi 30694379  458 LNAELFSSYF 467
Cdd:cd17980  158 LDAEKFRDFF 167
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
 299-465 1.84e-43

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: 156.36  E-value: 1.84e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILESEIEAARGATCSII-CTQPRRISAISVSERVAAERGeQIG 377
Cdd:cd17982    1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESDNPGMIgITQPRRVAAVSMAKRVAEELN-VFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  378 ESVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPD--------- 448
Cdd:cd17982   80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159

                        170
                 ....*....|....*...
gi 30694379  449 -LKLILMSATLNAELFSS 465
Cdd:cd17982  160 pLKLVIMSATLRVEDFTE 177
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
 299-475 5.74e-43

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: 154.63  E-value: 5.74e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILEseieAARGATCSIICTQPRRISAISVSERVAAERGEQIGE 378
Cdd:cd17984    1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYE----AGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  379 SVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLP-----RRPDLKLIL 453
Cdd:cd17984   77 KVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQekspnRKEHLKVVV 156

                        170       180
                 ....*....|....*....|..
gi 30694379  454 MSATLNAELFSSYFGGAPAMHI 475
Cdd:cd17984  157 MSATLELAKLSAFFGNCPVFDI 178
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
 299-471 3.75e-32

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: 123.40  E-value: 3.75e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTTQLPQYILES--EIEAARGAtcsIICTQPRRISAISVSERVAAERGEQI 376
Cdd:cd17977    1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYclSAHYQHGV---VVCTQVHKQTAVWLALRVADEMDVNI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  377 GESVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSA 456
Cdd:cd17977   78 GHEVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITC 157

                        170
                 ....*....|....*
gi 30694379  457 TLNAELFSSYFGGAP 471
Cdd:cd17977  158 PHLSSKLLSYYGNVP 172
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 761-850 4.45e-31

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: 117.72  E-value: 4.45e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    761 AVEYLKIIGALDDDENLTPLGKNLSMLPVEPKLGKMLILGAIFNCLDPVMTVVAGLSVRDPFLMPFD------------- 827
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 30694379    828 KKDLAETARSKFSGRD-YSDHLTL 850
Cdd:pfam04408   81 RRAADEKARAKFARLDlEGDHLTL 104
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
 299-475 1.43e-28

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: 113.45  E-value: 1.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAI-AANQVVVVSGETGCGKTTQLPQYIleSEIEAARGATC-SIICTQPRRISAISVSERVAAERGEQI 376
Cdd:cd17986    1 LPIWAAKFTFLEQLeSPSGIVLVSGEPGSGKSTQVPQWC--AEFALSRGFQKgQVTVTQPHPLAARSLALRVADEMDLNL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  377 GESVGYKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPRRPDLKLILMSA 456
Cdd:cd17986   79 GHEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTS 158

                        170
                 ....*....|....*....
gi 30694379  457 TLNAELFSSYFGGAPAMHI 475
Cdd:cd17986  159 PALEPKLRAFWGNPPVVHV 177
DEXDc smart00487
DEAD-like helicases superfamily;
305-481 3.51e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 107.19  E-value: 3.51e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379     305 KDALLKAIAANQVVVVSGETGCGKTTQLPQYILESeieAARGATCSIICTQPRRISAISVSERVAAERGEQIGESVGY-- 382
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEA---LKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLyg 90

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379     383 ----KVRLEGMRGRDTRLLFCTTGVLLRRLLVDR-SLKGVTHVVVDEIHERGmNEDFLLIVLKDLLPRRPDLKLILMSAT 457
Cdd:smart00487   91 gdskREQLRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLL-DGGFGDQLEKLLKLLPKNVQLLLLSAT 169

                           170       180
                    ....*....|....*....|....*.
gi 30694379     458 L--NAELFSSYFGGAPAMHIPGFTYP 481
Cdd:smart00487  170 PpeEIENLLELFLNDPVFIDVGFTPL 195
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 768-851 4.54e-26

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: 102.73  E-value: 4.54e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379     768 IGALDDDENLTPLGKNLSMLPVEPKLGKMLILGAIFNCLDPVMTVVAGLSVRDPFlmPFDKKDLAETARSKFSGRDySDH 847
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPE-SDH 78


                    ....
gi 30694379     848 LTLV 851
Cdd:smart00847   79 LTLL 82
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 916-998 1.79e-21

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: 89.62  E-value: 1.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    916 VRAIICAGMFPGVCSVVNKEKSITLKTmEDGQVLLYSSSVNGNVPMIPFPWLVFNDKVKVNSVFLRDSTAVSDSVLLLFG 995
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLS-DNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFA 79


                   ...
gi 30694379    996 DKI 998
Cdd:pfam07717   80 PHI 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 318-457 6.59e-16

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: 75.90  E-value: 6.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  318 VVVSGETGCGKTTQLPQyILESEIEAARGATCsIICtqPRRISAISVSERVAAERGEqiGESVGY------KVRLEGMRG 391
Cdd:cd00046    4 VLITAPTGSGKTLAALL-AALLLLLKKGKKVL-VLV--PTKALALQTAERLRELFGP--GIRVAVlvggssAEEREKNKL 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694379  392 RDTRLLFCTTGVLLRRLLVDR--SLKGVTHVVVDEIHERGMNEDFLLIVLKDLLPR-RPDLKLILMSAT 457
Cdd:cd00046   78 GDADIIIATPDMLLNLLLREDrlFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAgLKNAQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 309-462 5.42e-12

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: 65.34  E-value: 5.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    309 LKAIAANQVVVVSGETGCGKTT--QLPqyILESEIEAARGATCSIICtqPRRISAISVsERVAAERGEQIGESV-----G 381
Cdd:pfam00270    8 IPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLA--PTRELAEQI-YEELKKLGKGLGLKVasllgG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    382 YKVRLEGMRGRDTRLLFCTTGVLLRRLLVDRSLKGVTHVVVDEIHErgMNEDFLLIVLKDLLPR-RPDLKLILMSATLNA 460
Cdd:pfam00270   83 DSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAHR--LLDMGFGPDLEEILRRlPKKRQILLLSATLPR 160


                   ..
gi 30694379    461 EL 462
Cdd:pfam00270  161 NL 162
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 567-661 1.24e-10

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: 59.53  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379    567 NVLCHIVKGERPGAVLVFMTGwddinslKNQLEAHsLLGDPNKVLLLACHGSMASSEQRLIFDRPPEGIRKIVLATNMAE 646
Cdd:pfam00271    4 EALLELLKKERGGKVLIFSQT-------KKTLEAE-LLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAE 75

                           90
                   ....*....|....*
gi 30694379    647 TSITINDVVYVIDCG 661
Cdd:pfam00271   76 RGLDLPDVDLVINYD 90
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 305-476 2.89e-08

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: 54.96  E-value: 2.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  305 KDALLKAIAANQVVVVSGETGCGKTTqlpqyILESEIEAA-RGATCSIICTQPRRisaiSVSERVAAERGEQIGESVGYK 383
Cdd:cd17921    7 REALRALYLSGDSVLVSAPTSSGKTL-----IAELAILRAlATSGGKAVYIAPTR----ALVNQKEADLRERFGPLGKNV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  384 VRLEG------MRGRDTRLLFCTT---GVLLRRLlVDRSLKGVTHVVVDEIH-----ERGMnedfLLIVLKDLLPRR-PD 448
Cdd:cd17921   78 GLLTGdpsvnkLLLAEADILVATPeklDLLLRNG-GERLIQDVRLVVVDEAHligdgERGV----VLELLLSRLLRInKN 152

                        170       180
                 ....*....|....*....|....*....
gi 30694379  449 LKLILMSATL-NAELFSSYFGGAPAMHIP 476
Cdd:cd17921  153 ARFVGLSATLpNAEDLAEWLGVEDLIRFD 181
HELICc smart00490
helicase superfamily c-terminal domain;
616-661 5.17e-08

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 51.44  E-value: 5.17e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 30694379     616 HGSMASSEQRLIFDRPPEGIRKIVLATNMAETSITINDVVYVIDCG 661
Cdd:smart00490   18 HGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYD 63
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
299-463 1.54e-06

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 52.63  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  299 LPAYKEKDALLKAIAANQVVVVSGETGCGKTtqlpqYILESEIEAA--RGATCsiICTQPrrISAISvSERVAAERGEQI 376
Cdd:COG4581   24 FELDPFQEEAILALEAGRSVLVAAPTGSGKT-----LVAEFAIFLAlaRGRRS--FYTAP--IKALS-NQKFFDLVERFG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  377 GESVGykvrlegM------RGRDTRLLFCTTGVLLRRLLVD-RSLKGVTHVVVDEIH-----ERGMN-EDFLLivlkdLL 443
Cdd:COG4581   94 AENVG-------LltgdasVNPDAPIVVMTTEILRNMLYREgADLEDVGVVVMDEFHyladpDRGWVwEEPII-----HL 161

                        170       180
                 ....*....|....*....|.
gi 30694379  444 PRRpdLKLILMSATL-NAELF 463
Cdd:COG4581  162 PAR--VQLVLLSATVgNAEEF 180
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
 1106-1160 4.14e-06

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: 44.97  E-value: 4.14e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30694379 1106 QTLLARAGHGSPVYKTRQLK---NNQFRSMVTFNGLDFMGKPCgSKKNAEKDAAHEAL 1160
Cdd:cd00048    1 NELCQKNKWPPPEYETVEEGgphNPRFTCTVTVNGQTFEGEGK-SKKEAKQAAAEKAL 57
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
 1102-1163 5.94e-06

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: 44.91  E-value: 5.94e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30694379   1102 KNQLQTLLARAGHGSPVYKTRQL---KNNQFRSMVTFNGLDFMGKPCGSKKNAEKDAAHEALLWL 1163
Cdd:pfam00035    2 KSLLQEYAQKNGKPPPYEYVSEEgppHSPKFTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM_AtDRB-like_rpt2 cd19908
second double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding ...
 1102-1164 2.70e-05

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


Pssm-ID: 380737 [Multi-domain]  Cd Length: 69  Bit Score: 43.24  E-value: 2.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694379 1102 KNQLQTLLARAGHGSPVYKTRQL---KNNQFRSMVTFNGLDFMGKPCGSKKNAEKDAAHEALLWLQ 1164
Cdd:cd19908    4 KNLLQEYAQKAGLPLPLYTTVRSgpgHVPTFTCTVEIAGITFTGEAAKTKKQAEKSAARTAWSSIK 69
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
 1100-1163 4.47e-05

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: 42.48  E-value: 4.47e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694379 1100 NNKNQLQTLLARAGHGSPVYKTRQLK----NNQFRSMVTFNGlDFMGKPCG-SKKNAEKDAAHEALLWL 1163
Cdd:cd10845    2 DYKTALQEYLQKRGLPLPEYELVEEEgpdhNKTFTVEVKVNG-KVIGEGTGrSKKEAEQAAAKAALEKL 69
DSRM_AtDRB-like_rpt1 cd19907
first double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding ...
 1102-1160 9.42e-05

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


Pssm-ID: 380736 [Multi-domain]  Cd Length: 69  Bit Score: 41.69  E-value: 9.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30694379 1102 KNQLQTLLARAGHGSPVYKTRQ---LKNNQFRSMVTFNGLDFMGKP-CGSKKNAEKDAAHEAL 1160
Cdd:cd19907    3 KSQLQEYAQKSCLNLPVYACIRegpDHAPRFRATVTFNGVIFESPPgFPTLKAAEHSAAEVAL 65
DSRM_AtDRB-like cd19878
double-stranded RNA binding motif of Arabidopsis thaliana double-stranded RNA-binding proteins ...
 1102-1164 1.78e-04

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


Pssm-ID: 380707 [Multi-domain]  Cd Length: 67  Bit Score: 40.96  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30694379 1102 KNQLQTLLARAGHGSPVY---KTRQLKNNQFRSMVTFNGLDFMGKPCGSKKNAEKDAAHEALLWLQ 1164
Cdd:cd19878    2 KNLLQEYAQKKKIPLPKYesaKSGPSHQPTFVSTVIVLGVRFSSEGAKNKKQAEQSAAKVALKELG 67
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 318-458 3.35e-04

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 43.51  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  318 VVVSGETGCGKTTQ--LP--QYILESEIEAARG--ATCSIICTqPRRISAISVSeRVAaergEQIGESVGYKVR-LEGMR 390
Cdd:cd17948   30 TLCAAETGSGKTLTylLPiiQRLLRYKLLAEGPfnAPRGLVIT-PSRELAEQIG-SVA----QSLTEGLGLKVKvITGGR 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  391 GR---------DTRLLFCTTGVLLrRLLVDR--SLKGVTHVVVDE----IHER--GMNEDFL------LIVLKDLLPRRP 447
Cdd:cd17948  104 TKrqirnphfeEVDILVATPGALS-KLLTSRiySLEQLRHLVLDEadtlLDDSfnEKLSHFLrrfplaSRRSENTDGLDP 182

                        170
                 ....*....|.
gi 30694379  448 DLKLILMSATL 458
Cdd:cd17948  183 GTQLVLVSATM 193
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
1094-1167 8.91e-04

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 42.39  E-value: 8.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30694379 1094 QNSGGENNKNQLQTLLARAGHGSPVYKTRQLK----NNQFRSMVTFNGlDFMGKPCG-SKKNAEKDAAHEALLWLQGES 1167
Cdd:COG0571  152 PGGAGKDYKTALQEWLQARGLPLPEYEVVEEEgpdhAKTFTVEVLVGG-KVLGEGTGrSKKEAEQAAAKAALEKLGKKE 229
DEXHc_POLQ-like cd18026
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ...
 319-467 1.01e-03

DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.


Pssm-ID: 350784 [Multi-domain]  Cd Length: 202  Bit Score: 41.82  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  319 VVSGETGCGKTtqlpqyiLESEIEAARGATCsiictqpRRISAI-------SVSERVAAErgEQIGESVGYKVR-LEGMR 390
Cdd:cd18026   37 VYSLPTSGGKT-------LVAEILMLKRLLE-------RRKKALfvlpyvsIVQEKVDAL--SPLFEELGFRVEgYAGNK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694379  391 GR-------DTRLLFCT---TGVLLRRLLVDRSLKGVTHVVVDEIH-----ERGMNEDFLLIvlKDLLPRRPDLKLILMS 455
Cdd:cd18026  101 GRsppkrrkSLSVAVCTiekANSLVNSLIEEGRLDELGLVVVDELHmlgdgHRGALLELLLT--KLLYAAQKNIQIVGMS 178

                        170       180
                 ....*....|....*....|..
gi 30694379  456 AT----------LNAELFSSYF 467
Cdd:cd18026  179 ATlpnleelaswLRAELYTTNF 200
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
414-471 1.93e-03

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 42.19  E-value: 1.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30694379  414 LKGVTHVVVDEIH-----ERGMNedfLLIVLKDLLPRRPDLKLILMSATL-NAELFSSYFGGAP 471
Cdd:COG1204  135 LRDVDLVVVDEAHliddeSRGPT---LEVLLARLRRLNPEAQIVALSATIgNAEEIAEWLDAEL 195
 
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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