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Conserved domains on  [gi|240848573|ref|NP_082412|]
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ATP-dependent DNA/RNA helicase DHX36 [Mus musculus]

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 ...
 200-379 5.15e-122

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: 369.17  E-value: 5.15e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVATERAESCGN 279
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 GNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMS 359
Cdd:cd17981    81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160

                         170       180
                  ....*....|....*....|
gi 240848573  360 ATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17981   161 ATLNAEKFSDYFNNCPMIHI 180
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
208-769 2.42e-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: 369.41  E-value: 2.42e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  208 ELVNLINNHQVTVISGETGCGKTTQVTQFILDnyieRGKGSACRIVCTQPRRISAISVAERVATERAESCGNgnSTGYQI 287
Cdd:COG1643    18 ELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE--TVGYRV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  288 RLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILMSATLNAEK 366
Cdd:COG1643    92 RFEDKV-SAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPaLRPDLKLLVMSATLDAER 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  367 FSEYFGNCPMIHIPGFTFPVveyllediiEkIRYVPDQKEHRSQfkrgfmqghvnrqekeekeaiykerwpayikelrtr 446
Cdd:COG1643   171 FARLLGDAPVIESSGRTYPV---------E-VRYRPLPADERDL------------------------------------ 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  447 ysastvdvlqmmdddkvdLNLIAALIRyIVLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDKFLIIPLHSLMPTVNQ 526
Cdd:COG1643   205 ------------------EDAVADAVR-EALAEEPGDILVFLPGEREIRRTAEALRGRL---PPDTEILPLYGRLSAAEQ 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  527 TQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYH 606
Cdd:COG1643   263 DRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYR 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  607 LYNGLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAYFlsRLMDPPS----NEAVVLsikhLMELSALDKQEELTPL 682
Cdd:COG1643   343 LWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPParaiADARAL----LQELGALDADGRLTPL 416

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  683 GVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPfviplgkekiadaRRkelaKETRSDHLTVVNAFEGWEEA 762
Cdd:COG1643   417 GRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP-------------RR----GAAGSDLLARLNLWRRLREQ 479


                  ....*..
gi 240848573  763 KRRGFRY 769
Cdd:COG1643   480 QREFLSY 486
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 824-910 4.21e-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: 4.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   824 IKAVICAGLYPKVAKiRLNLGKKRKmvkvHTKSDGLVSIHPKSVNVEQTDFHYNWLIYHLKMRTSSIYLYDCTEVSPYCL 903
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYT----TLSDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWL 75


                   ....*..
gi 240848573   904 LFFGGDI 910
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 ...
 200-379 5.15e-122

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: 369.17  E-value: 5.15e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVATERAESCGN 279
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 GNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMS 359
Cdd:cd17981    81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160

                         170       180
                  ....*....|....*....|
gi 240848573  360 ATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17981   161 ATLNAEKFSDYFNNCPMIHI 180
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
208-769 2.42e-113

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 369.41  E-value: 2.42e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  208 ELVNLINNHQVTVISGETGCGKTTQVTQFILDnyieRGKGSACRIVCTQPRRISAISVAERVATERAESCGNgnSTGYQI 287
Cdd:COG1643    18 ELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE--TVGYRV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  288 RLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILMSATLNAEK 366
Cdd:COG1643    92 RFEDKV-SAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPaLRPDLKLLVMSATLDAER 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  367 FSEYFGNCPMIHIPGFTFPVveyllediiEkIRYVPDQKEHRSQfkrgfmqghvnrqekeekeaiykerwpayikelrtr 446
Cdd:COG1643   171 FARLLGDAPVIESSGRTYPV---------E-VRYRPLPADERDL------------------------------------ 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  447 ysastvdvlqmmdddkvdLNLIAALIRyIVLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDKFLIIPLHSLMPTVNQ 526
Cdd:COG1643   205 ------------------EDAVADAVR-EALAEEPGDILVFLPGEREIRRTAEALRGRL---PPDTEILPLYGRLSAAEQ 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  527 TQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYH 606
Cdd:COG1643   263 DRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYR 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  607 LYNGLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAYFlsRLMDPPS----NEAVVLsikhLMELSALDKQEELTPL 682
Cdd:COG1643   343 LWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPParaiADARAL----LQELGALDADGRLTPL 416

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  683 GVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPfviplgkekiadaRRkelaKETRSDHLTVVNAFEGWEEA 762
Cdd:COG1643   417 GRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP-------------RR----GAAGSDLLARLNLWRRLREQ 479


                  ....*..
gi 240848573  763 KRRGFRY 769
Cdd:COG1643   480 QREFLSY 486
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 181-754 7.87e-83

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 293.12  E-value: 7.87e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  181 LQRKKTDPRYiemqRFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACRIVCTQPRRI 260
Cdd:PRK11131   58 LLREAARPEI----TYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICL----ELGRGVKGLIGHTQPRRL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  261 SAISVAERVATERAESCGNgnSTGYQIRLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLM 340
Cdd:PRK11131  130 AARTVANRIAEELETELGG--CVGYKVRFNDQV-SDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFIL 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  341 TVIKDLLHFRSDLKVILMSATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYVPdqkehrsqfkrgfMQGHV 420
Cdd:PRK11131  207 GYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPV----------EVRYRP-------------IVEEA 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  421 NRQEKEEKEAIYkerwpayikelrtrysaSTVDVLQmmdddkvdlnliaaliryivlEEEDGAILVFLPGWDNISTLHDL 500
Cdd:PRK11131  264 DDTERDQLQAIF-----------------DAVDELG---------------------REGPGDILIFMSGEREIRDTADA 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  501 LMSQVMFKSDkflIIPLHSLMPTVNQTQVFKktPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMS 580
Cdd:PRK11131  306 LNKLNLRHTE---ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLP 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  581 AEWVSKANAKQRKGRAGRVQPGHCYHLYNGL----RASLLDdyqlPEILRTPLEELCLQIKILRLGGIAYFlsRLMDPPS 656
Cdd:PRK11131  381 IEPISQASANQRKGRCGRVSEGICIRLYSEDdflsRPEFTD----PEILRTNLASVILQMTALGLGDIAAF--PFVEAPD 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  657 NEAVVLSIKHLMELSALDKQE-----ELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKE 731
Cdd:PRK11131  455 KRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQ 534

                         570       580
                  ....*....|....*....|...
gi 240848573  732 KIADARRKELAKEtRSDHLTVVN 754
Cdd:PRK11131  535 QASDEKHRRFADK-ESDFLAFVN 556
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 456-608 3.55e-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: 3.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  456 QMMDDDKVDLNLIAALIRYIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKS-DKFLIIPLHSLMPTVNQTQVFKKTP 534
Cdd:cd18791    18 SSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDlGKLLVLPLHSSLPPEEQQRVFEPPP 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240848573  535 PGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYHLY 608
Cdd:cd18791    98 PGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 200-738 1.74e-72

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: 257.00  E-value: 1.74e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKgsacrIVCTQPRRISAISVAERVATERAESCGN 279
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGGK-----IIMLEPRRLAARSAAQRLASQLGEAVGQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   280 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILM 358
Cdd:TIGR01970   76 --TVGYRVRGENKVSRRT-RLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSsLREDLKILAM 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   359 SATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYVPDQKEHRsqfkrgfMQGHVNRQekeekeaiykerwpa 438
Cdd:TIGR01970  153 SATLDGERLSSLLPDAPVVESEGRSFPV----------EIRYLPLRGDQR-------LEDAVSRA--------------- 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   439 yikelrtrysastvdVLQMmdddkvdlnliaaliryivLEEEDGAILVFLPGWDNI----STLHDLLMSQVmfksdkfLI 514
Cdd:TIGR01970  201 ---------------VEHA-------------------LASETGSILVFLPGQAEIrrvqEQLAERLDSDV-------LI 239

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   515 IPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKG 594
Cdd:TIGR01970  240 CPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAG 319

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   595 RAGRVQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQikILRLGGIAYFLSRLMDPPSNEAVVLSIKHLMELSALD 674
Cdd:TIGR01970  320 RAGRLEPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALE--LAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALD 397

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   675 KQEELTPLGVHLARLPVEPHIGKMILFG------ALFCCLDPVLT-----------IAASLSFKDPFVIPLGKEKIADAR 737
Cdd:TIGR01970  398 AQGRLTAHGKAMAALGCHPRLAAMLLSAhstglaALACDLAALLEerglprqggadLMNRLHRLQQGRQGRGQRAQQLAK 477


                   .
gi 240848573   738 R 738
Cdd:TIGR01970  478 K 478
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 663-752 1.26e-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: 1.26e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   663 SIKHLMELSALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLG------------- 729
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 240848573   730 -KEKIADARRKELAKETRSDHLTV 752
Cdd:pfam04408   81 rRAADEKARAKFARLDLEGDHLTL 104
DEXDc smart00487
DEAD-like helicases superfamily;
203-385 2.77e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.50  E-value: 2.77e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573    203 YGMQKELVN-LINNHQVTVISGETGCGKTTQVTQFILDNYIergKGSACRIVCTQPRRISAISVAERVATERAESCGN-- 279
Cdd:smart00487   10 RPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALK---RGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKvv 86

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573    280 GNSTGYQIRLQ-SRLPRKQGSILYCTTGIILQWLQSDS-RLSSVSHIVLDEIHER--NLQSDVLMTVIKDLlhfRSDLKV 355
Cdd:smart00487   87 GLYGGDSKREQlRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQL 163

                           170       180       190
                    ....*....|....*....|....*....|..
gi 240848573    356 ILMSATL--NAEKFSEYFGNCPMIHIPGFTFP 385
Cdd:smart00487  164 LLLSATPpeEIENLLELFLNDPVFIDVGFTPL 195
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 669-753 9.36e-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: 9.36e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573    669 ELSALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFviPLGKEKIADARRKELAKEtRSD 748
Cdd:smart00847    1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADP-ESD 77


                    ....*
gi 240848573    749 HLTVV 753
Cdd:smart00847   78 HLTLL 82
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 824-910 4.21e-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: 4.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   824 IKAVICAGLYPKVAKiRLNLGKKRKmvkvHTKSDGLVSIHPKSVNVEQTDFHYNWLIYHLKMRTSSIYLYDCTEVSPYCL 903
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYT----TLSDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWL 75


                   ....*..
gi 240848573   904 LFFGGDI 910
Cdd:pfam07717   76 LLFAPHI 82
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 206-365 2.81e-12

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 65.73  E-value: 2.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   206 QKELVNLINNHQVTVISGETGCGKTTqVTQF-ILDNYIERGKGSacRIVCTQPRRISAISVAERvATERAESCG------ 278
Cdd:pfam00270    4 QAEAIPAILEGRDVLVQAPTGSGKTL-AFLLpALEALDKLDNGP--QALVLAPTRELAEQIYEE-LKKLGKGLGlkvasl 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   279 -NGNSTGYQIRLQSRLPrkqgsILYCTTGIILQWLQSDSRLSSVSHIVLDEIHE--RNLQSDVLMTVIKdllHFRSDLKV 355
Cdd:pfam00270   80 lGGDSRKEQLEKLKGPD-----ILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRllDMGFGPDLEEILR---RLPKKRQI 151

                          170
                   ....*....|
gi 240848573   356 ILMSATLNAE 365
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 ...
 200-379 5.15e-122

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: 369.17  E-value: 5.15e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVATERAESCGN 279
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 GNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMS 359
Cdd:cd17981    81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160

                         170       180
                  ....*....|....*....|
gi 240848573  360 ATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17981   161 ATLNAEKFSDYFNNCPMIHI 180
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
208-769 2.42e-113

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 369.41  E-value: 2.42e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  208 ELVNLINNHQVTVISGETGCGKTTQVTQFILDnyieRGKGSACRIVCTQPRRISAISVAERVATERAESCGNgnSTGYQI 287
Cdd:COG1643    18 ELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE--TVGYRV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  288 RLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILMSATLNAEK 366
Cdd:COG1643    92 RFEDKV-SAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPaLRPDLKLLVMSATLDAER 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  367 FSEYFGNCPMIHIPGFTFPVveyllediiEkIRYVPDQKEHRSQfkrgfmqghvnrqekeekeaiykerwpayikelrtr 446
Cdd:COG1643   171 FARLLGDAPVIESSGRTYPV---------E-VRYRPLPADERDL------------------------------------ 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  447 ysastvdvlqmmdddkvdLNLIAALIRyIVLEEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDKFLIIPLHSLMPTVNQ 526
Cdd:COG1643   205 ------------------EDAVADAVR-EALAEEPGDILVFLPGEREIRRTAEALRGRL---PPDTEILPLYGRLSAAEQ 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  527 TQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYH 606
Cdd:COG1643   263 DRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYR 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  607 LYNGLRASLLDDYQLPEILRTPLEELCLQIKILRLGGIAYFlsRLMDPPS----NEAVVLsikhLMELSALDKQEELTPL 682
Cdd:COG1643   343 LWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDL--PFLDPPParaiADARAL----LQELGALDADGRLTPL 416

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  683 GVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPfviplgkekiadaRRkelaKETRSDHLTVVNAFEGWEEA 762
Cdd:COG1643   417 GRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDP-------------RR----GAAGSDLLARLNLWRRLREQ 479


                  ....*..
gi 240848573  763 KRRGFRY 769
Cdd:COG1643   480 QREFLSY 486
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 216-379 6.23e-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: 275.49  E-value: 6.23e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  216 HQVTVISGETGCGKTTQVTQFILDNYIERGKGsaCRIVCTQPRRISAISVAERVATERAESCGNgnSTGYQIRLQSRLPR 295
Cdd:cd17917     1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGK--GRIVCTQPRRIAAISVAERVAEERGEKLGE--EVGYQIRFESKTSS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  296 KqGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMSATLNAEKFSEYFGNCP 375
Cdd:cd17917    77 K-TRIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAP 155


                  ....
gi 240848573  376 MIHI 379
Cdd:cd17917   156 VIHI 159
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 181-754 7.87e-83

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 293.12  E-value: 7.87e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  181 LQRKKTDPRYiemqRFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACRIVCTQPRRI 260
Cdd:PRK11131   58 LLREAARPEI----TYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICL----ELGRGVKGLIGHTQPRRL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  261 SAISVAERVATERAESCGNgnSTGYQIRLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLM 340
Cdd:PRK11131  130 AARTVANRIAEELETELGG--CVGYKVRFNDQV-SDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFIL 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  341 TVIKDLLHFRSDLKVILMSATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYVPdqkehrsqfkrgfMQGHV 420
Cdd:PRK11131  207 GYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPV----------EVRYRP-------------IVEEA 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  421 NRQEKEEKEAIYkerwpayikelrtrysaSTVDVLQmmdddkvdlnliaaliryivlEEEDGAILVFLPGWDNISTLHDL 500
Cdd:PRK11131  264 DDTERDQLQAIF-----------------DAVDELG---------------------REGPGDILIFMSGEREIRDTADA 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  501 LMSQVMFKSDkflIIPLHSLMPTVNQTQVFKktPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMS 580
Cdd:PRK11131  306 LNKLNLRHTE---ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLP 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  581 AEWVSKANAKQRKGRAGRVQPGHCYHLYNGL----RASLLDdyqlPEILRTPLEELCLQIKILRLGGIAYFlsRLMDPPS 656
Cdd:PRK11131  381 IEPISQASANQRKGRCGRVSEGICIRLYSEDdflsRPEFTD----PEILRTNLASVILQMTALGLGDIAAF--PFVEAPD 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  657 NEAVVLSIKHLMELSALDKQE-----ELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLGKE 731
Cdd:PRK11131  455 KRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQ 534

                         570       580
                  ....*....|....*....|...
gi 240848573  732 KIADARRKELAKEtRSDHLTVVN 754
Cdd:PRK11131  535 QASDEKHRRFADK-ESDFLAFVN 556
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 456-608 3.55e-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: 3.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  456 QMMDDDKVDLNLIAALIRYIVLEEEDGAILVFLPGWDNISTLHDLLMSQVMFKS-DKFLIIPLHSLMPTVNQTQVFKKTP 534
Cdd:cd18791    18 SSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDlGKLLVLPLHSSLPPEEQQRVFEPPP 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240848573  535 PGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKGRAGRVQPGHCYHLY 608
Cdd:cd18791    98 PGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 200-738 1.74e-72

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: 257.00  E-value: 1.74e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKgsacrIVCTQPRRISAISVAERVATERAESCGN 279
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGGK-----IIMLEPRRLAARSAAQRLASQLGEAVGQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   280 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILM 358
Cdd:TIGR01970   76 --TVGYRVRGENKVSRRT-RLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSsLREDLKILAM 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   359 SATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYVPDQKEHRsqfkrgfMQGHVNRQekeekeaiykerwpa 438
Cdd:TIGR01970  153 SATLDGERLSSLLPDAPVVESEGRSFPV----------EIRYLPLRGDQR-------LEDAVSRA--------------- 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   439 yikelrtrysastvdVLQMmdddkvdlnliaaliryivLEEEDGAILVFLPGWDNI----STLHDLLMSQVmfksdkfLI 514
Cdd:TIGR01970  201 ---------------VEHA-------------------LASETGSILVFLPGQAEIrrvqEQLAERLDSDV-------LI 239

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   515 IPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKG 594
Cdd:TIGR01970  240 CPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAG 319

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   595 RAGRVQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQikILRLGGIAYFLSRLMDPPSNEAVVLSIKHLMELSALD 674
Cdd:TIGR01970  320 RAGRLEPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALE--LAQWGAKDPSDLRWLDAPPSVALAAARQLLQRLGALD 397

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   675 KQEELTPLGVHLARLPVEPHIGKMILFG------ALFCCLDPVLT-----------IAASLSFKDPFVIPLGKEKIADAR 737
Cdd:TIGR01970  398 AQGRLTAHGKAMAALGCHPRLAAMLLSAhstglaALACDLAALLEerglprqggadLMNRLHRLQQGRQGRGQRAQQLAK 477


                   .
gi 240848573   738 R 738
Cdd:TIGR01970  478 K 478
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 200-379 2.98e-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: 233.96  E-value: 2.98e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVATERAESCGN 279
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 gnSTGYQIRLQSRlpRKQGS-ILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 358
Cdd:cd17985    81 --SVGYQIRLESV--KSSATrLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILM 156

                         170       180
                  ....*....|....*....|.
gi 240848573  359 SATLNAEKFSEYFGNCPMIHI 379
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 ...
 173-379 2.50e-70

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


Pssm-ID: 350730 [Multi-domain]  Cd Length: 234  Bit Score: 233.57  E-value: 2.50e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  173 LDQHLLEDLQ-RKKTDPRYIEMQRFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACR 251
Cdd:cd17972    31 ISMDLKNELMyQREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  252 IVCTQPRRISAISVAERVATERAESCgnGNSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRlsSVSHIVLDEIHE 331
Cdd:cd17972   111 IVVTQPRRISAVSVAERVAFERGEEV--GKSCGYSVRFESVLPRPHASILFCTVGVLLRKLEAGIR--GISHVIVDEIHE 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 240848573  332 RNLQSDVLMTVIKDLLHFRSDLKVILMSATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17972   187 RDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 200-379 4.72e-67

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: 222.36  E-value: 4.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKGSACRIVCTQPRRISAISVAERVATERAESCGN 279
Cdd:cd17976     1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 gnSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMS 359
Cdd:cd17976    81 --NVGYQVRLESRPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMS 158

                         170       180
                  ....*....|....*....|
gi 240848573  360 ATLNAEKFSEYFGNCPMIHI 379
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 ...
 200-379 4.01e-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: 205.92  E-value: 4.01e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYI-ERGKGSACRIVCTQPRRISAISVAERVATERAESCG 278
Cdd:cd17975     1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLlNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  279 NG--NS-TGYQIRLQSRlPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKV 355
Cdd:cd17975    81 PGgkNSlCGYQIRMESR-TGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHL 159

                         170       180
                  ....*....|....*....|....
gi 240848573  356 ILMSATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17975   160 ILMSATVDCEKFSSYFTHCPILRI 183
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 200-379 2.16e-60

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: 203.91  E-value: 2.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIErgKGSACRIVCTQPRRISAISVAERVATERAESCGN 279
Cdd:cd17987     1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYA--NGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQS-DSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 358
Cdd:cd17987    79 --TVGYQIRLESRVSPKT-LLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILS 155

                         170       180
                  ....*....|....*....|.
gi 240848573  359 SATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17987   156 SAALDVNLFIRYFGSCPVIYI 176
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 200-703 1.41e-57

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 213.25  E-value: 1.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILdnyieRGKGSACRIVCTQPRRISAISVAERVATERAESCGN 279
Cdd:PRK11664    4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLL-----QHGGINGKIIMLEPRRLAARNVAQRLAEQLGEKPGE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 gnSTGYQIRLQSRL-PRKQGSILycTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDV----LMTVIKDLlhfRSDLK 354
Cdd:PRK11664   79 --TVGYRMRAESKVgPNTRLEVV--TEGILTRMIQRDPELSGVGLVILDEFHERSLQADLalalLLDVQQGL---RDDLK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  355 VILMSATLNAEKFSEYFGNCPMIHIPGFTFPVveyllediieKIRYVPdqkehrsqfkrgfmqghVNRQEKEEkEAIYKE 434
Cdd:PRK11664  152 LLIMSATLDNDRLQQLLPDAPVIVSEGRSFPV----------ERRYQP-----------------LPAHQRFD-EAVARA 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  435 rwpayikelrtrysastvdVLQMMDddkvdlnliaaliryivleEEDGAILVFLPGWDNISTLHDLLMSQVmfkSDKFLI 514
Cdd:PRK11664  204 -------------------TAELLR-------------------QESGSLLLFLPGVGEIQRVQEQLASRV---ASDVLL 242

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  515 IPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIDGGKIKETHFDTQNNISTMSAEWVSKANAKQRKG 594
Cdd:PRK11664  243 CPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAG 322

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  595 RAGRVQPGHCYHLYNGLRASLLDDYQLPEILRTPLEELCLQikILRLGgiAYFLSRLM--DPPSNEAVVLSIKHLMELSA 672
Cdd:PRK11664  323 RAGRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLE--LLQWG--CHDPAQLSwlDQPPAAALAAAKRLLQQLGA 398

                         490       500       510
                  ....*....|....*....|....*....|.
gi 240848573  673 LDKQEELTPLGVHLARLPVEPHIGKMILFGA 703
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 ...
 188-379 1.16e-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: 182.23  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  188 PRYIEMQRFRKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNyiERGKGSACRIVCTQPRRISAISVAE 267
Cdd:cd17973     1 QRYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDD--ELPHQPKKLVACTQPRRVAAMSVAQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  268 RVATERAESCGNgnSTGYQIRLQSRLPRKqgSIL-YCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDL 346
Cdd:cd17973    79 RVAEEMDVKLGE--EVGYSIRFEDCSSAK--TILkYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEV 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 240848573  347 LHFRSDLKVILMSATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17973   155 VRRRPDLKLIVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 200-386 5.66e-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: 5.66e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKgsACRIVCTQPRRISAISVAERVATERAesCGN 279
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGK--YCNIVVTQPRRIAAISIARRVSQERE--WTL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 GNSTGYQIRLQsRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSD-LKVILM 358
Cdd:cd17988    77 GSLVGYQVGLE-RPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILM 155

                         170       180
                  ....*....|....*....|....*...
gi 240848573  359 SATLNAEKFSEYFGncpMIHIPGFTFPV 386
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 ...
 197-380 1.06e-49

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: 173.82  E-value: 1.06e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  197 RKKLPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFIldnyIERGKGSACRIVCTQPRRISAISVAERVATERAes 276
Cdd:cd17971     3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYL----AEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFG-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  277 CGNGNSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVI 356
Cdd:cd17971    77 CCLGQEVGYTIRFEDCTSPET-VIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLI 155

                         170       180
                  ....*....|....*....|....
gi 240848573  357 LMSATLNAEKFSEYFGNCPMIHIP 380
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 ...
 200-379 1.60e-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: 169.93  E-value: 1.60e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERgkgsacrIVCTQPRRISAISVAERVATERAEScgN 279
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH-------IACTQPRRIACISLAKRVAFESLNQ--Y 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 GNSTGYQIRLQ-SRLPRKQgsILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 358
Cdd:cd17979    72 GSKVAYQIRFErTRTLATK--LLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILM 149

                         170       180
                  ....*....|....*....|.
gi 240848573  359 SATLNAEKFSEYFGNCPMIHI 379
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 ...
 200-379 1.85e-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: 166.87  E-value: 1.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFIL-DNYIERGKgsacrIVCTQPRRISAISVAERVATERAESCG 278
Cdd:cd17983     1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHeDGYTDYGM-----IGCTQPRRVAAMSVAKRVSEEMGVELG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  279 NgnSTGYQIRLQSrLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 358
Cdd:cd17983    76 E--EVGYAIRFED-CTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVT 152

                         170       180
                  ....*....|....*....|.
gi 240848573  359 SATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17983   153 SATMDADKFADFFGNVPIFTI 173
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 200-379 2.15e-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: 166.91  E-value: 2.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKGsacRIVCTQPRRISAISVAERVATERaeSCGN 279
Cdd:cd17974     1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGG---KIGCTQPRRVAAMSVAARVAEEM--GVKL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 GNSTGYQIRLQSRLPRKqgSIL-YCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 358
Cdd:cd17974    76 GNEVGYSIRFEDCTSEK--TVLkYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLIS 153

                         170       180
                  ....*....|....*....|.
gi 240848573  359 SATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17974   154 SATMDAEKFSAFFDDAPIFRI 174
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 200-379 1.61e-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: 161.75  E-value: 1.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKgsacRIVCTQPRRISAISVAERVATERaeSCGN 279
Cdd:cd17978     1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGG----MIGITQPRRVAAVSVAKRVAEEM--GVEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 GNSTGYQIRLQSRLPRkQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFR-----SDLK 354
Cdd:cd17978    75 GQLVGYSVRFDDVTSE-ETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLK 153

                         170       180
                  ....*....|....*....|....*
gi 240848573  355 VILMSATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17978   154 VIIMSATLDADLFSEYFNGAPVLYI 178
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 200-371 1.44e-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: 1.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACR-IVCTQPRRISAISVAERVATERAESCG 278
Cdd:cd17980     1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLA----EAGWTAGGRvVGCTQPRRVAAVTVAGRVAEEMGAVLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  279 NgnSTGYQIRLQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILM 358
Cdd:cd17980    77 H--EVGYCIRFDDCTDPQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVA 154

                         170
                  ....*....|...
gi 240848573  359 SATLNAEKFSEYF 371
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 ...
 200-379 2.44e-42

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


Pssm-ID: 350747 [Multi-domain]  Cd Length: 173  Bit Score: 152.22  E-value: 2.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACRIVCTQPRRISAISVAERVATERAESCGN 279
Cdd:cd17989     1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICL----ELGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVILMS 359
Cdd:cd17989    77 --AVGYKVRFTDQTSDET-CVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITS 153

                         170       180
                  ....*....|....*....|
gi 240848573  360 ATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17989   154 ATIDAERFSRHFNNAPIIEV 173
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
 200-369 8.79e-40

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


Pssm-ID: 350740 [Multi-domain]  Cd Length: 191  Bit Score: 145.57  E-value: 8.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILD-NYIERGKGSACRIVCTQPRRISAISVAERVATERAEScg 278
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEaGFGSPESDNPGMIGITQPRRVAAVSMAKRVAEELNVF-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  279 nGNSTGYQIRLQSRLpRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSD------ 352
Cdd:cd17982    79 -GKEVSYQIRYDSTV-SENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdq 156

                         170       180
                  ....*....|....*....|.
gi 240848573  353 ----LKVILMSATLNAEKFSE 369
Cdd:cd17982   157 tvkpLKLVIMSATLRVEDFTE 177
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
 200-379 6.07e-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: 142.69  E-value: 6.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILdnyiERGKGSACRIVCTQPRRISAISVAERVATERaeSCGN 279
Cdd:cd17984     1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLY----EAGFSQHGMIGVTQPRRVAAISVAQRVAEEM--KCTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 GNSTGYQIRLQSrLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRS-----DLK 354
Cdd:cd17984    75 GSKVGYQVRFDD-CSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLK 153

                         170       180
                  ....*....|....*....|....*
gi 240848573  355 VILMSATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17984   154 VVVMSATLELAKLSAFFGNCPVFDI 178
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 200-377 2.38e-33

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: 126.68  E-value: 2.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERGKgsacRIVCTQPRRISAISVAERVATERAESCGN 279
Cdd:cd17990     1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG----KIIVLEPRRVAARAAARRLATLLGEAPGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  280 gnSTGYQIRLQSRLPRKQgSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLH-FRSDLKVILM 358
Cdd:cd17990    77 --TVGYRVRGESRVGRRT-RVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAM 153

                         170
                  ....*....|....*....
gi 240848573  359 SATLNAEKFSEYFGNCPMI 377
Cdd:cd17990   154 SATLDGDGLAALLPEAPVV 172
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 663-752 1.26e-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: 1.26e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   663 SIKHLMELSALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFVIPLG------------- 729
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 240848573   730 -KEKIADARRKELAKETRSDHLTV 752
Cdd:pfam04408   81 rRAADEKARAKFARLDLEGDHLTL 104
DEXDc smart00487
DEAD-like helicases superfamily;
203-385 2.77e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.50  E-value: 2.77e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573    203 YGMQKELVN-LINNHQVTVISGETGCGKTTQVTQFILDNYIergKGSACRIVCTQPRRISAISVAERVATERAESCGN-- 279
Cdd:smart00487   10 RPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALK---RGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKvv 86

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573    280 GNSTGYQIRLQ-SRLPRKQGSILYCTTGIILQWLQSDS-RLSSVSHIVLDEIHER--NLQSDVLMTVIKDLlhfRSDLKV 355
Cdd:smart00487   87 GLYGGDSKREQlRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQL 163

                           170       180       190
                    ....*....|....*....|....*....|..
gi 240848573    356 ILMSATL--NAEKFSEYFGNCPMIHIPGFTFP 385
Cdd:smart00487  164 LLLSATPpeEIENLLELFLNDPVFIDVGFTPL 195
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 669-753 9.36e-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: 9.36e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573    669 ELSALDKQEELTPLGVHLARLPVEPHIGKMILFGALFCCLDPVLTIAASLSFKDPFviPLGKEKIADARRKELAKEtRSD 748
Cdd:smart00847    1 ELGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADP-ESD 77


                    ....*
gi 240848573    749 HLTVV 753
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 ...
 200-379 3.47e-24

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


Pssm-ID: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 100.29  E-value: 3.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKELVNLINNHQVTVISGETGCGKTTQVTQ----FILDNYIERGKgsacrIVCTQPRRISAISVAERVATERae 275
Cdd:cd17977     1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHGV-----VVCTQVHKQTAVWLALRVADEM-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  276 SCGNGNSTGYQIRLQSRLprKQGSIL-YCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLK 354
Cdd:cd17977    74 DVNIGHEVGYVIPFENCC--TNETILrYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELK 151

                         170       180
                  ....*....|....*....|....*
gi 240848573  355 VILMSATLNAEKFSEYFGNCPMIHI 379
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 ...
 200-379 3.44e-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: 91.88  E-value: 3.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  200 LPSYGMQKE-LVNLINNHQVTVISGETGCGKTTQVTQFILDNYIERG--KGSacrIVCTQPRRISAISVAERVATERAES 276
Cdd:cd17986     1 LPIWAAKFTfLEQLESPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGfqKGQ---VTVTQPHPLAARSLALRVADEMDLN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  277 CGNgnSTGYQIRlQSRLPRKQGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFRSDLKVI 356
Cdd:cd17986    78 LGH--EVGYSIP-QEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVV 154

                         170       180
                  ....*....|....*....|...
gi 240848573  357 LMSATLNAEKFSEYFGNCPMIHI 379
Cdd:cd17986   155 VVTSPALEPKLRAFWGNPPVVHV 177
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 824-910 4.21e-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: 4.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   824 IKAVICAGLYPKVAKiRLNLGKKRKmvkvHTKSDGLVSIHPKSVNVEQTDFHYNWLIYHLKMRTSSIYLYDCTEVSPYCL 903
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYT----TLSDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKVYIRTVTAISPEWL 75


                   ....*..
gi 240848573   904 LFFGGDI 910
Cdd:pfam07717   76 LLFAPHI 82
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 205-602 8.39e-17

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 85.41  E-value: 8.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  205 MQKELVNLINNHQVTVISGETGCGKTTQVTQFIL----------------DNYIERgkgsacRIVCTQPR----RISAI- 263
Cdd:PHA02653  168 VQLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLLwfnylfggfdnldkidPNFIER------PIVLSLPRvalvRLHSIt 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  264 ---SVAERVATERAESCGNGNSTGYQIRLQsrlPRKQGsILYCTTGIILqwlqsdSRLSSVSHIVLDEIHERNLQSDVLM 340
Cdd:PHA02653  242 llkSLGFDEIDGSPISLKYGSIPDELINTN---PKPYG-LVFSTHKLTL------NKLFDYGTVIIDEVHEHDQIGDIII 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  341 TVI-KDLLHFRSdlkVILMSATL--NAEKFSEYFGNCPMIHIPGFT-FPVVEylledIIEKIRYVPDQKehrsqfkrgfm 416
Cdd:PHA02653  312 AVArKHIDKIRS---LFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISE-----VYVKNKYNPKNK----------- 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  417 qghvnRQEKEEkeaiykerwpayikELRtrysastvdvlqmmdddkvdlNLIAALIRYIVLEEEDGaiLVFLPgwdNIST 496
Cdd:PHA02653  373 -----RAYIEE--------------EKK---------------------NIVTALKKYTPPKGSSG--IVFVA---SVSQ 407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  497 LHDL--LMSQvMFKSDKFLIIplHSLMPTVNQ--TQVFKKTPPgvrKIVIATNIAETSITIDDVVYVIDGGKIKETHFDT 572
Cdd:PHA02653  408 CEEYkkYLEK-RLPIYDFYII--HGKVPNIDEilEKVYSSKNP---SIIISTPYLESSVTIRNATHVYDTGRVYVPEPFG 481

                         410       420       430
                  ....*....|....*....|....*....|
gi 240848573  573 QNNIstmsaeWVSKANAKQRKGRAGRVQPG 602
Cdd:PHA02653  482 GKEM------FISKSMRTQRKGRVGRVSPG 505
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 470-599 1.51e-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: 70.70  E-value: 1.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   470 ALIRYIVLEEEDGAILVFLPGWDnistlhdLLMSQVMFKSDKFLIIPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAET 549
Cdd:pfam00271    4 EALLELLKKERGGKVLIFSQTKK-------TLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 240848573   550 SITIDDVVYVIdggkiketHFDTQNNISTMsaewvskanaKQRKGRAGRV 599
Cdd:pfam00271   77 GLDLPDVDLVI--------NYDLPWNPASY----------IQRIGRAGRA 108
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 219-361 2.47e-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: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  219 TVISGETGCGKTTQVTQFILDNYIERGKgsacRIVCTQPRRISAISVAERVATERAE--SCGnGNSTGYQIRLQSRLPRK 296
Cdd:cd00046     4 VLITAPTGSGKTLAALLAALLLLLKKGK----KVLVLVPTKALALQTAERLRELFGPgiRVA-VLVGGSSAEEREKNKLG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240848573  297 QGSILYCTTGIILQWLQSD--SRLSSVSHIVLDEIHERNLQSDV-LMTVIKDLLHFRSDLKVILMSAT 361
Cdd:cd00046    79 DADIIIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGaLILDLAVRKAGLKNAQVILLSAT 146
HELICc smart00490
helicase superfamily c-terminal domain;
506-598 1.24e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 66.85  E-value: 1.24e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573    506 MFKSDKFLIIPLHSLMPTVNQTQVFKKTPPGVRKIVIATNIAETSITIDDVVYVIdggkiketHFDTqnnistmsaeWVS 585
Cdd:smart00490    6 LLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVI--------IYDL----------PWS 67

                            90
                    ....*....|...
gi 240848573    586 KANAKQRKGRAGR 598
Cdd:smart00490   68 PASYIQRIGRAGR 80
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 206-365 2.81e-12

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 65.73  E-value: 2.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   206 QKELVNLINNHQVTVISGETGCGKTTqVTQF-ILDNYIERGKGSacRIVCTQPRRISAISVAERvATERAESCG------ 278
Cdd:pfam00270    4 QAEAIPAILEGRDVLVQAPTGSGKTL-AFLLpALEALDKLDNGP--QALVLAPTRELAEQIYEE-LKKLGKGLGlkvasl 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573   279 -NGNSTGYQIRLQSRLPrkqgsILYCTTGIILQWLQSDSRLSSVSHIVLDEIHE--RNLQSDVLMTVIKdllHFRSDLKV 355
Cdd:pfam00270   80 lGGDSRKEQLEKLKGPD-----ILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRllDMGFGPDLEEILR---RLPKKRQI 151

                          170
                   ....*....|
gi 240848573   356 ILMSATLNAE 365
Cdd:pfam00270  152 LLLSATLPRN 161
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 206-380 2.89e-08

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 54.58  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  206 QKELVNLINNHQV-TVISGETGCGKTTQVTQFILDNYIERGKgsacRIVCTQPRRisAIsVAERVA--TERAESCGN--G 280
Cdd:cd17921     6 QREALRALYLSGDsVLVSAPTSSGKTLIAELAILRALATSGG----KAVYIAPTR--AL-VNQKEAdlRERFGPLGKnvG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  281 NSTGYQIRLQSRLPRKQgsILYCTTGIILQWLQ--SDSRLSSVSHIVLDEIHERNLQS--DVLMTVIKDLLHFRSDLKVI 356
Cdd:cd17921    79 LLTGDPSVNKLLLAEAD--ILVATPEKLDLLLRngGERLIQDVRLVVVDEAHLIGDGErgVVLELLLSRLLRINKNARFV 156

                         170       180
                  ....*....|....*....|....*
gi 240848573  357 LMSATL-NAEKFSEYFGNCPMIHIP 380
Cdd:cd17921   157 GLSATLpNAEDLAEWLGVEDLIRFD 181
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 206-246 3.14e-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: 42.16  E-value: 3.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 240848573  206 QKELVNLINNHQVTVISGETGCGKTTqVTQFILDNYIERGK 246
Cdd:cd17933     2 QKAAVRLVLRNRVSVLTGGAGTGKTT-TLKALLAALEAEGK 41
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 193-416 1.10e-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: 41.58  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  193 MQRFRKKLPSyGMQKELVNLINNHQVTVISGETGCGKTTQVTQFILDNYIER-----GKGSACRIVCTQPRRISAI---S 264
Cdd:cd17948     5 LQRQGITKPT-TVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYkllaeGPFNAPRGLVITPSRELAEqigS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  265 VAERVaTE----RAESCGNGNSTGyQIRLqsrLPRKQGSILYCTTGIILQWLQSD-SRLSSVSHIVLDEihernlqSDVL 339
Cdd:cd17948    84 VAQSL-TEglglKVKVITGGRTKR-QIRN---PHFEEVDILVATPGALSKLLTSRiYSLEQLRHLVLDE-------ADTL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  340 M--TVIKDLLHFRSDLKVilmsATLNAEKFSEYFGNCPMIhIPGFTFPV-VEYLLEDII--EKIRYVPDQKEHR--SQFK 412
Cdd:cd17948   152 LddSFNEKLSHFLRRFPL----ASRRSENTDGLDPGTQLV-LVSATMPSgVGEVLSKVIdvDSIETVTSDKLHRlmPHVK 226


                  ....
gi 240848573  413 RGFM 416
Cdd:cd17948   227 QKFL 230
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
 217-361 2.03e-03

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: 39.84  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  217 QVTVISGETGCGKTTQVtqfiLDNYIERGKGSACRIVCTQPRRISAISVAERVateraescgNGNSTGYQIRLQSRLPRK 296
Cdd:cd17931     2 QLTVLDLHPGAGKTTRV----LPQIIREAIKKRLRTLVLAPTRVVAAEMYEAL---------RGLPIRYRTGAVKEEHGG 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240848573  297 QGSILYCTTGIILQWLQSDSRLSSVSHIVLDEIHERNLQSDVLMTVIKDLLHFrSDLKVILMSAT 361
Cdd:cd17931    69 NEIVDYMCHGTFTCRLLSPKRVPNYNLIIMDEAHFTDPASIAARGYIHTRVEM-GEAAVIFMTAT 132
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 297-363 4.52e-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: 4.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240848573  297 QGSILYCTTGIILQWLQsdSRLSSVSHI---VLDE----IHERNLQSDVLMtvIKDLLhfRSDLKVILMSATLN 363
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 ...
 539-598 8.45e-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: 8.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240848573  539 KIVIATNIAETSITIDDVVYVIdggkiketHFDtqnnistmsaEWVSKANAKQRKGRAGR 598
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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