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Conserved domains on  [gi|157818387|ref|NP_001101148|]
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ATP-dependent DNA/RNA helicase DHX36 [Rattus norvegicus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 1000776)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to ATP-dependent RNA helicase that is involved in translation initiation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 199-378 1.24e-121

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: 368.40  E-value: 1.24e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIGSACRIVCTQPRRISAISVAERVAAERAESCGN 278
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 GNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMS 358
Cdd:cd17981    81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160

                         170       180
                  ....*....|....*....|
gi 157818387  359 ATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17981   161 ATLNAEKFSDYFNNCPMIHI 180
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
207-768 1.72e-113

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: 369.80  E-value: 1.72e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  207 ELVNLINNHQVTVISGETGCGKTTQVTQFILDnyieRGIGSACRIVCTQPRRISAISVAERVAAERAESCGNgnSTGYQI 286
Cdd:COG1643    18 ELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE--TVGYRV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  287 RLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILMSATLNAEK 365
Cdd:COG1643    92 RFEDKV-SAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPaLRPDLKLLVMSATLDAER 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  366 FSEYFGNCPMIHIPGFTFPVveyllediiEkIRYFPEQKEHRSQfkrgfmqghvnrqekeekeaiykerwpayikelqtr 445
Cdd:COG1643   171 FARLLGDAPVIESSGRTYPV---------E-VRYRPLPADERDL------------------------------------ 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  446 ysastidvlemmdddkvdLNLIAALIRyIVLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDRFLIIPLHSLMPTVNQ 525
Cdd:COG1643   205 ------------------EDAVADAVR-EALAEEPGDILVFLPGEREIRRTAEALRGRL---PPDTEILPLYGRLSAAEQ 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  526 TQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYH 605
Cdd:COG1643   263 DRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYR 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  606 LYNGLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAYFlsRLMDPPSDEAVVLSIKHLMELSALDKQEELTPLGVHL 685
Cdd:COG1643   343 LWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRAL 420

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  686 ARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPfviplgkekiadaRRkelaKETRSDHLTVVNAFEGWEEAKRRG 765
Cdd:COG1643   421 ARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP-------------RR----GAAGSDLLARLNLWRRLREQQREF 483


                  ...
gi 157818387  766 FRY 768
Cdd:COG1643   484 LSY 486
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 823-909 4.12e-18

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


:

Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 79.60  E-value: 4.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   823 IKAVICAGLYPKVAKiRLNLGKKRKmvkvHTKSDGLVSIHPKSVNVEQTDFHYNWLIYHLKMRTSSIYLYDCTEVSPYCL 902
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYT----TLSDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWL 75


                   ....*..
gi 157818387   903 LFFGGDI 909
Cdd:pfam07717   76 LLFAPHI 82
 
Name Accession Description Interval E-value
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 199-378 1.24e-121

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: 368.40  E-value: 1.24e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIGSACRIVCTQPRRISAISVAERVAAERAESCGN 278
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 GNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMS 358
Cdd:cd17981    81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160

                         170       180
                  ....*....|....*....|
gi 157818387  359 ATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17981   161 ATLNAEKFSDYFNNCPMIHI 180
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
207-768 1.72e-113

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 369.80  E-value: 1.72e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  207 ELVNLINNHQVTVISGETGCGKTTQVTQFILDnyieRGIGSACRIVCTQPRRISAISVAERVAAERAESCGNgnSTGYQI 286
Cdd:COG1643    18 ELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE--TVGYRV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  287 RLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILMSATLNAEK 365
Cdd:COG1643    92 RFEDKV-SAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPaLRPDLKLLVMSATLDAER 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  366 FSEYFGNCPMIHIPGFTFPVveyllediiEkIRYFPEQKEHRSQfkrgfmqghvnrqekeekeaiykerwpayikelqtr 445
Cdd:COG1643   171 FARLLGDAPVIESSGRTYPV---------E-VRYRPLPADERDL------------------------------------ 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  446 ysastidvlemmdddkvdLNLIAALIRyIVLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDRFLIIPLHSLMPTVNQ 525
Cdd:COG1643   205 ------------------EDAVADAVR-EALAEEPGDILVFLPGEREIRRTAEALRGRL---PPDTEILPLYGRLSAAEQ 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  526 TQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYH 605
Cdd:COG1643   263 DRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYR 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  606 LYNGLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAYFlsRLMDPPSDEAVVLSIKHLMELSALDKQEELTPLGVHL 685
Cdd:COG1643   343 LWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRAL 420

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  686 ARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPfviplgkekiadaRRkelaKETRSDHLTVVNAFEGWEEAKRRG 765
Cdd:COG1643   421 ARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP-------------RR----GAAGSDLLARLNLWRRLREQQREF 483


                  ...
gi 157818387  766 FRY 768
Cdd:COG1643   484 LSY 486
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 194-753 1.34e-81

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 289.65  E-value: 1.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  194 RFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILdnyiERGIGSACRIVCTQPRRISAISVAERVAAERA 273
Cdd:PRK11131   68 TYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICL----ELGRGVKGLIGHTQPRRLAARTVANRIAEELE 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  274 ESCGNgnSTGYQIRLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLK 353
Cdd:PRK11131  144 TELGG--CVGYKVRFNDQV-SDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLK 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  354 VILMSATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYFPeqkehrsqfkrgfMQGHVNRQEKEEKEAIYKE 433
Cdd:PRK11131  221 VIITSATIDPERFSRHFNNAPIIEVSGRTYPV----------EVRYRP-------------IVEEADDTERDQLQAIFDA 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  434 rwpayIKELQtrysastidvlemmdddkvdlnliaaliryivlEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDrflI 513
Cdd:PRK11131  278 -----VDELG---------------------------------REGPGDILIFMSGEREIRDTADALNKLNLRHTE---I 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  514 IPLHSLMPTVNQTQVFKktPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKG 593
Cdd:PRK11131  317 LPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKG 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  594 RAGRVQPGHCYHLYNGL----RASLLDdyqlPEILRTPLEELCLQIKILRLGGIAYFlsRLMDPPSDEAVVLSIKHLMEL 669
Cdd:PRK11131  395 RCGRVSEGICIRLYSEDdflsRPEFTD----PEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEEL 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  670 SALDKQE-----ELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKIADARRKELAKEt 744
Cdd:PRK11131  469 GAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADK- 547


                  ....*....
gi 157818387  745 RSDHLTVVN 753
Cdd:PRK11131  548 ESDFLAFVN 556
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 443-607 3.34e-76

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: 247.06  E-value: 3.34e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  443 QTRYSASTIDVL--EMMDDDKVDLNLIAALIRYIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKS-DRFLIIPLHSL 519
Cdd:cd18791     4 EVYYLEDILELLgiSSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDlGKLLVLPLHSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  520 MPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQ 599
Cdd:cd18791    84 LPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTR 163


                  ....*...
gi 157818387  600 PGHCYHLY 607
Cdd:cd18791   164 PGKCYRLY 171
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 199-737 1.10e-73

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


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 260.08  E-value: 1.10e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDnyiERGIGSacRIVCTQPRRISAISVAERVAAERAESCGN 278
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLD---APGIGG--KIIMLEPRRLAARSAAQRLASQLGEAVGQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   279 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILM 357
Cdd:TIGR01970   76 --TVGYRVRGENKVSRRT-RLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSsLREDLKILAM 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   358 SATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYFPEQKEHRsqfkrgfMQGHVNRQekeekeaiykerwpa 437
Cdd:TIGR01970  153 SATLDGERLSSLLPDAPVVESEGRSFPV----------EIRYLPLRGDQR-------LEDAVSRA--------------- 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   438 yikelqtrysastidVLEMmdddkvdlnliaaliryivLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDRFLIIPLH 517
Cdd:TIGR01970  201 ---------------VEHA-------------------LASETGSILVFLPGQAEIRRVQEQLAERL---DSDVLICPLY 243

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   518 SLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGR 597
Cdd:TIGR01970  244 GELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGR 323

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   598 VQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQikILRLGGIAYFLSRLMDPPSDEAVVLSIKHLMELSALDKQEE 677
Cdd:TIGR01970  324 LEPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALE--LAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGR 401

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157818387   678 LTPLGVHLARLPVEPHIGKMILFG------ALFCCLDPVLT-----------IAASLSFKDPFVIPLGKEKIADARR 737
Cdd:TIGR01970  402 LTAHGKAMAALGCHPRLAAMLLSAhstglaALACDLAALLEerglprqggadLMNRLHRLQQGRQGRGQRAQQLAKK 478
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 662-751 1.33e-27

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: 107.71  E-value: 1.33e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   662 SIKHLMELSALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLG------------- 728
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 157818387   729 -KEKIADARRKELAKETRSDHLTV 751
Cdd:pfam04408   81 rRAADEKARAKFARLDLEGDHLTL 104
DEXDc smart00487
DEAD-like helicases superfamily;
202-384 2.85e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.50  E-value: 2.85e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387    202 YGMQKELVN-LINNHQVTVISGETGCGKTTQVTQFILDNYIErgiGSACRIVCTQPRRISAISVAERVAAERAESCGN-- 278
Cdd:smart00487   10 RPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALKR---GKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKvv 86

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387    279 GNSTGYQIRLQ-SRLPRKQGSILYCTTGIILQWLQSDS-RLSSVSHIVLDEIHER--NLQSDVLMTVIKDLlhfRSDLKV 354
Cdd:smart00487   87 GLYGGDSKREQlRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQL 163

                           170       180       190
                    ....*....|....*....|....*....|..
gi 157818387    355 ILMSATL--NAEKFSEYFGNCPMIHIPGFTFP 384
Cdd:smart00487  164 LLLSATPpeEIENLLELFLNDPVFIDVGFTPL 195
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 668-752 9.35e-25

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: 98.88  E-value: 9.35e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387    668 ELSALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFviPLGKEKIADARRKELAKEtRSD 747
Cdd:smart00847    1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADP-ESD 77


                    ....*
gi 157818387    748 HLTVV 752
Cdd:smart00847   78 HLTLL 82
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 823-909 4.12e-18

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


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 79.60  E-value: 4.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   823 IKAVICAGLYPKVAKiRLNLGKKRKmvkvHTKSDGLVSIHPKSVNVEQTDFHYNWLIYHLKMRTSSIYLYDCTEVSPYCL 902
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYT----TLSDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWL 75


                   ....*..
gi 157818387   903 LFFGGDI 909
Cdd:pfam07717   76 LLFAPHI 82
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 205-364 8.47e-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: 64.57  E-value: 8.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   205 QKELVNLINNHQVTVISGETGCGKTTqVTQF-ILDNYIERGIGSacRIVCTQPRRISAISVAERvAAERAESCG------ 277
Cdd:pfam00270    4 QAEAIPAILEGRDVLVQAPTGSGKTL-AFLLpALEALDKLDNGP--QALVLAPTRELAEQIYEE-LKKLGKGLGlkvasl 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   278 -NGNSTGYQIRLQSRLPrkqgsILYCTTGIILQWLQSDSRLSSVSHIVLDEIHE--RNLQSDVLMTVIKdllHFRSDLKV 354
Cdd:pfam00270   80 lGGDSRKEQLEKLKGPD-----ILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRllDMGFGPDLEEILR---RLPKKRQI 151

                          170
                   ....*....|
gi 157818387   355 ILMSATLNAE 364
Cdd:pfam00270  152 LLLSATLPRN 161
 
Name Accession Description Interval E-value
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 199-378 1.24e-121

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: 368.40  E-value: 1.24e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIGSACRIVCTQPRRISAISVAERVAAERAESCGN 278
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 GNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMS 358
Cdd:cd17981    81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160

                         170       180
                  ....*....|....*....|
gi 157818387  359 ATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17981   161 ATLNAEKFSDYFNNCPMIHI 180
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
207-768 1.72e-113

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 369.80  E-value: 1.72e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  207 ELVNLINNHQVTVISGETGCGKTTQVTQFILDnyieRGIGSACRIVCTQPRRISAISVAERVAAERAESCGNgnSTGYQI 286
Cdd:COG1643    18 ELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE--TVGYRV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  287 RLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILMSATLNAEK 365
Cdd:COG1643    92 RFEDKV-SAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPaLRPDLKLLVMSATLDAER 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  366 FSEYFGNCPMIHIPGFTFPVveyllediiEkIRYFPEQKEHRSQfkrgfmqghvnrqekeekeaiykerwpayikelqtr 445
Cdd:COG1643   171 FARLLGDAPVIESSGRTYPV---------E-VRYRPLPADERDL------------------------------------ 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  446 ysastidvlemmdddkvdLNLIAALIRyIVLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDRFLIIPLHSLMPTVNQ 525
Cdd:COG1643   205 ------------------EDAVADAVR-EALAEEPGDILVFLPGEREIRRTAEALRGRL---PPDTEILPLYGRLSAAEQ 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  526 TQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYH 605
Cdd:COG1643   263 DRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYR 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  606 LYNGLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAYFlsRLMDPPSDEAVVLSIKHLMELSALDKQEELTPLGVHL 685
Cdd:COG1643   343 LWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRAL 420

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  686 ARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPfviplgkekiadaRRkelaKETRSDHLTVVNAFEGWEEAKRRG 765
Cdd:COG1643   421 ARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP-------------RR----GAAGSDLLARLNLWRRLREQQREF 483


                  ...
gi 157818387  766 FRY 768
Cdd:COG1643   484 LSY 486
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 215-378 5.32e-87

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: 275.88  E-value: 5.32e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  215 HQVTVISGETGCGKTTQVTQFILDNYIERGigSACRIVCTQPRRISAISVAERVAAERAESCGNgnSTGYQIRLQSRLPR 294
Cdd:cd17917     1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKG--GKGRIVCTQPRRIAAISVAERVAEERGEKLGE--EVGYQIRFESKTSS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  295 KqGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMSATLNAEKFSEYFGNCP 374
Cdd:cd17917    77 K-TRIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAP 155


                  ....
gi 157818387  375 MIHI 378
Cdd:cd17917   156 VIHI 159
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 194-753 1.34e-81

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 289.65  E-value: 1.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  194 RFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILdnyiERGIGSACRIVCTQPRRISAISVAERVAAERA 273
Cdd:PRK11131   68 TYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICL----ELGRGVKGLIGHTQPRRLAARTVANRIAEELE 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  274 ESCGNgnSTGYQIRLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLK 353
Cdd:PRK11131  144 TELGG--CVGYKVRFNDQV-SDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLK 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  354 VILMSATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYFPeqkehrsqfkrgfMQGHVNRQEKEEKEAIYKE 433
Cdd:PRK11131  221 VIITSATIDPERFSRHFNNAPIIEVSGRTYPV----------EVRYRP-------------IVEEADDTERDQLQAIFDA 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  434 rwpayIKELQtrysastidvlemmdddkvdlnliaaliryivlEEEDGAILVFLPGWDNISTLHDLLMSQVMFKSDrflI 513
Cdd:PRK11131  278 -----VDELG---------------------------------REGPGDILIFMSGEREIRDTADALNKLNLRHTE---I 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  514 IPLHSLMPTVNQTQVFKktPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKG 593
Cdd:PRK11131  317 LPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKG 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  594 RAGRVQPGHCYHLYNGL----RASLLDdyqlPEILRTPLEELCLQIKILRLGGIAYFlsRLMDPPSDEAVVLSIKHLMEL 669
Cdd:PRK11131  395 RCGRVSEGICIRLYSEDdflsRPEFTD----PEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEEL 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  670 SALDKQE-----ELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKEKIADARRKELAKEt 744
Cdd:PRK11131  469 GAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADK- 547


                  ....*....
gi 157818387  745 RSDHLTVVN 753
Cdd:PRK11131  548 ESDFLAFVN 556
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 443-607 3.34e-76

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: 247.06  E-value: 3.34e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  443 QTRYSASTIDVL--EMMDDDKVDLNLIAALIRYIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKS-DRFLIIPLHSL 519
Cdd:cd18791     4 EVYYLEDILELLgiSSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDlGKLLVLPLHSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  520 MPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQ 599
Cdd:cd18791    84 LPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTR 163


                  ....*...
gi 157818387  600 PGHCYHLY 607
Cdd:cd18791   164 PGKCYRLY 171
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 199-737 1.10e-73

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


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 260.08  E-value: 1.10e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDnyiERGIGSacRIVCTQPRRISAISVAERVAAERAESCGN 278
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLD---APGIGG--KIIMLEPRRLAARSAAQRLASQLGEAVGQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   279 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILM 357
Cdd:TIGR01970   76 --TVGYRVRGENKVSRRT-RLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSsLREDLKILAM 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   358 SATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYFPEQKEHRsqfkrgfMQGHVNRQekeekeaiykerwpa 437
Cdd:TIGR01970  153 SATLDGERLSSLLPDAPVVESEGRSFPV----------EIRYLPLRGDQR-------LEDAVSRA--------------- 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   438 yikelqtrysastidVLEMmdddkvdlnliaaliryivLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDRFLIIPLH 517
Cdd:TIGR01970  201 ---------------VEHA-------------------LASETGSILVFLPGQAEIRRVQEQLAERL---DSDVLICPLY 243

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   518 SLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGR 597
Cdd:TIGR01970  244 GELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGR 323

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   598 VQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQikILRLGGIAYFLSRLMDPPSDEAVVLSIKHLMELSALDKQEE 677
Cdd:TIGR01970  324 LEPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALE--LAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALDAQGR 401

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157818387   678 LTPLGVHLARLPVEPHIGKMILFG------ALFCCLDPVLT-----------IAASLSFKDPFVIPLGKEKIADARR 737
Cdd:TIGR01970  402 LTAHGKAMAALGCHPRLAAMLLSAhstglaALACDLAALLEerglprqggadLMNRLHRLQQGRQGRGQRAQQLAKK 478
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 199-378 1.44e-71

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: 234.73  E-value: 1.44e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIGSACRIVCTQPRRISAISVAERVAAERAESCGN 278
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 gnSTGYQIRLQSRlpRKQGS-ILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 357
Cdd:cd17985    81 --SVGYQIRLESV--KSSATrLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILM 156

                         170       180
                  ....*....|....*....|.
gi 157818387  358 SATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17985   157 SATLNAELFSDYFNSCPVIHI 177
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 172-378 1.22e-69

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: 231.65  E-value: 1.22e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  172 LDQQLLEDLQ-KKKTDPRYIEMQRFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIGSACR 250
Cdd:cd17972    31 ISMDLKNELMyQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  251 IVCTQPRRISAISVAERVAAERAESCgnGNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRlsSVSHIVLDEIHE 330
Cdd:cd17972   111 IVVTQPRRISAVSVAERVAFERGEEV--GKSCGYSVRFESVLPRPHASILFCTVGVLLRKLEAGIR--GISHVIVDEIHE 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157818387  331 RNLQSDVLMTVIKDLLHFRSDLKVILMSATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17972   187 RDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 199-378 3.54e-66

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: 220.05  E-value: 3.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIGSACRIVCTQPRRISAISVAERVAAERAESCGN 278
Cdd:cd17976     1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 gnSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMS 358
Cdd:cd17976    81 --NVGYQVRLESRPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMS 158

                         170       180
                  ....*....|....*....|
gi 157818387  359 ATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17976   159 ATGDNQRLSRYFGGCPVVRV 178
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
 199-378 5.54e-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: 205.53  E-value: 5.54e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYI-ERGIGSACRIVCTQPRRISAISVAERVAAERAESCG 277
Cdd:cd17975     1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLlNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  278 NG--NS-TGYQIRLQSRlPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKV 354
Cdd:cd17975    81 PGgkNSlCGYQIRMESR-TGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHL 159

                         170       180
                  ....*....|....*....|....
gi 157818387  355 ILMSATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17975   160 ILMSATVDCEKFSSYFTHCPILRI 183
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 199-378 6.29e-61

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: 205.06  E-value: 6.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIgsACRIVCTQPRRISAISVAERVAAERAESCGN 278
Cdd:cd17987     1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGI--PCRIFCTQPRRLAAIAVAERVAAERGEKIGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQS-DSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 357
Cdd:cd17987    79 --TVGYQIRLESRVSPKT-LLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILS 155

                         170       180
                  ....*....|....*....|.
gi 157818387  358 SATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17987   156 SAALDVNLFIRYFGSCPVIYI 176
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 199-702 3.31e-57

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 212.48  E-value: 3.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGigsacRIVCTQPRRISAISVAERVAAERAESCGN 278
Cdd:PRK11664    4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLLQHGGING-----KIIMLEPRRLAARNVAQRLAEQLGEKPGE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 gnSTGYQIRLQSRL-PRKQGSILycTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDV----LMTVIKDLlhfRSDLK 353
Cdd:PRK11664   79 --TVGYRMRAESKVgPNTRLEVV--TEGILTRMIQRDPELSGVGLVILDEFHERSLQADLalalLLDVQQGL---RDDLK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  354 VILMSATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYFPeqkehrsqfkrgfMQGHvnrQEKEEKEAiyke 433
Cdd:PRK11664  152 LLIMSATLDNDRLQQLLPDAPVIVSEGRSFPV----------ERRYQP-------------LPAH---QRFDEAVA---- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  434 rwpayikelqtrysastidvlemmdddkvdlNLIAALiryivLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDRFLI 513
Cdd:PRK11664  202 -------------------------------RATAEL-----LRQESGSLLLFLPGVGEIQRVQEQLASRV---ASDVLL 242

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  514 IPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKG 593
Cdd:PRK11664  243 CPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAG 322

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  594 RAGRVQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQikILRLGgiAYFLSRLM--DPPSDEAVVLSIKHLMELSA 671
Cdd:PRK11664  323 RAGRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLE--LLQWG--CHDPAQLSwlDQPPAAALAAAKRLLQQLGA 398

                         490       500       510
                  ....*....|....*....|....*....|.
gi 157818387  672 LDKQEELTPLGVHLARLPVEPHIGKMILFGA 702
Cdd:PRK11664  399 LDGQGRLTARGRKMAALGNDPRLAAMLVAAK 429
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
 187-378 2.41e-52

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: 181.46  E-value: 2.41e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  187 PRYIEMQRFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIGSAcrIVCTQPRRISAISVAE 266
Cdd:cd17973     1 QRYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKL--VACTQPRRVAAMSVAQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  267 RVAAERAESCGNgnSTGYQIRLQSRLPRKqgSIL-YCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDL 345
Cdd:cd17973    79 RVAEEMDVKLGE--EVGYSIRFEDCSSAK--TILkYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEV 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 157818387  346 LHFRSDLKVILMSATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17973   155 VRRRPDLKLIVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 199-385 5.59e-52

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: 180.01  E-value: 5.59e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIgsACRIVCTQPRRISAISVAERVAAERAesCGN 278
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGK--YCNIVVTQPRRIAAISIARRVSQERE--WTL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 GNSTGYQIRLQsRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSD-LKVILM 357
Cdd:cd17988    77 GSLVGYQVGLE-RPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILM 155

                         170       180
                  ....*....|....*....|....*...
gi 157818387  358 SATLNAEKFSEYFGncpMIHIPGFTFPV 385
Cdd:cd17988   156 SATISCKEFADYFT---TPNNPAYVFEV 180
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
 196-379 5.31e-50

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: 174.59  E-value: 5.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  196 RKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFIldnyIERGIGSACRIVCTQPRRISAISVAERVAAERAes 275
Cdd:cd17971     3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYL----AEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFG-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  276 CGNGNSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVI 355
Cdd:cd17971    77 CCLGQEVGYTIRFEDCTSPET-VIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLI 155

                         170       180
                  ....*....|....*....|....
gi 157818387  356 LMSATLNAEKFSEYFGNCPMIHIP 379
Cdd:cd17971   156 VTSATLDAVKFSQYFYEAPIFTIP 179
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 199-378 1.35e-48

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: 170.32  E-value: 1.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNyierGIGsacRIVCTQPRRISAISVAERVAAERAEScgN 278
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAA----GFR---HIACTQPRRIACISLAKRVAFESLNQ--Y 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 GNSTGYQIRLQ-SRLPRKQgsILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 357
Cdd:cd17979    72 GSKVAYQIRFErTRTLATK--LLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILM 149

                         170       180
                  ....*....|....*....|.
gi 157818387  358 SATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17979   150 SATINIELFSGYFEGAPVVQV 170
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
 199-378 1.17e-47

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: 167.64  E-value: 1.17e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFIL-DNYIERGIgsacrIVCTQPRRISAISVAERVAAERAESCG 277
Cdd:cd17983     1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHeDGYTDYGM-----IGCTQPRRVAAMSVAKRVSEEMGVELG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  278 NgnSTGYQIRLQSrLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 357
Cdd:cd17983    76 E--EVGYAIRFED-CTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVT 152

                         170       180
                  ....*....|....*....|.
gi 157818387  358 SATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17983   153 SATMDADKFADFFGNVPIFTI 173
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 199-378 5.15e-47

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: 165.75  E-value: 5.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIGsacRIVCTQPRRISAISVAERVAAERaeSCGN 278
Cdd:cd17974     1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGG---KIGCTQPRRVAAMSVAARVAEEM--GVKL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 GNSTGYQIRLQSRLPRKqgSIL-YCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 357
Cdd:cd17974    76 GNEVGYSIRFEDCTSEK--TVLkYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLIS 153

                         170       180
                  ....*....|....*....|.
gi 157818387  358 SATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17974   154 SATMDAEKFSAFFDDAPIFRI 174
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 199-378 4.03e-45

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: 160.60  E-value: 4.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERG--IGsacrivCTQPRRISAISVAERVAAERaeSC 276
Cdd:cd17978     1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGgmIG------ITQPRRVAAVSVAKRVAEEM--GV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  277 GNGNSTGYQIRLQSRLPRkQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFR-----SD 351
Cdd:cd17978    73 ELGQLVGYSVRFDDVTSE-ETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSP 151

                         170       180
                  ....*....|....*....|....*..
gi 157818387  352 LKVILMSATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17978   152 LKVIIMSATLDADLFSEYFNGAPVLYI 178
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 199-370 1.15e-43

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: 156.48  E-value: 1.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILdnyiERGIGSACR-IVCTQPRRISAISVAERVAAERAESCG 277
Cdd:cd17980     1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLA----EAGWTAGGRvVGCTQPRRVAAVTVAGRVAEEMGAVLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  278 NgnSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 357
Cdd:cd17980    77 H--EVGYCIRFDDCTDPQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVA 154

                         170
                  ....*....|...
gi 157818387  358 SATLNAEKFSEYF 370
Cdd:cd17980   155 SATLDAEKFRDFF 167
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
 199-378 4.52e-42

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


Pssm-ID: 350747 [Multi-domain]  Cd Length: 173  Bit Score: 151.45  E-value: 4.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILdnyiERGIGSACRIVCTQPRRISAISVAERVAAERAESCGN 278
Cdd:cd17989     1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICL----ELGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMS 358
Cdd:cd17989    77 --AVGYKVRFTDQTSDET-CVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITS 153

                         170       180
                  ....*....|....*....|
gi 157818387  359 ATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17989   154 ATIDAERFSRHFNNAPIIEV 173
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
 199-378 1.55e-39

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: 144.61  E-value: 1.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILdnyiERGIGSACRIVCTQPRRISAISVAERVAAERaeSCGN 278
Cdd:cd17984     1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLY----EAGFSQHGMIGVTQPRRVAAISVAQRVAEEM--KCTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 GNSTGYQIRLQSrLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRS-----DLK 353
Cdd:cd17984    75 GSKVGYQVRFDD-CSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLK 153

                         170       180
                  ....*....|....*....|....*
gi 157818387  354 VILMSATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17984   154 VVVMSATLELAKLSAFFGNCPVFDI 178
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
 199-368 2.40e-39

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: 144.42  E-value: 2.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILD-NYIERGIGSACRIVCTQPRRISAISVAERVAAERAEScg 277
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEaGFGSPESDNPGMIGITQPRRVAAVSMAKRVAEELNVF-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  278 nGNSTGYQIRLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSD------ 351
Cdd:cd17982    79 -GKEVSYQIRYDSTV-SENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdq 156

                         170       180
                  ....*....|....*....|.
gi 157818387  352 ----LKVILMSATLNAEKFSE 368
Cdd:cd17982   157 tvkpLKLVIMSATLRVEDFTE 177
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 199-376 1.24e-32

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: 124.75  E-value: 1.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGigsaCRIVCTQPRRISAISVAERVAAERAESCGN 278
Cdd:cd17990     1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAG----GKIIVLEPRRVAARAAARRLATLLGEAPGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILM 357
Cdd:cd17990    77 --TVGYRVRGESRVGRRT-RVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAM 153

                         170
                  ....*....|....*....
gi 157818387  358 SATLNAEKFSEYFGNCPMI 376
Cdd:cd17990   154 SATLDGDGLAALLPEAPVV 172
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 662-751 1.33e-27

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: 107.71  E-value: 1.33e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   662 SIKHLMELSALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLG------------- 728
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 157818387   729 -KEKIADARRKELAKETRSDHLTV 751
Cdd:pfam04408   81 rRAADEKARAKFARLDLEGDHLTL 104
DEXDc smart00487
DEAD-like helicases superfamily;
202-384 2.85e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.50  E-value: 2.85e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387    202 YGMQKELVN-LINNHQVTVISGETGCGKTTQVTQFILDNYIErgiGSACRIVCTQPRRISAISVAERVAAERAESCGN-- 278
Cdd:smart00487   10 RPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALKR---GKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKvv 86

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387    279 GNSTGYQIRLQ-SRLPRKQGSILYCTTGIILQWLQSDS-RLSSVSHIVLDEIHER--NLQSDVLMTVIKDLlhfRSDLKV 354
Cdd:smart00487   87 GLYGGDSKREQlRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQL 163

                           170       180       190
                    ....*....|....*....|....*....|..
gi 157818387    355 ILMSATL--NAEKFSEYFGNCPMIHIPGFTFP 384
Cdd:smart00487  164 LLLSATPpeEIENLLELFLNDPVFIDVGFTPL 195
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 668-752 9.35e-25

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: 98.88  E-value: 9.35e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387    668 ELSALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFviPLGKEKIADARRKELAKEtRSD 747
Cdd:smart00847    1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADP-ESD 77


                    ....*
gi 157818387    748 HLTVV 752
Cdd:smart00847   78 HLTLL 82
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
 199-378 1.90e-24

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


Pssm-ID: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 101.06  E-value: 1.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQ----FILDNYIERGIgsacrIVCTQPRRISAISVAERVAAERae 274
Cdd:cd17977     1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHGV-----VVCTQVHKQTAVWLALRVADEM-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  275 SCGNGNSTGYQIRLQSRLprKQGSIL-YCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLK 353
Cdd:cd17977    74 DVNIGHEVGYVIPFENCC--TNETILrYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELK 151

                         170       180
                  ....*....|....*....|....*
gi 157818387  354 VILMSATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17977   152 LVIITCPHLSSKLLSYYGNVPLIEV 176
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
 199-378 4.17e-21

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: 91.50  E-value: 4.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  199 LPSYGMQKE-LVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGIgSACRIVCTQPRRISAISVAERVAAERAESCG 277
Cdd:cd17986     1 LPIWAAKFTfLEQLESPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGF-QKGQVTVTQPHPLAARSLALRVADEMDLNLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  278 NgnSTGYQIRlQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 357
Cdd:cd17986    80 H--EVGYSIP-QEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVV 156

                         170       180
                  ....*....|....*....|.
gi 157818387  358 SATLNAEKFSEYFGNCPMIHI 378
Cdd:cd17986   157 TSPALEPKLRAFWGNPPVVHV 177
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 823-909 4.12e-18

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


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 79.60  E-value: 4.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   823 IKAVICAGLYPKVAKiRLNLGKKRKmvkvHTKSDGLVSIHPKSVNVEQTDFHYNWLIYHLKMRTSSIYLYDCTEVSPYCL 902
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYT----TLSDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWL 75


                   ....*..
gi 157818387   903 LFFGGDI 909
Cdd:pfam07717   76 LLFAPHI 82
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 204-601 5.34e-16

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 82.72  E-value: 5.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  204 MQKELVNLINNHQVTVISGETGCGKTTQVTQFIL----------------DNYIERgigsacRIVCTQPRrisaISVAER 267
Cdd:PHA02653  168 VQLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLLwfnylfggfdnldkidPNFIER------PIVLSLPR----VALVRL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  268 VAAERAESCGNGNSTGYQIRLQ---------SRLPRKQGsILYCTTGIILqwlqsdSRLSSVSHIVLDEIHERNLQSDVL 338
Cdd:PHA02653  238 HSITLLKSLGFDEIDGSPISLKygsipdeliNTNPKPYG-LVFSTHKLTL------NKLFDYGTVIIDEVHEHDQIGDII 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  339 MTVI-KDLLHFRSdlkVILMSATL--NAEKFSEYFGNCPMIHIPGFT-FPVVEylledIIEKIRYFPEQKEhrsqfkrgf 414
Cdd:PHA02653  311 IAVArKHIDKIRS---LFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISE-----VYVKNKYNPKNKR--------- 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  415 mqghvnRQEKEEKEAIYKErwpayIKELQTRYSASTIdvlemmdddkVDLNLIAALIRYI-VLEEEdgailvfLPGWDni 493
Cdd:PHA02653  374 ------AYIEEEKKNIVTA-----LKKYTPPKGSSGI----------VFVASVSQCEEYKkYLEKR-------LPIYD-- 423

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  494 stlhdllmsqvmfksdrFLIIplHSLMPTVNQ--TQVFKKTPPgvrKIVIATNIAETSITIDDVVYVIDGGKIKETHFDT 571
Cdd:PHA02653  424 -----------------FYII--HGKVPNIDEilEKVYSSKNP---SIIISTPYLESSVTIRNATHVYDTGRVYVPEPFG 481

                         410       420       430
                  ....*....|....*....|....*....|
gi 157818387  572 QNNIstmsaeWVSKANAKQRKGRAGRVQPG 601
Cdd:PHA02653  482 GKEM------FISKSMRTQRKGRVGRVSPG 505
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 218-360 2.09e-14

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: 71.28  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  218 TVISGETGCGKTTQVTQFILDNYIERGigsaCRIVCTQPRRISAISVAERVAAERAE--SCGnGNSTGYQIRLQSRLPRK 295
Cdd:cd00046     4 VLITAPTGSGKTLAALLAALLLLLKKG----KKVLVLVPTKALALQTAERLRELFGPgiRVA-VLVGGSSAEEREKNKLG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818387  296 QGSILYCTTGIILQWLQSD--SRLSSVSHIVLDEIHERNLQSDV-LMTVIKDLLHFRSDLKVILMSAT 360
Cdd:cd00046    79 DADIIIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGaLILDLAVRKAGLKNAQVILLSAT 146
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 469-598 3.69e-14

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: 69.55  E-value: 3.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   469 ALIRYIVLEEEDGAILVFLPGWDnistlhdLLMSQVMFKSDRFLIIPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAET 548
Cdd:pfam00271    4 EALLELLKKERGGKVLIFSQTKK-------TLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 157818387   549 SITIDDVVYVIdggkiketHFDTQNNISTMsaewvskanaKQRKGRAGRV 598
Cdd:pfam00271   77 GLDLPDVDLVI--------NYDLPWNPASY----------IQRIGRAGRA 108
HELICc smart00490
helicase superfamily c-terminal domain;
505-597 2.29e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 66.08  E-value: 2.29e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387    505 MFKSDRFLIIPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIdggkiketHFDTqnnistmsaeWVS 584
Cdd:smart00490    6 LLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVI--------IYDL----------PWS 67

                            90
                    ....*....|...
gi 157818387    585 KANAKQRKGRAGR 597
Cdd:smart00490   68 PASYIQRIGRAGR 80
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 205-364 8.47e-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: 64.57  E-value: 8.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   205 QKELVNLINNHQVTVISGETGCGKTTqVTQF-ILDNYIERGIGSacRIVCTQPRRISAISVAERvAAERAESCG------ 277
Cdd:pfam00270    4 QAEAIPAILEGRDVLVQAPTGSGKTL-AFLLpALEALDKLDNGP--QALVLAPTRELAEQIYEE-LKKLGKGLGlkvasl 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387   278 -NGNSTGYQIRLQSRLPrkqgsILYCTTGIILQWLQSDSRLSSVSHIVLDEIHE--RNLQSDVLMTVIKdllHFRSDLKV 354
Cdd:pfam00270   80 lGGDSRKEQLEKLKGPD-----ILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRllDMGFGPDLEEILR---RLPKKRQI 151

                          170
                   ....*....|
gi 157818387   355 ILMSATLNAE 364
Cdd:pfam00270  152 LLLSATLPRN 161
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 205-379 1.42e-07

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 52.65  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  205 QKELVNLINNHQV-TVISGETGCGKTTQVTQFILDNYIERGigsaCRIVCTQPRRisaiSVAERVAAERAESCGN----- 278
Cdd:cd17921     6 QREALRALYLSGDsVLVSAPTSSGKTLIAELAILRALATSG----GKAVYIAPTR----ALVNQKEADLRERFGPlgknv 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  279 GNSTGYQIRLQSRLPRKQgsILYCTTGIILQWLQ--SDSRLSSVSHIVLDEIHERNLQS--DVLMTVIKDLLHFRSDLKV 354
Cdd:cd17921    78 GLLTGDPSVNKLLLAEAD--ILVATPEKLDLLLRngGERLIQDVRLVVVDEAHLIGDGErgVVLELLLSRLLRINKNARF 155

                         170       180
                  ....*....|....*....|....*.
gi 157818387  355 ILMSATL-NAEKFSEYFGNCPMIHIP 379
Cdd:cd17921   156 VGLSATLpNAEDLAEWLGVEDLIRFD 181
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
 216-360 2.17e-04

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 42.54  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  216 QVTVISGETGCGKTTQVtqfiLDNYIERGIGSACRIVCTQPRRISAISVAERVaaeraescgNGNSTGYQIRLQSRLPRK 295
Cdd:cd17931     2 QLTVLDLHPGAGKTTRV----LPQIIREAIKKRLRTLVLAPTRVVAAEMYEAL---------RGLPIRYRTGAVKEEHGG 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157818387  296 QGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFrSDLKVILMSAT 360
Cdd:cd17931    69 NEIVDYMCHGTFTCRLLSPKRVPNYNLIIMDEAHFTDPASIAARGYIHTRVEM-GEAAVIFMTAT 132
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 205-245 4.29e-04

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 41.77  E-value: 4.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 157818387  205 QKELVNLINNHQVTVISGETGCGKTTqVTQFILDNYIERGI 245
Cdd:cd17933     2 QKAAVRLVLRNRVSVLTGGAGTGKTT-TLKALLAALEAEGK 41
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
 158-557 6.27e-04

CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 43.53  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  158 DSEYLLQQNEPNLGLDQQLLEDLQKKKTDPRYiEMQRFRKKLpsygMQKELVNLINNHQVTVISGETGCGKTTQVTQFIL 237
Cdd:COG1203    95 DSANFDMARQALDHLLAERLERLLPKKSKPRT-PINPLQNEA----LELALEAAEEEPGLFILTAPTGGGKTEAALLFAL 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  238 DNYIERGigsACRIVCTQP------------RRISAISVAE---RVAAERAESCGNGNSTGYQIRLQSRL---PrkqgsI 299
Cdd:COG1203   170 RLAAKHG---GRRIIYALPftsiinqtydrlRDLFGEDVLLhhsLADLDLLEEEEEYESEARWLKLLKELwdaP-----V 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  300 LYCTtgiILQWLqsDSRLSSVSH------------IVLDEIH--ERNLQSdVLMTVIKDLLHFRSdlKVILMSATLnaek 365
Cdd:COG1203   242 VVTT---IDQLF--ESLFSNRKGqerrlhnlansvIILDEVQayPPYMLA-LLLRLLEWLKNLGG--SVILMTATL---- 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  366 fseyfgncPMIHIPGFtFPVVEYLLEDIIEKIRYFPEQKEHRSQFKRGFMQghvnrqekeekeaiykerWPAYIKELQTR 445
Cdd:COG1203   310 --------PPLLREEL-LEAYELIPDEPEELPEYFRAFVRKRVELKEGPLS------------------DEELAELILEA 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  446 YSASTiDVLemmdddkVDLNLIAALIR-YIVLEEEDGAILVFLpgwdnistLHdllmSQVMFKsDRFLIIplhslmptvn 524
Cdd:COG1203   363 LHKGK-SVL-------VIVNTVKDAQElYEALKEKLPDEEVYL--------LH----SRFCPA-DRSEIE---------- 411

                         410       420       430
                  ....*....|....*....|....*....|....
gi 157818387  525 qTQVFKKTPPGVRKIVIATNIAETSITID-DVVY 557
Cdd:COG1203   412 -KEIKERLERGKPCILVSTQVVEAGVDIDfDVVI 444
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 192-327 2.18e-03

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: 40.81  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  192 MQRFRKKLPSyGMQKELVNLINNHQVTVISGETGCGKTTQ----VTQFILDNYI--ERGIGSACRIVCTQPRRISAI--S 263
Cdd:cd17948     5 LQRQGITKPT-TVQKQGIPSILRGRNTLCAAETGSGKTLTyllpIIQRLLRYKLlaEGPFNAPRGLVITPSRELAEQigS 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818387  264 VAERVAAE---RAESCGNGNSTGyQIRLqsrLPRKQGSILYCTTGIILQWLQSD-SRLSSVSHIVLDE 327
Cdd:cd17948    84 VAQSLTEGlglKVKVITGGRTKR-QIRN---PHFEEVDILVATPGALSKLLTSRiYSLEQLRHLVLDE 147
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 296-362 4.95e-03

DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members 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: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 39.48  E-value: 4.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157818387  296 QGSILYCTTGIILQWLQsdSRLSSVSHI---VLDE----IHERNLQSDVLMtvIKDLLhfRSDLKVILMSATLN 362
Cdd:cd17963   111 TAQIVIGTPGTVLDWLK--KRQLDLKKIkilVLDEadvmLDTQGHGDQSIR--IKRML--PRNCQILLFSATFP 178
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 538-597 9.31e-03

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The 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: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 36.14  E-value: 9.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818387  538 KIVIATNIAETSITIDDVVYVIdggkiketHFDtqnnistmsaEWVSKANAKQRKGRAGR 597
Cdd:cd18785    24 EILVATNVLGEGIDVPSLDTVI--------FFD----------PPSSAASYIQRVGRAGR 65
 
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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